RU2002104700A - Fc proteins with immunoglobulin Fc fragment to increase the immunogenicity of protein and peptide antigens - Google Patents

Fc proteins with immunoglobulin Fc fragment to increase the immunogenicity of protein and peptide antigens

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RU2002104700A
RU2002104700A RU2002104700/15A RU2002104700A RU2002104700A RU 2002104700 A RU2002104700 A RU 2002104700A RU 2002104700/15 A RU2002104700/15 A RU 2002104700/15A RU 2002104700 A RU2002104700 A RU 2002104700A RU 2002104700 A RU2002104700 A RU 2002104700A
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heavy chain
constant region
domain
adjuvant
protein
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RU2002104700/15A
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RU2248214C2 (en
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Стефен Д. Джиллиз
Кин Минг ЛО
Джон С. Джр. ВЕСОЛОВСКИ
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Лексиген Фармасьютикэлс Корп.
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Claims (45)

1. Способ повышения иммуногенности предварительно выбранного антигена у млекопитающего, включающий введение млекопитающему внутримышечно, внутривенно, через кожу или подкожно слитого белка, содержащего константную область тяжелой цепи иммуноглобулина, присоединенную полипептидной связью к предварительно выбранному антигену таким образом, чтобы вызвать иммунную реакцию на предварительно выбранный антиген, причем предварительно выбранный антиген в слитом белке вызывает более сильную иммунную реакцию у млекопитающего, чем один предварительно выбранный антиген.1. A method of increasing the immunogenicity of a pre-selected antigen in a mammal, comprising administering to the mammal, intramuscularly, intravenously, through the skin or subcutaneously, a fusion protein containing an immunoglobulin heavy chain constant region joined by a polypeptide bond to the pre-selected antigen in such a way as to elicit an immune response to the pre-selected antigen moreover, a pre-selected antigen in a fusion protein causes a stronger immune response in a mammal than one pre aritelno selected antigen. 2. Способ по п.1, отличающийся тем, что он дополнительно включает введение слитого белка в комбинации с адъювантом, количество которого достаточно для усиления иммунной реакции на предварительно выбранный антиген в слитом белке по сравнению с иммунной реакцией на предварительно выбранный антиген в слитом белке, введенный без адъюванта.2. The method according to claim 1, characterized in that it further comprises administering a fusion protein in combination with an adjuvant, the amount of which is sufficient to enhance the immune response to a preselected antigen in a fusion protein compared to an immune response to a preselected antigen in a fusion protein administered without adjuvant. 3. Способ по п.2, отличающийся тем, что слитый белок и адъювант вводят одновременно.3. The method according to claim 2, characterized in that the fusion protein and adjuvant are administered simultaneously. 4. Способ по п.2, отличающийся тем, что адъювант представляет собой слитый белок, содержащий константную область тяжелой цепи иммуноглобулина, присоединенную полипептидной связью к адъювантному белку.4. The method according to claim 2, characterized in that the adjuvant is a fusion protein containing an immunoglobulin heavy chain constant region attached by a polypeptide bond to the adjuvant protein. 5. Способ по п.1 или 4, отличающийся тем, что константная область тяжелой цепи иммуноглобулина содержит шарнирную область иммуноглобулина.5. The method according to claim 1 or 4, characterized in that the constant region of the heavy chain of the immunoglobulin contains a hinge region of the immunoglobulin. 6. Способ по п.5, отличающийся тем, что константная область тяжелой цепи иммуноглобулина содержит домен константной области тяжелой цепи иммуноглобулина, выбранный из группы, состоящей из домена СН2, домена СН3 и домена СН4.6. The method according to claim 5, characterized in that the constant region of the immunoglobulin heavy chain contains a domain of the constant region of the immunoglobulin heavy chain selected from the group consisting of CH2 domain, CH3 domain and CH4 domain. 7. Способ по п.5, отличающийся тем, что константная область тяжелой цепи иммуноглобулина содержит домен СН2 и домен СН3.7. The method according to claim 5, characterized in that the constant region of the immunoglobulin heavy chain contains a CH2 domain and a CH3 domain. 8. Способ по п.1 или 4, отличающийся тем, что константная область тяжелой цепи иммуноглобулина определена аминокислотной последовательностью, соответствующей аминокислотной последовательности, определяющей константную область тяжелой цепи иммуноглобулина, имеющуюся в организмах того же вида, к которому принадлежит млекопитающее.8. The method according to claim 1 or 4, characterized in that the constant region of the heavy chain of the immunoglobulin is determined by the amino acid sequence corresponding to the amino acid sequence that defines the constant region of the heavy chain of the immunoglobulin present in organisms of the same species to which the mammal belongs. 9. Способ по п.8, отличающийся тем, что аминокислотная последовательность, определяющая константную область тяжелой цепи иммуноглобулина, соответствует константной области тяжелой цепи иммуноглобулина человека.9. The method according to claim 8, characterized in that the amino acid sequence that defines the constant region of the heavy chain of the immunoglobulin corresponds to the constant region of the heavy chain of the human immunoglobulin. 10. Способ по п.1, отличающийся тем, что предварительно выбранный антиген выбран из группы, состоящей из простато-специфичного мембранного антигена, эктодомена рецептора цитокина, вирусного белка и опухоле специфичного белка.10. The method according to claim 1, characterized in that the pre-selected antigen is selected from the group consisting of a prostate-specific membrane antigen, an ectodomain of a cytokine receptor, a viral protein and a tumor of a specific protein. 11. Способ по п.4, отличающийся тем, что адъювантный белок является цитокином.11. The method according to claim 4, characterized in that the adjuvant protein is a cytokine. 12. Способ по п.11, отличающийся тем, что цитокин определен аминокислотной последовательностью, соответствующей аминокислотной последовательности, определяющей цитокин, имеющийся в организмах того же вида, к которому принадлежит млекопитающее.12. The method according to claim 11, characterized in that the cytokine is determined by the amino acid sequence corresponding to the amino acid sequence that defines the cytokine present in organisms of the same species to which the mammal belongs. 13. Способ по п.12, отличающийся тем, что цитокин является человеческим цитокином.13. The method according to p. 12, characterized in that the cytokine is a human cytokine. 14. Способ по п.1, отличающийся тем, что млекопитающее является человеком.14. The method according to claim 1, characterized in that the mammal is a human. 15. Композиция, предназначенная для того, чтобы вызвать у млекопитающего иммунную реакцию на предварительно выбранный антиген, отличающаяся тем, что представляет собой смесь для внутримышечного, внутривенного, трансдермального или подкожного введения, выбранную из группы, состоящей из (a) антигенного слитого белка, содержащего константную область тяжелой цепи иммуноглобулина, присоединенную полипептидной связью к предварительно выбранному антигену, и смешанного с адъювантом, и (b) предварительно выбранного антигена, смешанного с адъювантным слитым белком, содержащим константную область тяжелой цепи иммуноглобулина, присоединенную полипептидной связью к адъювантному белку.15. A composition intended to induce an immune response in a mammal to a preselected antigen, characterized in that it is a mixture for intramuscular, intravenous, transdermal or subcutaneous administration selected from the group consisting of (a) an antigenic fusion protein containing an immunoglobulin heavy chain constant region attached by a polypeptide bond to a preselected antigen and mixed with an adjuvant; and (b) a preselected antigen mixed with an adjuvant tnym fusion protein comprising a constant region of an immunoglobulin heavy chain fused polypeptide bond to an adjuvant protein. 16. Композиция по п.15, отличающаяся тем, что адъювант, указанный в подпункте (а), включает слитый белок, содержащий константную область тяжелой цепи иммуноглобулина, присоединенную полипептидной связью к адъювантному белку.16. The composition according to p. 15, wherein the adjuvant referred to in subparagraph (a) includes a fusion protein containing an immunoglobulin heavy chain constant region attached by a polypeptide bond to an adjuvant protein. 