WO2017001491A2 - Novel peptides and combination of peptides for use in immunotherapy against ovarian cancer and other cancers - Google Patents

Novel peptides and combination of peptides for use in immunotherapy against ovarian cancer and other cancers Download PDF

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Publication number
WO2017001491A2
WO2017001491A2 PCT/EP2016/065166 EP2016065166W WO2017001491A2 WO 2017001491 A2 WO2017001491 A2 WO 2017001491A2 EP 2016065166 W EP2016065166 W EP 2016065166W WO 2017001491 A2 WO2017001491 A2 WO 2017001491A2
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WO
WIPO (PCT)
Prior art keywords
cancer
peptide
cell
melanoma
seq
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Ceased
Application number
PCT/EP2016/065166
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English (en)
French (fr)
Other versions
WO2017001491A3 (en
Inventor
Andrea Mahr
Toni Weinschenk
Helen HÖRZER
Oliver Schoor
Jens Fritsche
Harpreet Singh
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Immatics Biotechnologies GmbH
Original Assignee
Immatics Biotechnologies GmbH
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
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First worldwide family litigation filed litigation Critical https://patents.darts-ip.com/?family=53872514&utm_source=google_patent&utm_medium=platform_link&utm_campaign=public_patent_search&patent=WO2017001491(A2) "Global patent litigation dataset” by Darts-ip is licensed under a Creative Commons Attribution 4.0 International License.
Priority to JP2017563564A priority Critical patent/JP2018521641A/ja
Priority to KR1020187003095A priority patent/KR20180022968A/ko
Priority to MA42294A priority patent/MA42294B1/fr
Priority to CA2990989A priority patent/CA2990989A1/en
Priority to EP16733523.1A priority patent/EP3317296B1/en
Priority to MA41520A priority patent/MA41520B2/fr
Priority to EP20170129.9A priority patent/EP3712165A3/en
Priority to IL308735A priority patent/IL308735A/en
Priority to EP21177102.7A priority patent/EP3919507A3/en
Priority to EA201792632A priority patent/EA201792632A1/ru
Priority to UAA201711177A priority patent/UA123699C2/uk
Priority to AU2016286274A priority patent/AU2016286274B2/en
Priority to BR112017027459-0A priority patent/BR112017027459A2/en
Priority to MX2017017145A priority patent/MX2017017145A/es
Priority to SI201630998T priority patent/SI3317296T1/sl
Priority to HRP20202019TT priority patent/HRP20202019T1/hr
Priority to PE2022002253A priority patent/PE20230321A1/es
Application filed by Immatics Biotechnologies GmbH filed Critical Immatics Biotechnologies GmbH
Priority to DK16733523.1T priority patent/DK3317296T3/da
Priority to LTEP16733523.1T priority patent/LT3317296T/lt
Priority to CR20180001A priority patent/CR20180001A/es
Priority to CN201680037792.7A priority patent/CN108026154B/zh
Priority to MYPI2017704911A priority patent/MY191654A/en
Priority to PE2017002488A priority patent/PE20181618A1/es
Priority to MDE20180477T priority patent/MD3317296T2/ro
Priority to RS20201506A priority patent/RS61190B1/sr
Priority to ES16733523T priority patent/ES2839223T3/es
Publication of WO2017001491A2 publication Critical patent/WO2017001491A2/en
Publication of WO2017001491A3 publication Critical patent/WO2017001491A3/en
Priority to ZA2017/07942A priority patent/ZA201707942B/en
Priority to IL256189A priority patent/IL256189A/en
Priority to PH12017502261A priority patent/PH12017502261A1/en
Priority to CONC2017/0012891A priority patent/CO2017012891A2/es
Anticipated expiration legal-status Critical
Priority to CY20201101195T priority patent/CY1123635T1/el
Priority to AU2021200599A priority patent/AU2021200599B2/en
Priority to AU2022215208A priority patent/AU2022215208A1/en
Ceased legal-status Critical Current

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    • C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
    • C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
    • C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
    • C07K14/4748—Tumour specific antigens; Tumour rejection antigen precursors [TRAP], e.g. MAGE
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    • C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
    • C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
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    • C07K2317/34—Identification of a linear epitope shorter than 20 amino acid residues or of a conformational epitope defined by amino acid residues
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Definitions

  • Novel peptides and combination of peptides for use in immunotherapy against ovarian cancer and other cancers are novel peptides and combination of peptides for use in immunotherapy against ovarian cancer and other cancers
  • the present invention relates to peptides, proteins, nucleic acids and cells for use in immunotherapeutic methods.