17. Композиция по п.15, отличающаяся тем, что предварительно выбранный антиген, указанный в подпункте (b), присоединен полипептидной связью к константной области тяжелой цепи иммуноглобулина.17. The composition according to p. 15, characterized in that the pre-selected antigen specified in subparagraph (b) is attached by a polypeptide bond to the constant region of the immunoglobulin heavy chain. 18. Композиция по п.15, 16 или 17, отличающаяся тем, что константная область тяжелой цепи иммуноглобулина содержит шарнирную область иммуноглобулина.18. The composition according to p. 15, 16 or 17, characterized in that the constant region of the heavy chain of the immunoglobulin contains a hinge region of the immunoglobulin. 19. Композиция по п.18, отличающаяся тем, что константная область тяжелой цепи иммуноглобулина содержит домен константной области тяжелой цепи иммуноглобулина, выбранный из группы, состоящей из домена СН2, домена СН3 и домена СН4.19. The composition according to p. 18, characterized in that the constant region of the immunoglobulin heavy chain contains a domain of the constant region of the immunoglobulin heavy chain selected from the group consisting of CH2 domain, CH3 domain and CH4 domain. 20. Композиция по п.18, отличающаяся тем, что константная область тяжелой цепи иммуноглобулина содержит домен СН2 и домен СН3.20. The composition according to p. 18, characterized in that the constant region of the immunoglobulin heavy chain contains a CH2 domain and a CH3 domain. 21. Композиция по п.15, отличающаяся тем, что адъювант, указанный в подпункте (а), содержит олигонуклеотидную последовательность CpG.21. The composition according to p. 15, characterized in that the adjuvant specified in subparagraph (a) contains the CpG oligonucleotide sequence. 22. Композиция по п.15, отличающаяся тем, что предварительно выбранный антиген выбран из группы, состоящей из простато-специфичного мембранного антигена, эктодомена рецептора цитокина, вирусного белка и опухоле-специфичного белка.22. The composition according to p. 15, wherein the pre-selected antigen is selected from the group consisting of a prostate-specific membrane antigen, an ectodomain of a cytokine receptor, a viral protein and a tumor-specific protein. 23. Композиция по п.15, отличающаяся тем, что предварительно выбранный антиген, указанный в подпункте (а), или адъювантный слитый белок, указанный в подпункте (b), соединен дисульфидной связью со второй константной областью тяжелой цепи иммуноглобулина.23. The composition according to p. 15, characterized in that the pre-selected antigen specified in subparagraph (a), or the adjuvant fusion protein specified in subparagraph (b), is connected by a disulfide bond to the second constant region of the immunoglobulin heavy chain. 24. Композиция по п.15, отличающаяся тем, что адъювант, указанный в подпункте (а), или адъювантный белок, указанный в подпункте (b), является цитокином.24. The composition according to p. 15, wherein the adjuvant specified in subparagraph (a), or the adjuvant protein indicated in subparagraph (b), is a cytokine. 25. Композиция по п.24, отличающаяся тем, что цитокин является человеческим цитокином.25. The composition according to paragraph 24, wherein the cytokine is a human cytokine. 26. Композиция по п.15, 16 или 17, отличающаяся тем, что константная область тяжелой цепи иммуноглобулина определена аминокислотной последовательностью, соответствующей аминокислотной последовательности, определяющей константную область тяжелой цепи иммуноглобулина человека.26. The composition according to p. 15, 16 or 17, characterized in that the constant region of the heavy chain of the immunoglobulin is determined by the amino acid sequence corresponding to the amino acid sequence that defines the constant region of the heavy chain of a human immunoglobulin. 27. Способ повышения иммуногенности предварительно выбранного антигена у млекопитающего, включающий введение млекопитающему последовательности нуклеиновой кислоты, кодирующей слитый белок, содержащий константную область тяжелой цепи иммуноглобулина, присоединенную к предварительно выбранному антигену, вследствие чего экспрессия последовательности нуклеиновой кислоты у млекопитающего приводит к продуцированию слитого белка, предварительно выбранный антиген которого вызывает более сильную иммунную реакцию, чем предварительно выбранный антиген, экспрессированный по нуклеиновой кислоте, кодирующей только предварительно выбранный антиген.27. A method of increasing the immunogenicity of a preselected antigen in a mammal, comprising administering to the mammal a nucleic acid sequence encoding a fusion protein containing an immunoglobulin heavy chain constant region attached to a preselected antigen, whereby expression of the nucleic acid sequence in a mammal leads to the production of a fusion protein previously the selected antigen of which causes a stronger immune response than previously you ranny antigen expressed by a nucleic acid encoding the preselected antigen alone. 28. Способ по п.27, отличающийся тем, что нуклеиновая кислота кодирует в направлении от 5’ к 3’ константную область тяжелой цепи иммуноглобулина и предварительно выбранный антиген.28. The method according to item 27, wherein the nucleic acid encodes in the direction from 5 ’to 3’ the constant region of the immunoglobulin heavy chain and the pre-selected antigen. 29. Способ по п.28, отличающийся тем, что константная область тяжелой цепи иммуноглобулина содержит шарнирную область иммуноглобулина.29. The method according to p, characterized in that the constant region of the heavy chain of the immunoglobulin contains a hinge region of the immunoglobulin. 30. Способ по п.27 или 29, отличающийся тем, что константная область тяжелой цепи иммуноглобулина содержит домен тяжелой цепи иммуноглобулина, выбранный из группы, состоящей из домена СН2, домена СН3 и домена СН4.30. The method according to item 27 or 29, characterized in that the constant region of the immunoglobulin heavy chain contains an immunoglobulin heavy chain domain selected from the group consisting of CH2 domain, CH3 domain and CH4 domain. 31. Способ по п.29, отличающийся тем, что константная область тяжелой цепи иммуноглобулина содержит домен СН2 и домен СН3.31. The method according to clause 29, wherein the constant region of the immunoglobulin heavy chain contains a CH2 domain and a CH3 domain. 32. Способ по п.27, отличающийся тем, что предварительно выбранный антиген выбран из группы, состоящей из простато-специфичного мембранного антигена, эктодомена рецептора цитокина, вирусного белка и опухоле-специфичного белка.32. The method according to item 27, wherein the pre-selected antigen is selected from the group consisting of a prostate-specific membrane antigen, an ectodomain of a cytokine receptor, a viral protein and a tumor-specific protein. 33. Способ по п.27, отличающийся тем, что он дополнительно включает введение последовательности нуклеиновой кислоты в комбинации с адъювантом.33. The method according to item 27, wherein it further includes the introduction of a nucleic acid sequence in combination with an adjuvant. 34. Способ по п.33, отличающийся тем, что адъювант представляет собой последовательность нуклеиновой кислоты, кодирующую слитый белок, содержащий константную область тяжелой цепи иммуноглобулина, присоединенную к адъювантному белку.34. The method according to p, characterized in that the adjuvant is a nucleic acid sequence encoding a fusion protein containing an immunoglobulin heavy chain constant region attached to an adjuvant protein. 35. Композиция, предназначенная для того, чтобы вызвать у млекопитающего иммунную реакцию на предварительно выбранный антиген, содержащая (a) первую последовательность нуклеиновой кислоты, кодирующую слитый белок, содержащий константную область тяжелой цепи иммуноглобулина и предварительно выбранный антиген, вследствие чего экспрессия последовательности нуклеиновой кислоты у млекопитающего приводит к продуцированию слитого белка, предварительно выбранный антиген которого вызывает более сильную иммунную реакцию, чем предварительно выбранный антиген, экспрессированный по нуклеиновой кислоте, кодирующей только предварительно выбранный антиген, и (b) адъювант.35. The composition is designed to induce an immune response in a mammal to a preselected antigen containing (a) a first nucleic acid sequence encoding a fusion protein containing an immunoglobulin heavy chain constant region and a preselected antigen, whereby expression of a nucleic acid sequence in of a mammal leads to the production of a fusion protein, the pre-selected antigen of which causes a stronger immune response than previously a selected antigen expressed by a nucleic acid encoding only the preselected antigen; and (b) an adjuvant. 36. Композиция по п.35, отличающаяся тем, что адъювант включает вторую последовательность нуклеиновой кислоты, кодирующую слитый белок, содержащий константную область тяжелой цепи иммуноглобулина, присоединенную пептидной связью к адъювантному белку.36. The composition according to p, characterized in that the adjuvant comprises a second nucleic acid sequence encoding a fusion protein containing an immunoglobulin heavy chain constant region attached by a peptide bond to the adjuvant protein. 37. Композиция по п.35 или 36, отличающаяся тем, что константная область тяжелой цепи иммуноглобулина содержит шарнирную область иммуноглобулина.37. The composition according to p. 35 or 36, characterized in that the constant region of the heavy chain of the immunoglobulin contains a hinge region of the immunoglobulin. 38. Композиция по п.35 или 36, отличающаяся тем, что константная область тяжелой цепи иммуноглобулина содержит домен тяжелой цепи иммуноглобулина, выбранный из группы, состоящей из домена СН2, домена СН3 и домена СН4.38. The composition according to p. 35 or 36, characterized in that the constant region of the immunoglobulin heavy chain contains an immunoglobulin heavy chain domain selected from the group consisting of CH2 domain, CH3 domain and CH4 domain. 39. Композиция по п.37, отличающаяся тем, что константная область тяжелой цепи иммуноглобулина содержит домен тяжелой цепи иммуноглобулина, выбранный из группы, состоящей из домена СН2, домена СН3 и домена СН4.39. The composition according to clause 37, wherein the constant region of the immunoglobulin heavy chain contains an immunoglobulin heavy chain domain selected from the group consisting of CH2 domain, CH3 domain and CH4 domain. 40. Композиция по п.35, отличающаяся тем, что предварительно выбранный антиген выбран из группы, состоящей из простато-специфичного мембранного антигена, эктодомена рецептора цитокина, вирусного белка и опухоле-специфичного белка.40. The composition according to p, characterized in that the pre-selected antigen is selected from the group consisting of a prostate-specific membrane antigen, an ectodomain of a cytokine receptor, a viral protein and a tumor-specific protein. 41. Композиция по п.36, отличающаяся тем, что адъювантный белок является цитокином.41. The composition according to p, characterized in that the adjuvant protein is a cytokine. 42. Композиция по п.35, отличающаяся тем, что первая последовательность нуклеиновой кислоты функционально размещена в способном к репликации экспрессирующем векторе.42. The composition according to p, characterized in that the first nucleic acid sequence is functionally located in a replicable expression vector. 43. Композиция по п.36, отличающаяся тем, что вторая последовательность нуклеиновой кислоты функционально размещена в способном к репликации экспрессирующем векторе.43. The composition according to clause 36, wherein the second nucleic acid sequence is functionally located in a replicable expression vector. 44. Способ повышения иммуногенности предварительно выбранного антигена у млекопитающего, включающий введение млекопитающему, одновременно или последовательно, первого слитого белка, содержащего антигенный белок с локализующим белком, и второго слитого белка, содержащего адъювантный белок и указанный локализующий белок, причем указанный локализующий белок приводит к повышению концентрации указанных первого и второго слитых белков в участке млекопитающего, доступном для иммунной системы.44. A method of increasing the immunogenicity of a pre-selected antigen in a mammal, comprising administering to the mammal, simultaneously or sequentially, a first fusion protein containing an antigenic protein with a localizing protein, and a second fusion protein containing an adjuvant protein and said localizing protein, wherein said localizing protein increases the concentration of said first and second fusion proteins in a portion of a mammal accessible to the immune system. 45. Способ повышения иммуногенности предварительно выбранного антигена у млекопитающего, включающий введение млекопитающему слитого белка, содержащего антигенный белок, адъювантный белок и локализующий белок, причем указанный локализующий белок приводит к повышению концентрации указанных антигенного и адъювантного белков в участке млекопитающего, доступном для иммунной системы.45. A method of increasing the immunogenicity of a preselected antigen in a mammal, comprising administering to the mammal a fusion protein containing an antigenic protein, an adjuvant protein and a localizing protein, said localizing protein leading to an increase in the concentration of said antigenic and adjuvant proteins in a portion of the mammal accessible to the immune system.
RU2002104700/15A 1999-07-21 2000-07-21 Fused proteins with immunoglobulin fc-fragment for enhancing immunogenicity of protein and peptide antigens RU2248214C2 (en)

Applications Claiming Priority (2)

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Families Citing this family (115)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
SK782002A3 (en) 1999-07-21 2003-08-05 Lexigen Pharm Corp FC fusion proteins for enhancing the immunogenicity of protein and peptide antigens
ATE336514T1 (en) 2000-02-11 2006-09-15 Merck Patent Gmbh INCREASE THE CIRCULATION HALF-LIFE OF ANTIBODIES-BASED FUSION PROTEINS
GB0102145D0 (en) 2001-01-26 2001-03-14 Scancell Ltd Substances
EP1363931A4 (en) * 2001-02-01 2004-04-07 Tanox Inc Methods to generate and identify monoclonal antibodies to a large number of human antigens
KR20090010127A (en) 2001-03-07 2009-01-28 메르크 파텐트 게엠베하 Expression technology for proteins containing a hybrid isotype antibody moiety
WO2002079415A2 (en) 2001-03-30 2002-10-10 Lexigen Pharmaceuticals Corp. Reducing the immunogenicity of fusion proteins
DK1383785T3 (en) 2001-05-03 2011-05-23 Merck Patent Gmbh Recombinant tumor-specific antibody and its use
KR100976743B1 (en) * 2001-05-24 2010-08-19 지모제넥틱스, 인코포레이티드 Taci-immunoglobulin fusion proteins
ATE542137T1 (en) 2001-12-04 2012-02-15 Merck Patent Gmbh IMMUNOCYTOKINE WITH MODULATED SELECTIVITY
DE10160248A1 (en) * 2001-12-07 2003-06-26 Alexander Cherkasky New fusion protein, useful for treating e.g. tumors, viral infections and autoimmune disease, comprises an Fc antibody region and at least one other domain and improves the response of antigen-presenting cells
US8025873B2 (en) * 2002-06-20 2011-09-27 Paladin Labs, Inc. Chimeric antigens for eliciting an immune response
US8029803B2 (en) 2002-06-20 2011-10-04 Paladin Labs, Inc. Chimeric antigens for eliciting an immune response
CN1315536C (en) * 2002-09-13 2007-05-16 李进 Novel vaccine of tumor antigen, its preparation method and vaccine composition
TWI353991B (en) 2003-05-06 2011-12-11 Syntonix Pharmaceuticals Inc Immunoglobulin chimeric monomer-dimer hybrids
US8007805B2 (en) 2003-08-08 2011-08-30 Paladin Labs, Inc. Chimeric antigens for breaking host tolerance to foreign antigens
US20050069521A1 (en) * 2003-08-28 2005-03-31 Emd Lexigen Research Center Corp. Enhancing the circulating half-life of interleukin-2 proteins
AU2004308952A1 (en) * 2003-12-23 2005-07-14 Centocor, Inc. Anti-retroviral agents, compositions, methods and uses
DE602004013372T2 (en) 2003-12-30 2009-07-02 Merck Patent Gmbh IL-7 FUSION PROTEINS WITH ANTIBODY PORTIONS, THEIR PREPARATION AND THEIR USE
AU2005203962C1 (en) 2004-01-05 2012-11-08 Antisoma Research Limited Interleukin-12 targeted to oncofoetal fibronectin
US7670595B2 (en) * 2004-06-28 2010-03-02 Merck Patent Gmbh Fc-interferon-beta fusion proteins
CN101072793B (en) * 2004-12-09 2012-06-20 默克专利有限公司 Il-7 variants with reduced immunogenicity
DK3050963T3 (en) 2005-03-31 2019-12-09 Chugai Pharmaceutical Co Ltd Process for producing polypeptide by arrangement control
US7566456B2 (en) * 2005-06-23 2009-07-28 Haiming Chen Allergen vaccine proteins for the treatment and prevention of allergic diseases
US20070104689A1 (en) * 2005-09-27 2007-05-10 Merck Patent Gmbh Compositions and methods for treating tumors presenting survivin antigens
JP2009511024A (en) * 2005-10-13 2009-03-19 ヴィレックス メディカル コーポレイション Chimeric antigen comprising hepatitis C virus polypeptide and Fc fragment for inducing immune response
PT1966238E (en) 2005-12-30 2012-07-31 Merck Patent Gmbh Interleukin-12p40 variants with improved stability
KR101397290B1 (en) * 2005-12-30 2014-05-21 메르크 파텐트 게엠베하 Anti-cd19 antibodies with reduced immunogenicity
DK1966244T3 (en) 2005-12-30 2012-04-23 Merck Patent Gmbh ANTI-IL-6 ANTIBODIES PREVENTING THE BINDING OF IL-6 COMPOSITION OF IL-6RALFA TO GP130
EP3345616A1 (en) 2006-03-31 2018-07-11 Chugai Seiyaku Kabushiki Kaisha Antibody modification method for purifying bispecific antibody
US11046784B2 (en) * 2006-03-31 2021-06-29 Chugai Seiyaku Kabushiki Kaisha Methods for controlling blood pharmacokinetics of antibodies
WO2008122039A2 (en) 2007-04-02 2008-10-09 The Government Of The United States Of America, As Represented By The Secretary, Department Of Health And Human Services Selenocysteine mediated hybrid antibody molecules
WO2009041621A1 (en) 2007-09-26 2009-04-02 Chugai Seiyaku Kabushiki Kaisha Anti-il-6 receptor antibody
CA2700394C (en) 2007-09-26 2017-10-24 Chugai Seiyaku Kabushiki Kaisha Modified antibody constant region
MX369784B (en) 2007-09-26 2019-11-21 Chugai Pharmaceutical Co Ltd Method of modifying isoelectric point of antibody via amino acid substitution in cdr.