  • the present invention relates to the immunotherapy of cancer.
  • the present invention furthermore relates to tumor- associated T-cell peptide epitopes, alone or in combination with other tumor-associated peptides that can for example serve as active pharmaceutical ingredients of vaccine compositions that stimulate anti-tumor immune responses, or to stimulate T cells ex vivo and transfer into patients.
  • Peptides bound to molecules of the major histocompatibility complex (MHC), or peptides as such can also be targets of antibodies, soluble T-cell receptors, and other binding molecules.
  • MHC major histocompatibility complex
  • the present invention relates to several novel peptide sequences and their variants derived from HLA class I molecules of human tumor cells that can be used in vaccine compositions for eliciting anti-tumor immune responses, or as targets for the development of pharmaceutically/immunologically active compounds and cells.
  • ovarian cancer is the seventh most common cancer in women, representing 4% of all cancers in women.
  • the fatality rate of ovarian cancer tends to be rather high relative to other cancers of the female reproductive organs, and case fatality is higher in lower-resource settings.
  • ovarian cancer is the eighth most frequent cause of cancer death among women, with 152 000 deaths.
  • In 2012 almost 55% of all new cases occurred in countries with high or very high levels of human development; 37% of the new cases and 39% of the deaths occurred in Europe and North America. Incidence rates are highest in northern and eastern Europe, North America, and Oceania, and tend to be relatively low in Africa and much of Asia. Incidence rates have been declining in certain countries with very high levels of human development, notably in Europe and North America.
  • ovarian carcinomas are also the most lethal gynecological malignancies. Based on histopathology and molecular genetics, ovarian carcinomas are divided into five main types: high-grade serous (70%), endometrioid (10%), clear cell (10%), mucinous (3%), and low-grade serous carcinomas ( ⁇ 5%), which together account for more than 95% of cases. Much less common are malignant germ cell tumours (dysgerminomas, yolk sac tumours, and immature teratomas) (3% of ovarian cancers) and potentially malignant sex cord stromal tumours (1-2%), the most common of which are granulosa cell tumours.
  • Surgical resection is the primary therapy in early as well as advanced stage ovarian carcinoma. Surgical removal is followed by systemic chemotherapy with platinum analogs, except for very low grade ovarian cancers (stage IA, grade 1 ), where postoperative chemotherapy is not indicated.
  • the first line chemotherapy comprises a combination of carboplatin with paclitaxel, which can be supplemented with bevacizumab.
  • the standard treatment for platinum-resistant ovarian cancers consists of a monotherapy with one of the following chemotherapeutics: pegylated liposomal doxorubicin, topotecane, gemcitabine or paclitaxel (S3-Leitline maligne Ovarialtumore, 2013).
  • Immunotherapy appears to be a promising strategy to ameliorate the treatment of ovarian cancer patients, as the presence of pro-inflammatory tumor infiltrating lymphocytes, especially CD8-positive T cells, correlates with good prognosis and T cells specific for tumor-associated antigens can be isolated from cancer tissue.
  • Cytokine therapy with interleukin-2, interferon-alpha, interferon-gamma or granulocyte- macrophage colony stimulating factor aims at boosting the patient's own anti-tumor immune response and these treatments have already shown promising results in small study cohorts.
  • Monoclonal antibodies that specifically recognize tumor-associated proteins are thought to enhance immune cell-mediated killing of tumor cells.
  • the anti-CA-125 antibodies oregovomab and abagovomab as well as the anti-EpCAM antibody catumaxomab achieved promising results in phase II and III studies.
  • the anti-MUC1 antibody HMFG1 failed to clearly enhance survival in a phase III study.
  • An alternative approach uses monoclonal antibodies to target and block growth factor and survival receptors on tumor cells. While administration of trastuzumab (anti- HER2/neu antibody) and MOv18 and MORAb-003 (anti-folate receptor alpha antibodies) only conferred limited clinical benefit to ovarian cancer patients, addition of bevacizumab (anti-VEGF antibody) to the standard chemotherapy in advanced ovarian cancer appears to be advantageous. Adoptive transfer of immune cells achieved heterogeneous results in clinical trials. Adoptive transfer of autologous, in vitro expanded tumor infiltrating T cells was shown to be a promising approach in a pilot trial.