AU2008332271C1 (en) 2007-12-05 2014-04-24 Chugai Seiyaku Kabushiki Kaisha Anti-NR10 antibody and use thereof
CN107551270A (en) 2008-04-11 2018-01-09 中外制药株式会社 The antigen binding molecules combined repeatedly with the antigen of multiple molecules
US8383767B2 (en) * 2008-06-27 2013-02-26 Academia Sinica Immunogenic protein carrier containing an antigen presenting cell binding domain and a cysteine-rich domain
TWI440469B (en) 2008-09-26 2014-06-11 Chugai Pharmaceutical Co Ltd Improved antibody molecules
WO2010107110A1 (en) 2009-03-19 2010-09-23 中外製薬株式会社 Antibody constant region variant
TWI646193B (en) 2009-03-19 2019-01-01 中外製藥股份有限公司 Antibody constant region alteration
EA201171259A1 (en) 2009-04-22 2012-05-30 Мерк Патент Гмбх ANTIBODY HYBRID PROTEINS WITH MODIFIED FCRN BINDING SITES
CA2761891A1 (en) 2009-05-15 2010-11-18 Chugai Seiyaku Kabushiki Kaisha Anti-axl antibody
EA017172B1 (en) * 2009-08-04 2012-10-30 Государственное Учреждение "Республиканский Научно-Практический Центр Трансфузиологии И Медицинских Биотехнологий" Method for producing isoimmune blood plasma
US10150808B2 (en) 2009-09-24 2018-12-11 Chugai Seiyaku Kabushiki Kaisha Modified antibody constant regions
GB0922209D0 (en) 2009-12-18 2010-02-03 Univ Nottingham Proteins, nucleic acid molecules and compositions
WO2011108714A1 (en) 2010-03-04 2011-09-09 中外製薬株式会社 Antibody constant region variant
CN103596587B (en) * 2010-10-28 2016-09-07 健康和人类服务部秘书长代表的美利坚合众国政府 Filovirus fusion protein and application thereof
RU2620071C2 (en) 2010-11-17 2017-05-22 Чугаи Сеияку Кабушики Каиша Multispecific antigen-binding molecule with alternate function to blood coagulation factor viii function
RU2658504C9 (en) 2010-11-30 2018-08-21 Чугаи Сейяку Кабусики Кайся Antigen-binding molecule, that is capable of multiple binding with a lot of antigenic molecules
KR20230005405A (en) 2011-02-25 2023-01-09 추가이 세이야쿠 가부시키가이샤 FcγRIIb-specific Fc antibody
CN102212139A (en) * 2011-03-29 2011-10-12 中国人民解放军第二军医大学 Fusion protein of tick-borne encephalitis virus envelop E protein and human antibody Fc fragment, and application thereof
EP2762493B1 (en) 2011-09-30 2021-06-09 Chugai Seiyaku Kabushiki Kaisha Antigen-binding molecule promoting disappearance of antigens having plurality of biological activities
TW201817744A (en) 2011-09-30 2018-05-16 日商中外製藥股份有限公司 Therapeutic antigen-binding molecule with a FcRn-binding domain that promotes antigen clearance
AR091902A1 (en) * 2012-07-25 2015-03-11 Hanmi Pharm Ind Co Ltd LIQUID FORMULATION OF A PROLONGED INSULIN CONJUGATE
MY187936A (en) * 2013-03-15 2021-10-29 In3Bio Ltd Self-assembling synthetic proteins
CN103212069B (en) * 2013-05-13 2014-07-30 上海赛伦生物技术有限公司 Immunologic adjuvant capable of improving antibody titer as well as preparation method and applications thereof
WO2014200018A1 (en) 2013-06-11 2014-12-18 独立行政法人 国立精神・神経医療研究センター Method for predicting post-therapy prognosis of relapsing-remitting multiple sclerosis (rrms) patient, and method for determining applicability of novel therapy
US20150004161A1 (en) * 2013-07-01 2015-01-01 University Of Maryland Fc Coupled Compositions and Methods of Their Use
ES2871418T3 (en) * 2013-08-28 2021-10-28 Abbvie Stemcentrx Llc Compositions and methods of conjugation of site-specific antibodies
US11124576B2 (en) 2013-09-27 2021-09-21 Chungai Seiyaku Kabushiki Kaisha Method for producing polypeptide heteromultimer
GB201403775D0 (en) 2014-03-04 2014-04-16 Kymab Ltd Antibodies, uses & methods
US9738702B2 (en) 2014-03-14 2017-08-22 Janssen Biotech, Inc. Antibodies with improved half-life in ferrets
SI3482766T1 (en) 2014-08-11 2020-09-30 Delinia, Inc. Modified il-2 variants that selectively activate regulatory t cells for the treatment of autoimmune diseases
MA40764A (en) 2014-09-26 2017-08-01 Chugai Pharmaceutical Co Ltd THERAPEUTIC AGENT INDUCING CYTOTOXICITY
TW201627318A (en) * 2014-10-22 2016-08-01 臺北醫學大學 A CETP antigenic peptide and fusion protein and their composition and applications
TWI808330B (en) 2014-12-19 2023-07-11 日商中外製藥股份有限公司 ANTI-MYOSTATIN ANTIBODIES, POLYPEPTIDES CONTAINING VARIANT Fc REGIONs, AND METHODS OF USE
TW201809008A (en) 2014-12-19 2018-03-16 日商中外製藥股份有限公司 Anti-C5 antibodies and methods of use
SG10201907215QA (en) 2015-02-05 2019-09-27 Chugai Pharmaceutical Co Ltd Antibodies Comprising An Ion Concentration Dependent Antigen-Binding Domain, Fc Region Variants, Il-8-Binding Antibodies, And Uses Therof
TWI805046B (en) 2015-02-27 2023-06-11 日商中外製藥股份有限公司 Use of IL-6 receptor antibody for preparing pharmaceutical composition
EP3279216A4 (en) 2015-04-01 2019-06-19 Chugai Seiyaku Kabushiki Kaisha Method for producing polypeptide hetero-oligomer
MA42059A (en) 2015-05-06 2018-03-14 Janssen Biotech Inc PROSTATE-SPECIFIC MEMBRANE ANTIGEN (PSMA) BISPECIFIC BINDING AGENTS AND USES
US10697883B2 (en) 2015-05-19 2020-06-30 National Center Of Neurology And Psychiatry Method for determining application of therapy to multiple sclerosis (MS) patient
WO2016199904A1 (en) * 2015-06-10 2016-12-15 国立大学法人東京大学 Adjuvant for vaccines, vaccine, and immunity induction method
JP7141336B2 (en) 2015-12-25 2022-09-22 中外製薬株式会社 Anti-myostatin antibodies and methods of use
CA3004288A1 (en) 2015-12-28 2017-07-06 Nobuyuki Tanaka Method for promoting efficiency of purification of fc region-containing polypeptide
US20170204154A1 (en) 2016-01-20 2017-07-20 Delinia, Inc. Molecules that selectively activate regulatory t cells for the treatment of autoimmune diseases
CA3016424A1 (en) 2016-03-14 2017-09-21 Chugai Seiyaku Kabushiki Kaisha Cell injury inducing therapeutic drug for use in cancer therapy
US9567399B1 (en) 2016-06-20 2017-02-14 Kymab Limited Antibodies and immunocytokines
CN106177932A (en) * 2016-07-03 2016-12-07 查文娟 A kind of vaccine of methicillin-resistant staphylococcus aureus
SG11201801024XA (en) 2016-08-05 2018-05-30 Chugai Pharmaceutical Co Ltd Therapeutic or preventive compositions for il-8-related diseases
SG10201607778XA (en) 2016-09-16 2018-04-27 Chugai Pharmaceutical Co Ltd Anti-Dengue Virus Antibodies, Polypeptides Containing Variant Fc Regions, And Methods Of Use
WO2018083248A1 (en) 2016-11-03 2018-05-11 Kymab Limited Antibodies, combinations comprising antibodies, biomarkers, uses & methods
KR20190083656A (en) 2016-11-08 2019-07-12 데리니아, 인크. IL-2 variants for the treatment of autoimmune diseases
US11129906B1 (en) 2016-12-07 2021-09-28 David Gordon Bermudes Chimeric protein toxins for expression by therapeutic bacteria
US11851486B2 (en) 2017-05-02 2023-12-26 National Center Of Neurology And Psychiatry Method for predicting and evaluating therapeutic effect in diseases related to IL-6 and neutrophils
JP7235249B2 (en) 2017-10-20 2023-03-08 学校法人兵庫医科大学 Pharmaceutical composition for suppressing postoperative adhesion containing anti-IL-6 receptor antibody
US11319355B2 (en) 2017-12-19 2022-05-03 Xencor, Inc. Engineered IL-2 Fc fusion proteins
CN110028588A (en) * 2018-01-11 2019-07-19 上海细胞治疗研究院 Antigen-Fc fusion protein and its application for detecting positive CAR-T cell
US11512127B2 (en) * 2018-02-14 2022-11-29 Viela Bio, Inc. Antibodies to Feline McDonough Sarcoma (FMS)-like tyrosine kinase 3 receptor ligand (FLT3L) and uses thereof for treating autoimmune and inflammatory diseases
TWI827585B (en) 2018-03-15 2024-01-01 日商中外製藥股份有限公司 Anti-dengue virus antibodies having cross-reactivity to zika virus and methods of use
US11696948B2 (en) 2018-06-12 2023-07-11 Kbio Holdings Limited Vaccines formed by virus and antigen conjugation
SG11202012366WA (en) 2018-06-12 2021-01-28 Kentucky Bioprocessing Inc Virus and antigen purification and conjugation
US11690907B2 (en) 2018-06-12 2023-07-04 Kbio Holdings Limited Vaccines formed by virus and antigen conjugation
US11529413B2 (en) 2018-06-12 2022-12-20 Kbio Holdings Limited Virus and antigen purification and conjugation
BR112020026112A2 (en) * 2018-06-21 2021-04-06 Shattuck Labs, Inc. HETERODIMERIC PROTEINS AND USES OF THE SAME
EP3843755A4 (en) * 2018-08-29 2022-08-31 Shattuck Labs, Inc. Flt3l-based chimeric proteins
EP4321530A3 (en) 2018-09-27 2024-05-22 Xilio Development, Inc. Masked cytokine polypeptides
JP2022503959A (en) 2018-10-03 2022-01-12 ゼンコア インコーポレイテッド IL-12 heterodimer FC-fusion protein
WO2020118605A1 (en) * 2018-12-13 2020-06-18 丁邦 ANTIBODY-TUMOR NECROSIS FACTOR-α FUSION PROTEIN, PREPARATION METHOD THEREFOR AND USES THEREOF
US12006345B2 (en) 2019-02-21 2024-06-11 Xencor, Inc. Untargeted and targeted IL-10 Fc-fusion proteins
JP2022529892A (en) * 2019-03-28 2022-06-27 オリオニス バイオサイエンシズ,インコーポレイテッド Chimeric protein and chimeric protein complex for FMS-like tyrosine kinase 3 (FLT3)
CN114080397A (en) 2019-05-17 2022-02-22 Xencor股份有限公司 IL-7-FC fusion proteins
EP4037700A2 (en) 2019-10-03 2022-08-10 Xencor, Inc. Targeted il-12 heterodimeric fc-fusion proteins
CN114945586A (en) * 2020-01-21 2022-08-26 张晋宇 Pharmaceutical composition and application thereof
WO2021172971A1 (en) * 2020-02-28 2021-09-02 (주)셀트리온 Varicella zoster virus fusion protein and immunogenic composition comprising same
AU2021245922A1 (en) * 2020-04-01 2022-10-13 Xilio Development, Inc. Masked IL-2 cytokines and their cleavage products
JP2023523716A (en) * 2020-04-21 2023-06-07 クビオ・ホールディングス・リミテッド Vaccine formed by conjugation of virus and antigen
CN113876938B (en) * 2020-07-01 2024-04-19 中国科学院生物物理研究所 Construction and application of fusion protein vaccine platform
TWI815194B (en) 2020-10-22 2023-09-11 美商基利科學股份有限公司 INTERLEUKIN-2-Fc FUSION PROTEINS AND METHODS OF USE
MX2023007607A (en) * 2020-12-23 2023-07-11 Immunowake Inc Immunocytokines and uses thereof.
EP4301404A1 (en) * 2021-03-04 2024-01-10 Helix Nanotechnologies, Inc. Compositions including sbi adjuvants and methods of use thereof
WO2023125976A1 (en) * 2021-12-31 2023-07-06 广州国家实验室 Fusion protein vaccine
WO2023178169A2 (en) * 2022-03-15 2023-09-21 Anemoi Biotech Holdings, Inc. Compositions and methods for treating the pathophysiology of severe viral infection
WO2023224914A1 (en) * 2022-05-16 2023-11-23 Mayo Foundation For Medical Education And Research Assessing and treating caveolinopathy diseases
CN114699521B (en) * 2022-06-07 2023-02-24 中国人民解放军军事科学院军事医学研究院 Immunity adjuvant based on metallothionein family and application thereof

Family Cites Families (203)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US650064A (en) * 1898-11-14 1900-05-22 Kitson Hydrocarbon Heating And Incandescent Lighting Company System of liquid distribution.
US3941763A (en) * 1975-03-28 1976-03-02 American Home Products Corporation PGlu-D-Met-Trp-Ser-Tyr-D-Ala-Leu-Arg-Pro-Gly-NH2 and intermediates
US4196265A (en) 1977-06-15 1980-04-01 The Wistar Institute Method of producing antibodies
US6936694B1 (en) * 1982-05-06 2005-08-30 Intermune, Inc. Manufacture and expression of large structural genes
US4469797A (en) 1982-09-23 1984-09-04 Miles Laboratories, Inc. Digoxigenin immunogens, antibodies, labeled conjugates, and related derivatives
US4816567A (en) 1983-04-08 1989-03-28 Genentech, Inc. Recombinant immunoglobin preparations
KR850004274A (en) 1983-12-13 1985-07-11 원본미기재 Method for preparing erythropoietin
NZ210501A (en) 1983-12-13 1991-08-27 Kirin Amgen Inc Erythropoietin produced by procaryotic or eucaryotic expression of an exogenous dna sequence
US4703008A (en) 1983-12-13 1987-10-27 Kiren-Amgen, Inc. DNA sequences encoding erythropoietin
US5082658A (en) 1984-01-16 1992-01-21 Genentech, Inc. Gamma interferon-interleukin-2 synergism
EP0158198A1 (en) 1984-03-29 1985-10-16 Takeda Chemical Industries, Ltd. DNA and use thereof
US5189015A (en) 1984-05-30 1993-02-23 Alfa-Laval Agri International Ab Method for prophylactic treatment of the colonization of a Staphylococcus aureus bacterial strain by bacterial cell surface protein with fibronectin and fibrinogen binding ability
US5077204A (en) * 1984-06-21 1991-12-31 Chiron Corporation Yeast endopeptidase for basic amino-acid site cleavage, preparation and use
US5807715A (en) 1984-08-27 1998-09-15 The Board Of Trustees Of The Leland Stanford Junior University Methods and transformed mammalian lymphocyte cells for producing functional antigen-binding protein including chimeric immunoglobulin
GR860984B (en) * 1985-04-17 1986-08-18 Zymogenetics Inc Expression of factor vii and ix activities in mammalian cells
US4690915A (en) 1985-08-08 1987-09-01 The United States Of America As Represented By The Department Of Health And Human Services Adoptive immunotherapy as a treatment modality in humans
US5679543A (en) 1985-08-29 1997-10-21 Genencor International, Inc. DNA sequences, vectors and fusion polypeptides to increase secretion of desired polypeptides from filamentous fungi
US5643565A (en) 1985-09-20 1997-07-01 Chiron Corporation Human IL-2 as a vaccine adjuvant
US4676980A (en) 1985-09-23 1987-06-30 The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services Target specific cross-linked heteroantibodies
US4935233A (en) 1985-12-02 1990-06-19 G. D. Searle And Company Covalently linked polypeptide cell modulators
DE3712985A1 (en) 1987-04-16 1988-11-03 Hoechst Ag BIFUNCTIONAL PROTEINS
US5359035A (en) 1985-12-21 1994-10-25 Hoechst Aktiengesellschaft Bifunctional proteins including interleukin-2 (IL-2) and granuloctyte macrophage colony stimulating factor (GM-CSF)
EP0237019A3 (en) 1986-03-14 1988-03-09 Toray Industries, Inc. Interferon conjugate and production thereof using recombinant gene
US5225539A (en) 1986-03-27 1993-07-06 Medical Research Council Recombinant altered antibodies and methods of making altered antibodies
DK173067B1 (en) 1986-06-27 1999-12-13 Univ Washington Human erythropoietin gene, method of expression thereof in transfected cell lines, the transfected cell lines
US4894227A (en) 1986-08-01 1990-01-16 Cetus Corporation Composition of immunotoxins with interleukin-2
US4946778A (en) 1987-09-21 1990-08-07 Genex Corporation Single polypeptide chain binding molecules
US5508031A (en) 1986-11-21 1996-04-16 Cetus Oncology Corporation Method for treating biological damage using a free-radial scavenger and interleukin-2
US4987071A (en) 1986-12-03 1991-01-22 University Patents, Inc. RNA ribozyme polymerases, dephosphorylases, restriction endoribonucleases and methods
US5019368A (en) 1989-02-23 1991-05-28 Cancer Biologics, Inc. Detection of necrotic malignant tissue and associated therapy
JP3101690B2 (en) 1987-03-18 2000-10-23 エス・ビィ・2・インコーポレイテッド Modifications of or for denatured antibodies
EP0318554B2 (en) 1987-05-21 2005-01-12 Micromet AG Targeted multifunctional proteins
US5091513A (en) 1987-05-21 1992-02-25 Creative Biomolecules, Inc. Biosynthetic antibody binding sites
US5258498A (en) 1987-05-21 1993-11-02 Creative Biomolecules, Inc. Polypeptide linkers for production of biosynthetic proteins
DE3853740T2 (en) 1987-06-10 1995-11-09 Dana Farber Cancer Inst Inc Bifunctional antibody designs and methods for the selective killing of cell populations.