  • T cells harboring a chimeric antigen receptor specific for folate receptor alpha did not induce a significant clinical response in a phase I trial.
  • Dendritic cells pulsed with tumor cell lysate or tumor- associated proteins in vitro were shown to enhance the anti-tumor T cell response upon transfer, but the extent of T cell activation did not correlate with clinical effects. Transfer of natural killer cells caused significant toxicities in a phase II study.
  • Intrinsic anti-tumor immunity as well as immunotherapy are hampered by an immunosuppressive tumor microenvironment.
  • immunomodulatory drugs like cyclophosphamide, anti-CD25 antibodies and pegylated liposomal doxorubicin are tested in combination with immunotherapy.
  • Most reliable data are currently available for ipilimumab, an anti-CTLA4 antibody, which enhances T cell activity. Ipilimumab was shown to exert significant anti-tumor effects in ovarian cancer patients (Mantia-Smaldone et al., 2012).
  • Immunotherapy of cancer represents an option of specific targeting of cancer cells while minimizing side effects. Cancer immunotherapy makes use of the existence of tumor associated antigens.
  • TAAs tumor associated antigens
  • CT antigens The first TAAs ever identified that can be recognized by T cells belong to this class, which was originally called cancer-testis (CT) antigens because of the expression of its members in histologically different human tumors and, among normal tissues, only in spermatocytes/spermatogonia of testis and, occasionally, in placenta. Since the cells of testis do not express class I and II HLA molecules, these antigens cannot be recognized by T cells in normal tissues and can therefore be considered as immunologically tumor-specific.
  • CT antigens are the MAGE family members and NY-ESO-1 .
  • TAAs Differentiation antigens: These TAAs are shared between tumors and the normal tissue from which the tumor arose. Most of the known differentiation antigens are found in melanomas and normal melanocytes. Many of these melanocyte lineage-related proteins are involved in biosynthesis of melanin and are therefore not tumor specific but nevertheless are widely used for cancer immunotherapy. Examples include, but are not limited to, tyrosinase and Melan-A/MART-1 for melanoma or PSA for prostate cancer. c) Over-expressed TAAs: Genes encoding widely expressed TAAs have been detected in histologically different types of tumors as well as in many normal tissues, generally with lower expression levels.
  • TAAs Her-2/neu, survivin, telomerase, or WT1.
  • Tumor-specific antigens arise from mutations of normal genes (such as ⁇ -catenin, CDK4, etc.). Some of these molecular changes are associated with neoplastic transformation and/or progression. Tumor-specific antigens are generally able to induce strong immune responses without bearing the risk for autoimmune reactions against normal tissues. On the other hand, these TAAs are in most cases only relevant to the exact tumor on which they were identified and are usually not shared between many individual tumors. Tumor-specificity (or -association) of a peptide may also arise if the peptide originates from a tumor- (-associated) exon in case of proteins with tumor-specific (-associated) isoforms.
  • TAAs arising from abnormal post-translational modifications may arise from proteins which are neither specific nor overexpressed in tumors but nevertheless become tumor associated by posttranslational processes primarily active in tumors. Examples for this class arise from altered glycosylation patterns leading to novel epitopes in tumors as for MUC1 or events like protein splicing during degradation which may or may not be tumor specific.
  • Oncoviral proteins are viral proteins that may play a critical role in the oncogenic process and, because they are foreign (not of human origin), they can evoke a T-cell response. Examples of such proteins are the human papilloma type 16 virus proteins, E6 and E7, which are expressed in cervical carcinoma.
  • T-cell based immunotherapy targets peptide epitopes derived from tumor-associated or tumor-specific proteins, which are presented by molecules of the major histocompatibility complex (MHC).
  • MHC major histocompatibility complex
  • the antigens that are recognized by the tumor specific T lymphocytes, that is, the epitopes thereof, can be molecules derived from all protein classes, such as enzymes, receptors, transcription factors, etc. which are expressed and, as compared to unaltered cells of the same origin, usually up-regulated in cells of the respective tumor.
  • MHC class I There are two classes of MHC-molecules, MHC class I and MHC class II.
  • MHC class I molecules are composed of an alpha heavy chain and beta-2-microglobulin, MHC class II molecules of an alpha and a beta chain. Their three-dimensional conformation results in a binding groove, which is used for non-covalent interaction with peptides.