US5064646A (en) 1988-08-02 1991-11-12 The University Of Maryland Novel infectious bursal disease virus
PH26813A (en) 1987-09-02 1992-11-05 Ciba Geigy Ag Conjugates of cytokines with immunoglobulins
US5677425A (en) 1987-09-04 1997-10-14 Celltech Therapeutics Limited Recombinant antibody
DE3850542T2 (en) 1987-09-23 1994-11-24 Bristol Myers Squibb Co Antibody heteroconjugates for killing HIV-infected cells.
PT88641B (en) 1987-10-02 1993-04-30 Genentech Inc METHOD FOR PREPARING A VARIETY OF ADHESION
PT89121A (en) 1987-12-04 1989-12-29 Du Pont PROCESS FOR THE PREPARATION OF INTERLEUQUIN-2 FIXED AND INTERLEUKIN-2 CONTAINING AN EXTENSION IN THE TERMINAL-CARBOXYL WITH ACTIVITY OF INTERLEUQUIN-2 NATURAL
WO1989006692A1 (en) 1988-01-12 1989-07-27 Genentech, Inc. Method of treating tumor cells by inhibiting growth factor receptor function
CA1341588C (en) 1988-01-26 2009-01-06 Michel Revel Human ifn-beta2/i1-6, its purification and use
JP2643968B2 (en) 1988-02-03 1997-08-25 サントリー株式会社 KEX2 endoprotease and method for producing the same
US5234830A (en) 1988-02-03 1993-08-10 Suntory Limited DNA encoding a KEX2 endoprotease without a C-terminal hydrophobic region
US5120525A (en) 1988-03-29 1992-06-09 Immunomedics, Inc. Radiolabeled antibody cytotoxic therapy of cancer
IE62463B1 (en) 1988-07-07 1995-02-08 Res Dev Foundation Immunoconjugates for cancer diagnosis and therapy
US5601819A (en) 1988-08-11 1997-02-11 The General Hospital Corporation Bispecific antibodies for selective immune regulation and for selective immune cell binding
US5457038A (en) 1988-11-10 1995-10-10 Genetics Institute, Inc. Natural killer stimulatory factor
US5242824A (en) 1988-12-22 1993-09-07 Oncogen Monoclonal antibody to human carcinomas
US5530101A (en) 1988-12-28 1996-06-25 Protein Design Labs, Inc. Humanized immunoglobulins
US5225538A (en) 1989-02-23 1993-07-06 Genentech, Inc. Lymphocyte homing receptor/immunoglobulin fusion proteins
US5116964A (en) 1989-02-23 1992-05-26 Genentech, Inc. Hybrid immunoglobulins
US5703055A (en) 1989-03-21 1997-12-30 Wisconsin Alumni Research Foundation Generation of antibodies through lipid mediated DNA delivery
US5166322A (en) 1989-04-21 1992-11-24 Genetics Institute Cysteine added variants of interleukin-3 and chemical modifications thereof
US6750329B1 (en) 1989-05-05 2004-06-15 Research Development Foundation Antibody delivery system for biological response modifiers
IE63847B1 (en) 1989-05-05 1995-06-14 Res Dev Foundation A novel antibody delivery system for biological response modifiers
SE8901687D0 (en) 1989-05-11 1989-05-11 Alfa Laval Agri Int FIBRONECTIN BINDING PROTEIN AS WELL AS IT'S PREPARATION
US5399346A (en) 1989-06-14 1995-03-21 The United States Of America As Represented By The Department Of Health And Human Services Gene therapy
ATE123065T1 (en) * 1989-07-07 1995-06-15 Takeda Chemical Industries Ltd PROTEINS AND THEIR PRODUCTION.
AU648509B2 (en) * 1989-07-14 1994-04-28 Wyeth Holdings Corporation Stable vaccine compositions containing interleukins
US5073627A (en) 1989-08-22 1991-12-17 Immunex Corporation Fusion proteins comprising GM-CSF and IL-3
DK0417563T3 (en) 1989-09-12 2000-11-06 Hoffmann La Roche TNF-binding proteins
US5856298A (en) 1989-10-13 1999-01-05 Amgen Inc. Erythropoietin isoforms
DK0433827T3 (en) 1989-12-22 1998-09-28 Hoffmann La Roche Cytotoxic lymphocyte maturation factor
US5314995A (en) 1990-01-22 1994-05-24 Oncogen Therapeutic interleukin-2-antibody based fusion proteins
US5349053A (en) * 1990-06-01 1994-09-20 Protein Design Labs, Inc. Chimeric ligand/immunoglobulin molecules and their uses
US7253264B1 (en) 1990-06-28 2007-08-07 Sanofi-Arentideutschland GmbH Immunoglobulin fusion proteins, their production and use
US5650150A (en) 1990-11-09 1997-07-22 Gillies; Stephen D. Recombinant antibody cytokine fusion proteins
US5709859A (en) 1991-01-24 1998-01-20 Bristol-Myers Squibb Company Mixed specificity fusion proteins
JPH06505496A (en) * 1991-03-11 1994-06-23 ザ・ジェネラル・ホスピタル・コーポレーション Compositions and methods for inhibiting activation of active factor X111
US6072039A (en) 1991-04-19 2000-06-06 Rohm And Haas Company Hybrid polypeptide comparing a biotinylated avidin binding polypeptide fused to a polypeptide of interest
DK0636173T3 (en) 1991-05-31 1999-05-31 Genentech Inc Treatment of HIV-associated immune thrombocytopenic purpura
US5199942A (en) 1991-06-07 1993-04-06 Immunex Corporation Method for improving autologous transplantation
DE69227693T2 (en) 1991-08-30 1999-07-22 Hutchinson Fred Cancer Res HYBRID CYTOKINE
US20020037558A1 (en) 1991-10-23 2002-03-28 Kin-Ming Lo E.coli produced immunoglobulin constructs
US6627615B1 (en) 1991-12-17 2003-09-30 The Regents Of The University Of California Methods and compositions for in vivo gene therapy
KR100254759B1 (en) 1992-01-23 2000-05-01 플레믹 크리스티안 Monomeric and cimeric antibody-fragment fusion proteins
ATE260971T1 (en) 1992-04-01 2004-03-15 Univ Rockefeller METHOD FOR THE IN VITRO CULTIVATION OF DENDRITIC PRECURSOR CELLS AND THEIR USE FOR IMMUNOGENIC PRODUCTION
EP0615451B1 (en) 1992-05-26 2005-12-07 Immunex Corporation Novel cytokine that binds cd30
IL105914A0 (en) 1992-06-04 1993-10-20 Univ California Methods and compositions for in vivo gene therapy
US5614184A (en) 1992-07-28 1997-03-25 New England Deaconess Hospital Recombinant human erythropoietin mutants and therapeutic methods employing them
CA2142007C (en) 1992-08-11 2007-10-30 Robert Glen Urban Immunomodulatory peptides
DE4228839A1 (en) 1992-08-29 1994-03-03 Behringwerke Ag Methods for the detection and determination of mediators
CA2147499C (en) 1992-11-05 2010-10-19 Ron S. Israeli Prostate-specific membrane antigen
US5738849A (en) 1992-11-24 1998-04-14 G. D. Searle & Co. Interleukin-3 (IL-3) variant fusion proteins, their recombinant production, and therapeutic compositions comprising them
US5543297A (en) 1992-12-22 1996-08-06 Merck Frosst Canada, Inc. Human cyclooxygenase-2 cDNA and assays for evaluating cyclooxygenase-2 activity
US6096331A (en) 1993-02-22 2000-08-01 Vivorx Pharmaceuticals, Inc. Methods and compositions useful for administration of chemotherapeutic agents
AU6816194A (en) 1993-04-20 1994-11-08 Robinson, William S. Methods and materials for treatment of individuals infected with intracellular infectious agents
US5759551A (en) 1993-04-27 1998-06-02 United Biomedical, Inc. Immunogenic LHRH peptide constructs and synthetic universal immune stimulators for vaccines
WO1994025055A1 (en) 1993-04-29 1994-11-10 Abbott Laboratories Erythropoietin analog compositions and methods
US5554512A (en) 1993-05-24 1996-09-10 Immunex Corporation Ligands for flt3 receptors
US6017536A (en) 1993-06-07 2000-01-25 Trimeris, Inc. Simian immunodeficiency virus peptides with antifusogenic and antiviral activities
US6479055B1 (en) 1993-06-07 2002-11-12 Trimeris, Inc. Methods for inhibition of membrane fusion-associated events, including respiratory syncytial virus transmission
US5464933A (en) 1993-06-07 1995-11-07 Duke University Synthetic peptide inhibitors of HIV transmission
US6518013B1 (en) 1993-06-07 2003-02-11 Trimeris, Inc. Methods for the inhibition of epstein-barr virus transmission employing anti-viral peptides capable of abrogating viral fusion and transmission
US6310180B1 (en) 1993-06-21 2001-10-30 Vanderbilt University Method for synthesis of proteins
CA2125763C (en) 1993-07-02 2007-08-28 Maurice Kent Gately P40 homodimer of interleukin-12
ZA946122B (en) 1993-08-17 1995-03-20 Amgen Inc Erythropoietin analogs
US5639725A (en) 1994-04-26 1997-06-17 Children's Hospital Medical Center Corp. Angiostatin protein
US5837682A (en) 1996-03-08 1998-11-17 The Children's Medical Center Corporation Angiostatin fragments and method of use
IL113509A (en) 1994-04-26 2005-12-18 Childrens Medical Center Angiostatin protein compositions and methods of use
US5648240A (en) 1994-05-24 1997-07-15 Texas A&M University MHC II analog from Staphylococcus aureus
US6429199B1 (en) 1994-07-15 2002-08-06 University Of Iowa Research Foundation Immunostimulatory nucleic acid molecules for activating dendritic cells
CA2194761C (en) * 1994-07-15 2006-12-19 Arthur M. Krieg Immunomodulatory oligonucleotides
US6309853B1 (en) 1994-08-17 2001-10-30 The Rockfeller University Modulators of body weight, corresponding nucleic acids and proteins, and diagnostic and therapeutic uses thereof
US5541087A (en) * 1994-09-14 1996-07-30 Fuji Immunopharmaceuticals Corporation Expression and export technology of proteins as immunofusins
EP0706799B1 (en) 1994-09-16 2001-11-14 MERCK PATENT GmbH Immunoconjugates II
WO1996018412A1 (en) * 1994-12-12 1996-06-20 Beth Israel Hospital Association Chimeric cytokines and uses thereof
US6086875A (en) 1995-01-17 2000-07-11 The Brigham And Women's Hospital, Inc. Receptor specific transepithelial transport of immunogens
US6485726B1 (en) 1995-01-17 2002-11-26 The Brigham And Women's Hospital, Inc. Receptor specific transepithelial transport of therapeutics
US6030613A (en) 1995-01-17 2000-02-29 The Brigham And Women's Hospital, Inc. Receptor specific transepithelial transport of therapeutics
US5691309A (en) 1995-01-31 1997-11-25 Eli Lilly And Company Anti-obesity proteins
US5552524A (en) 1995-01-31 1996-09-03 Eli Lilly And Company Anti-obesity proteins
US5891680A (en) 1995-02-08 1999-04-06 Whitehead Institute For Biomedical Research Bioactive fusion proteins comprising the p35 and p40 subunits of IL-12
US5731168A (en) 1995-03-01 1998-03-24 Genentech, Inc. Method for making heteromultimeric polypeptides
AU712585B2 (en) 1995-03-10 1999-11-11 Genentech Inc. Receptor activation by gas6
US5719266A (en) 1995-03-17 1998-02-17 Eli Lilly And Company Anti-obesity proteins
US5591573A (en) 1995-04-10 1997-01-07 Alpha Therapeutic Corporation Method and system for testing blood samples
US5739277A (en) 1995-04-14 1998-04-14 Genentech Inc. Altered polypeptides with increased half-life
US5579277A (en) 1995-05-01 1996-11-26 Apple Computer, Inc. System and method for interleaving memory banks
US6184344B1 (en) 1995-05-04 2001-02-06 The Scripps Research Institute Synthesis of proteins by native chemical ligation
US6281010B1 (en) 1995-06-05 2001-08-28 The Trustees Of The University Of Pennsylvania Adenovirus gene therapy vehicle and cell line
KR100571215B1 (en) 1995-06-07 2006-10-24 트라이머리스 인코퍼레이티드 Treatment of HIV and Other Virus Infections Using Combination Therapy
CN1195293A (en) 1995-06-30 1998-10-07 伊莱利利公司 Method for treating disbetes
US6406689B1 (en) 1995-10-03 2002-06-18 Frank W. Falkenberg Compositions and methods for treatment of tumors and metastatic diseases
US5854205A (en) 1995-10-23 1998-12-29 The Children's Medical Center Corporation Therapeutic antiangiogenic compositions and methods
US6620413B1 (en) 1995-12-27 2003-09-16 Genentech, Inc. OB protein-polymer chimeras
US5723125A (en) * 1995-12-28 1998-03-03 Tanox Biosystems, Inc. Hybrid with interferon-alpha and an immunoglobulin Fc linked through a non-immunogenic peptide
US6080409A (en) 1995-12-28 2000-06-27 Dendreon Corporation Immunostimulatory method
US6750334B1 (en) 1996-02-02 2004-06-15 Repligen Corporation CTLA4-immunoglobulin fusion proteins having modified effector functions and uses therefor
US6096313A (en) * 1996-02-09 2000-08-01 Ludwig Institute For Cancer Research Compositions containing immunogenic molecules and granulocyte-macrophage colony stimulating factor, as an adjuvant
CA2198968C (en) 1996-03-04 2010-02-09 Toyofumi Masuda Process for production of secretory kex2 derivatives
JP2001502521A (en) 1996-04-26 2001-02-27 ベス イスラエル デアコネス メディカル センター Interleukin-15 antagonist
CN1136197C (en) 1996-05-30 2004-01-28 霍夫曼-拉罗奇有限公司 Novel pyridajinone derivatives
US5922685A (en) 1996-06-05 1999-07-13 Powderject Vaccines, Inc. IL-12 gene therapy of tumors
EP0826696B1 (en) 1996-09-03 2002-05-29 GSF-Forschungszentrum für Umwelt und Gesundheit GmbH Use of bi-and trispecific antibodies for inducing tumor immunity
US5994104A (en) 1996-11-08 1999-11-30 Royal Free Hospital School Of Medicine Interleukin-12 fusion protein
US6737057B1 (en) * 1997-01-07 2004-05-18 The University Of Tennessee Research Corporation Compounds, compositions and methods for the endocytic presentation of immunosuppressive factors
US6100387A (en) 1997-02-28 2000-08-08 Genetics Institute, Inc. Chimeric polypeptides containing chemokine domains
US6277375B1 (en) 1997-03-03 2001-08-21 Board Of Regents, The University Of Texas System Immunoglobulin-like domains with increased half-lives
US5998598A (en) * 1997-03-10 1999-12-07 The United States Of America, As Represented By The Department Of Health And Human Services Immunoadhesins and methods of production and use thereof
EP0973550B1 (en) 1997-04-11 2002-10-09 G.D. SEARLE & CO. Antagonistic anti-avb3 integrin antibodies
CA2292724A1 (en) 1997-06-13 1998-12-17 Gryphon Sciences Solid phase native chemical ligation of unprotected or n-terminal cysteine protected peptides in aqueous solution
US6310183B1 (en) 1997-09-10 2001-10-30 Novo Nordisk A/S Coagulation factor VIIa composition
ATE267215T1 (en) 1997-12-08 2004-06-15 Lexigen Pharm Corp HETERODIMARY FUSION PROTEINS FOR USE FOR TARGETED IMMUNTHERAPY AND GENERAL IMMUNE EXCITATION
GB9727262D0 (en) * 1997-12-24 1998-02-25 Smithkline Beecham Biolog Vaccine
US20030105294A1 (en) 1998-02-25 2003-06-05 Stephen Gillies Enhancing the circulating half life of antibody-based fusion proteins
US6008321A (en) 1998-03-16 1999-12-28 Pharmacopeia, Inc. Universal linker for combinatorial synthesis
US6281331B1 (en) 1998-03-23 2001-08-28 Trimeris, Inc. Methods and compositions for peptide synthesis
JP2002511432A (en) 1998-04-15 2002-04-16 レキシジェン ファーマシューティカルズ コーポレイション Enhancement of antibody-cytokine fusion protein-mediated immune response by co-administration of an angiogenesis inhibitor