  • MHC class I molecules can be found on most nucleated cells. They present peptides that result from proteolytic cleavage of predominantly endogenous proteins, defective ribosomal products (DRIPs) and larger peptides. However, peptides derived from endosomal compartments or exogenous sources are also frequently found on MHC class I molecules. This non-classical way of class I presentation is referred to as cross- presentation in the literature (Brossart and Bevan, 1997; Rock et al., 1990). MHC class II molecules can be found predominantly on professional antigen presenting cells (APCs), and primarily present peptides of exogenous or transmembrane proteins that are taken up by APCs e.g. during endocytosis, and are subsequently processed.
  • APCs professional antigen presenting cells
  • TCR T-cell receptor
  • CD4-positive-helper-T cells bearing the appropriate TCR. It is well known that the TCR, the peptide and the MHC are thereby present in a stoichiometric amount of 1 :1 :1.
  • CD4-positive helper T cells play an important role in inducing and sustaining effective responses by CD8-positive cytotoxic T cells.
  • TAA tumor associated antigens
  • T helper cells support a cytotoxic T cell- (CTL-) friendly cytokine milieu (Mortara et al., 2006) and attract effector cells, e.g. CTLs, natural killer (NK) cells, macrophages, and granulocytes (Hwang et al., 2007).
  • CTL- cytotoxic T cell- friendly cytokine milieu
  • NK natural killer cells
  • macrophages macrophages
  • granulocytes Hwang et al., 2007.
  • MHC class II molecules In the absence of inflammation, expression of MHC class II molecules is mainly restricted to cells of the immune system, especially professional antigen-presenting cells (APC), e.g., monocytes, monocyte-derived cells, macrophages, dendritic cells.
  • APC professional antigen-presenting cells
  • monocytes e.g., monocytes, monocyte-derived cells, macrophages, dendritic cells.
  • monocytes e.g., monocytes, monocyte-derived cells, macrophages, dendritic cells.
  • Elongated (longer) peptides of the invention can act as MHC class II active epitopes.
  • T- helper cells activated by MHC class II epitopes, play an important role in orchestrating the effector function of CTLs in anti-tumor immunity.
  • T-helper cell epitopes that trigger a T-helper cell response of the TH1 type support effector functions of CD8-positive killer T cells, which include cytotoxic functions directed against tumor cells displaying tumor- associated peptide/MHC complexes on their cell surfaces. In this way tumor-associated T-helper cell peptide epitopes, alone or in combination with other tumor-associated peptides, can serve as active pharmaceutical ingredients of vaccine compositions that stimulate anti-tumor immune responses.
  • CD4-positive T cells are sufficient for inhibiting manifestation of tumors via inhibition of angiogenesis by secretion of interferon-gamma (IFNy) (Beatty and Paterson, 2001 ; Mumberg et al., 1999). There is evidence for CD4 T cells as direct anti-tumor effectors (Braumuller et al., 2013; Tran et al., 2014).
  • IFNy interferon-gamma
  • HLA class II molecules Since the constitutive expression of HLA class II molecules is usually limited to immune cells, the possibility of isolating class II peptides directly from primary tumors was previously not considered possible. However, Dengjel et al. were successful in identifying a number of MHC Class II epitopes directly from tumors (WO 2007/028574, EP 1 760 088 B1 ).
  • CD8 and CD4 dependent Since both types of response, CD8 and CD4 dependent, contribute jointly and synergistically to the anti-tumor effect, the identification and characterization of tumor- associated antigens recognized by either CD8+ T cells (ligand: MHC class I molecule + peptide epitope) or by CD4-positive T-helper cells (ligand: MHC class II molecule + peptide epitope) is important in the development of tumor vaccines.
  • MHC-class-l- binding peptides are usually 8-12 amino acid residues in length and usually contain two conserved residues ("anchors") in their sequence that interact with the corresponding binding groove of the MHC-molecule. In this way each MHC allele has a "binding motif" determining which peptides can bind specifically to the binding groove.
  • TCR T cell bearing specific T cell receptors
  • the antigen should be expressed mainly by tumor cells and not, or in comparably small amounts, by normal healthy tissues.
  • the peptide should be over-presented by tumor cells as compared to normal healthy tissues. It is furthermore desirable that the respective antigen is not only present in a type of tumor, but also in high concentrations (i.e. copy numbers of the respective peptide per cell).
  • Tumor- specific and tumor-associated antigens are often derived from proteins directly involved in transformation of a normal cell to a tumor cell due to their function, e.g. in cell cycle control or suppression of apoptosis.
  • downstream targets of the proteins directly causative for a transformation may be up-regulated und thus may be indirectly tumor-associated.
  • Such indirect tumor-associated antigens may also be targets of a vaccination approach (Singh-Jasuja et al., 2004). It is essential that epitopes are present in the amino acid sequence of the antigen, in order to ensure that such a peptide ("immunogenic peptide"), being derived from a tumor associated antigen, leads to an in vitro or in vivo T-cell-response.
  • any peptide able to bind an MHC molecule may function as a T-cell epitope.
  • a prerequisite for the induction of an in vitro or in vivo T-cell-response is the presence of a T cell having a corresponding TCR and the absence of immunological tolerance for this particular epitope.
  • TAAs are a starting point for the development of a T cell based therapy including but not limited to tumor vaccines.
  • the methods for identifying and characterizing the TAAs are usually based on the use of T-cells that can be isolated from patients or healthy subjects, or they are based on the generation of differential transcription profiles or differential peptide expression patterns between tumors and normal tissues.
  • the identification of genes over-expressed in tumor tissues or human tumor cell lines, or selectively expressed in such tissues or cell lines does not provide precise information as to the use of the antigens being transcribed from these genes in an immune therapy.
  • T cell which upon stimulation with a specific antigen can be clonally expanded and is able to execute effector functions
  • the immunogenicity of the underlying peptides is secondary. In these cases, the presentation is the determining factor.
  • the present invention relates to a peptide comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 1 to SEQ ID NO: 640 or a variant sequence thereof which is at least 77%, preferably at least 88%, homologous (preferably at least 77% or at least 88% identical) to SEQ ID NO: 1 to SEQ ID NO: 640, wherein said variant binds to MHC and/or induces T cells cross-reacting with said peptide, or a pharmaceutical acceptable salt thereof, wherein said peptide is not the underlying full-length polypeptide.
  • the present invention further relates to a peptide of the present invention comprising a sequence that is selected from the group consisting of SEQ ID NO: 1 to SEQ ID NO: 640 or a variant thereof, which is at least 77%, preferably at least 88%, homologous (preferably at least 77% or at least 88% identical) to SEQ ID NO: 1 to SEQ ID NO: 640, wherein said peptide or variant thereof has an overall length of between 8 and 100, preferably between 8 and 30, and most preferred of between 8 and 14 amino acids.
  • the following tables show the peptides according to the present invention, their respective SEQ ID NOs, and the prospective source (underlying) genes for these peptides. All peptides in Table 1 and Table 2 bind to HLA-A*02. The peptides in Table 2 have been disclosed before, e.g. in large listings as results of high-throughput screenings with high error rates or calculated using algorithms, but have not been associated with cancer at all before.
  • the peptides in Table 3 are additional peptides that may be useful in combination with the other peptides of the invention.
  • the peptides in Table 4 are furthermore useful in the diagnosis and/or treatment of various other malignancies that involve an over-expression or over-presentation of the respective underlying polypeptide.
  • the present invention furthermore generally relates to the peptides according to the present invention for use in the treatment of proliferative diseases, such as, for example non-small cell lung cancer, small cell lung cancer, kidney cancer, brain cancer, colon or rectum cancer, stomach cancer, liver cancer, pancreatic cancer, prostate cancer, leukemia, breast cancer, Merkel cell carcinoma, melanoma, esophageal cancer, urinary bladder cancer, uterine cancer, gallbladder cancer, bile duct cancer.
  • proliferative diseases such as, for example non-small cell lung cancer, small cell lung cancer, kidney cancer, brain cancer, colon or rectum cancer, stomach cancer, liver cancer, pancreatic cancer, prostate cancer, leukemia, breast cancer, Merkel cell carcinoma, melanoma, esophageal cancer, urinary bladder cancer, uterine cancer, gallbladder cancer, bile duct cancer.
  • peptide SEQ ID NO. 466 VLIANLEKL
  • VLIANLEKL peptide SEQ ID NO. 466
  • peptide - alone or in combination - according to the present invention selected from the group consisting of SEQ ID NO: 1 , 11 , 427, 408, 198, 512, 519, and 587 and their uses in the immunotherapy of ovarian cancer, non-small cell lung cancer, small cell lung cancer, kidney cancer, brain cancer, colon or rectum cancer, stomach cancer, liver cancer, pancreatic cancer, prostate cancer, leukemia, breast cancer, Merkel cell carcinoma, melanoma, esophageal cancer, urinary bladder cancer, uterine cancer, gallbladder cancer, bile duct cancer, and preferably ovarian cancer.