RU2217168C2 (en) 1998-04-17 2003-11-27 Лексиген Фармасьютикэлс Корпорейшн Enhancement of immune response mediated by proteins fused of antibody and cytokine by means of combined administration of prostaglandin inhibitor
AU3655899A (en) 1998-04-20 1999-11-08 Regents Of The University Of California, The Modified immunoglobulin molecules and methods for use thereof
CA2328490A1 (en) 1998-05-14 1999-11-18 Merck Patent Gesellschaft Mit Beschraenkter Haftung Fused protein
US6620382B1 (en) 1998-05-22 2003-09-16 Biopheresis Technologies, Llc. Method and compositions for treatment of cancers
EP1105427A2 (en) 1998-08-17 2001-06-13 Abgenix, Inc. Generation of modified molecules with increased serum half-lives
ATE462725T1 (en) 1998-08-25 2010-04-15 Merck Patent Gmbh EXPRESSION AND EXPORT OF ANGIOSTATIN AND ENDOSTATIN AS IMMUNOFUSINS
US6646113B1 (en) 1998-09-17 2003-11-11 The Trustees Of The University Of Pennsylvania Nucleic acid molecule encoding human survival of motor neuron-interacting protein 1 (SIP1) deletion mutants
US6335176B1 (en) 1998-10-16 2002-01-01 Pharmacopeia, Inc. Incorporation of phosphorylation sites
US6660843B1 (en) 1998-10-23 2003-12-09 Amgen Inc. Modified peptides as therapeutic agents
US7488590B2 (en) * 1998-10-23 2009-02-10 Amgen Inc. Modified peptides as therapeutic agents
JP4463988B2 (en) 1998-11-06 2010-05-19 ノボ ノルディスク ヘルス ケア アクチェンゲゼルシャフト Method for producing factor VII
HUP0105090A2 (en) 1999-01-07 2002-04-29 Lexigen Pharmaceuticals Corporation Expression and export of anti-obesity proteins as fc fusion proteins
DE60041183D1 (en) 1999-05-06 2009-02-05 Univ Wake Forest COMPOSITIONS AND METHODS FOR IDENTIFYING ANTIGENES WHICH CAUSE AN IMMUNE RESPONSE
US6348192B1 (en) 1999-05-11 2002-02-19 Bayer Corporation Interleukin-2 mutein expressed from mammalian cells
BR0010725A (en) 1999-05-19 2002-02-19 Lexigen Pharm Corp Expression and export of interferon-alpha proteins as fc fusion proteins
WO2000078334A1 (en) 1999-06-17 2000-12-28 University Of Maryland Biotechnology Institute Chimeric chemokine-antigen polypeptides and uses therefor
WO2001001749A2 (en) * 1999-07-02 2001-01-11 Genentech, Inc. FVIIa ANTAGONISTS
JO2291B1 (en) 1999-07-02 2005-09-12 اف . هوفمان لاروش ايه جي Erythopintin derivatives
CZ299516B6 (en) 1999-07-02 2008-08-20 F. Hoffmann-La Roche Ag Erythropoietin glycoprotein conjugate, process for its preparation and use and pharmaceutical composition containing thereof
US6469136B1 (en) 1999-07-07 2002-10-22 Trimeris, Inc. Methods and composition for peptide synthesis
US7067110B1 (en) 1999-07-21 2006-06-27 Emd Lexigen Research Center Corp. Fc fusion proteins for enhancing the immunogenicity of protein and peptide antigens
SK782002A3 (en) 1999-07-21 2003-08-05 Lexigen Pharm Corp FC fusion proteins for enhancing the immunogenicity of protein and peptide antigens
HUP0202442A3 (en) 1999-08-09 2005-01-28 Lexigen Pharmaceuticals Corp L Multiple cytokine-antibody complexes
JP2004500047A (en) * 1999-10-20 2004-01-08 ザ ジョンズ ホプキンス ユニバーシティー スクール オブ メディシン Chimeric immunogenic compositions and nucleic acids encoding them
EP1228214A2 (en) 1999-11-12 2002-08-07 MERCK PATENT GmbH Erythropoietin forms with improved properties
DE19963859A1 (en) 1999-12-30 2001-07-12 Apotech Res & Dev Ltd Bi- or oligomer of a di-, tri-, quattro- or pentamer of recombinant fusion proteins
ATE336514T1 (en) 2000-02-11 2006-09-15 Merck Patent Gmbh INCREASE THE CIRCULATION HALF-LIFE OF ANTIBODIES-BASED FUSION PROTEINS
WO2001062298A2 (en) 2000-02-24 2001-08-30 Philogen S.R.L. Compositions and methods for treatment of angiogenesis in pathological lesions
US6586398B1 (en) 2000-04-07 2003-07-01 Amgen, Inc. Chemically modified novel erythropoietin stimulating protein compositions and methods
WO2001088117A2 (en) 2000-05-12 2001-11-22 Neose Technologies, Inc. In vitro fucosylation recombinant glycopeptides
PT1294401E (en) 2000-06-29 2007-11-09 Merck Patent Gmbh Enhancement of antibody-cytokine fusion protein mediated immune responses by combined treatment with immunocytokine uptake enhancing agents
US7138119B2 (en) * 2000-09-15 2006-11-21 Progenics Pharmaceuticals, Inc. Compositions and methods for inhibition of HIV-1 infection
HUP0401300A3 (en) 2001-01-18 2005-06-28 Merck Patent Gmbh Bifunctional fusion proteins with glucocerebrosidase activity
EP1361891A2 (en) 2001-02-19 2003-11-19 MERCK PATENT GmbH Artificial fusion proteins with reduced immunogenicity
CA2438652A1 (en) 2001-02-19 2002-09-06 Merck Patent Gesellschaft Mit Beschraenkter Haftung Method for identification of t-cell epitopes and use for preparing molecules with reeduced immunogenicity
KR20090010127A (en) 2001-03-07 2009-01-28 메르크 파텐트 게엠베하 Expression technology for proteins containing a hybrid isotype antibody moiety
WO2002079415A2 (en) 2001-03-30 2002-10-10 Lexigen Pharmaceuticals Corp. Reducing the immunogenicity of fusion proteins
DE10118308A1 (en) * 2001-04-12 2002-10-17 Bayer Ag Process for the preparation of benzyl hydroxybenzoates
DK1383785T3 (en) 2001-05-03 2011-05-23 Merck Patent Gmbh Recombinant tumor-specific antibody and its use
US7371371B2 (en) 2001-08-13 2008-05-13 University Of Southern California Interleukin-2 mutants with reduced toxicity
ATE542137T1 (en) 2001-12-04 2012-02-15 Merck Patent Gmbh IMMUNOCYTOKINE WITH MODULATED SELECTIVITY
SI1946776T1 (en) * 2002-02-27 2017-07-31 Immunex Corporation Stabilized tnfr-fc composition comprising arginine
AU2002316574B2 (en) 2002-03-15 2008-05-01 Brandeis University Central airway administration for systemic delivery of therapeutics
WO2004055056A1 (en) 2002-12-17 2004-07-01 Merck Patent Gmbh Humanized antibody (h14.18) of the mouse 14.18 antibody binding to gd2 and its fusion with il-2
US20050281829A1 (en) * 2003-05-06 2005-12-22 Hehir Cristina A T Fc chimeric proteins with anti-HIV drugs
US7348004B2 (en) 2003-05-06 2008-03-25 Syntonix Pharmaceuticals, Inc. Immunoglobulin chimeric monomer-dimer hybrids
US20050037947A1 (en) * 2003-05-06 2005-02-17 Bitonti Alan J. Inhibition of drug binding to serum albumin
TWI353991B (en) 2003-05-06 2011-12-11 Syntonix Pharmaceuticals Inc Immunoglobulin chimeric monomer-dimer hybrids
ES2361036T3 (en) * 2003-05-06 2011-06-13 Syntonix Pharmaceuticals, Inc. CHEMICAL PROTEINS VII-FC OF THE COAGULATION FACTOR FOR THE TREATMENT OF A HEMOSTATIC DISORDER.
US20050069521A1 (en) 2003-08-28 2005-03-31 Emd Lexigen Research Center Corp. Enhancing the circulating half-life of interleukin-2 proteins
RU2251699C1 (en) * 2003-09-25 2005-05-10 Киселев Всеволод Иванович Method for early and preclinical diagnostics of cervical cancer
EA201171259A1 (en) * 2009-04-22 2012-05-30 Мерк Патент Гмбх ANTIBODY HYBRID PROTEINS WITH MODIFIED FCRN BINDING SITES

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