  • peptide - alone or in combination - selected from the group consisting of SEQ ID NO: 3, 4, 5, 6, 8, 10, 12, 14, 15, 18, 20, 25, 29, 32, 37, 38, 39, 41 , 44, 45, 52, 53, 54, 57, 64, 69, 72, 73, 77, 78, 83, 89, 90, 91 , 93, 94, 96, 99, 100, 102, 104, 106, 107, 109, 113, 114, 117, 120, 123, 124, 136, 137, 138, 139, 141 , 143, 148, 150, 151 , 157, 158, 160, 163, 165, 166, 170, 171 , 173, 175, 179, 180, 184, 185, 187, 189, 191 , 192, 193, 194, 195, 196, 200, 202, 204, 206, 209, 211 , 215, 216,
  • peptides - alone or in combination - selected from the group consisting of SEQ ID NO: 1 to SEQ ID NO: 640. More preferred are the peptides - alone or in combination - selected from the group consisting of SEQ ID NO: 1 to SEQ ID NO: 259 (see Table 1 ), and their uses in the immunotherapy of ovarian cancer, non-small cell lung cancer, small cell lung cancer, kidney cancer, brain cancer, colon or rectum cancer, stomach cancer, liver cancer, pancreatic cancer, prostate cancer, leukemia, breast cancer, Merkel cell carcinoma, melanoma, esophageal cancer, urinary bladder cancer, uterine cancer, gallbladder cancer, bile duct cancer, and preferably ovarian cancer.
  • Table 4A Peptides according to the present invention and their specific uses in other proliferative diseases, especially in other cancerous diseases.
  • the table shows for selected peptides on which additional tumor types they were found and either over- presented on more than 5% of the measured tumor samples, or presented on more than 5% of the measured tumor samples with a ratio of geometric means tumor vs normal tissues being larger than 3. Over-presentation is defined as higher presentation on the tumor sample as compared to the normal sample with highest presentation.
  • adipose tissue adrenal gland, artery, bone marrow, brain, central nerve, colon, duodenum, esophagus, gallbladder, heart, kidney, liver, lung, lymph node, mononuclear white blood cells, pancreas, peripheral nerve, peritoneum, pituitary, pleura, rectum, salivary gland, skeletal muscle, skin, small intestine, spleen, stomach, thymus, thyroid gland, trachea, ureter, urinary bladder, vein.
  • J phospho-serine
  • VLVSDGVHSV SCLC Brain Cancer, BrCa, MCC, Esophageal Cancer
  • SCLC SCLC, CRC, HCC, Leukemia, Melanoma, Esophageal
  • NSCLC NSCLC, SCLC, HCC, Leukemia, Melanoma, Esophageal
  • NSCLC NSCLC
  • SCLC SCLC
  • GC CRC
  • HCC Leukemia
  • NSCLC NSCLC, SCLC, PC, Leukemia, BrCa, Esophageal
  • NSCLC NSCLC, SCLC, CRC, Leukemia, Esophageal Cancer,
  • NSCLC NSCLC, RCC, CRC, HCC, PC, Melanoma, Esophageal
  • NSCLC NSCLC, SCLC, RCC, CRC, HCC, Leukemia, Melanoma,
  • NSCLC NSCLC, SCLC, CRC, PC, Leukemia, Esophageal
  • NSCLC Brain Cancer
  • HCC HCC
  • NSCLC NSCLC
  • SCLC RCC
  • GC GABA
  • PC Leukemia
  • BrCa BrCa
  • NSCLC NSCLC, SCLC, HCC, Melanoma, Esophageal Cancer
  • NSCLC NSCLC, RCC, CRC, HCC, Melanoma, Esophageal
  • NSCLC NSCLC
  • SCLC Uterine Cancer
  • Gallbladder Cancer Bile
  • ALYTGFSILV SCLC Leukemia, Melanoma
  • NSCLC NSCLC, SCLC, PrC, BrCa, Melanoma, Esophageal

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LTEP16733523.1T LT3317296T (lt) 2015-07-01 2016-06-29 Nauji peptidai ir peptidų deriniai, skirti naudoti imunoterapijai nuo kiaušidžių vėžio ir kitų rūšių vėžio
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