CN1810830A - HIV-1 yesisting polypeptide C22, its coding sequence and prepn process - Google Patents
HIV-1 yesisting polypeptide C22, its coding sequence and prepn process Download PDFInfo
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- CN1810830A CN1810830A CNA2005100235421A CN200510023542A CN1810830A CN 1810830 A CN1810830 A CN 1810830A CN A2005100235421 A CNA2005100235421 A CN A2005100235421A CN 200510023542 A CN200510023542 A CN 200510023542A CN 1810830 A CN1810830 A CN 1810830A
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Abstract
The present invention relates to one kind of HIV-1 resisting polypeptide C22, and its expression precursor, coding DNA sequence, monomer polypeptide medicine composite and preparation process. The polypeptide C22 is prepared through expression with fusion protein to obtain the polypeptide precursor, and cleaving the precursor to obtain polypeptide C22. The preparation process is simple, high in final product yield and suitable for industrial production.
Description
Technical field
The present invention relates to the genetically engineered field.More specifically, the present invention relates to a kind of peptide C 22 sequences, its encoding sequence and preparation method of anti-HIV-1.
Background technology
Acquired immune deficiency syndrome (AIDS) (AIDS) is a kind ofly to destroy immune function of human body after invading human body by hiv virus, makes human body that the multiple infection that can not cure and tumour take place, and causes a kind of serious transmissible disease of infected person's death at last.
Since 1985 first routine HIV-positives after China is found, acquired immune deficiency syndrome (AIDS) is the rising tendency of geometricprogression in China, its rising tendency even surpassed Africa.Not only infected person's quantity sharply rises, and the kind of all hiv viruses of whole world discovery all occurs in China.
Why acquired immune deficiency syndrome (AIDS) is rampantly in the whole world, just be directly to invade the human immune system after hiv virus HIV invades human body, amount to the T4 lymphocyte most important among the human immune system, that have offensiveness most that makes on verifying, make body be in the status of forfeiture defence capability at the very start.In a single day hiv virus enters human body, just parasitize most crucial position in the T4 lymphocyte, and integrate in nuclear hereditary material DNA, the human body ability does not make it separately, more unablely kill it, acquired immune deficiency syndrome (AIDS) just becomes the chronic illness of a kind of " disease is gone into gene ".Hiv virus is duplicated with the immunocyte dna replication dna.The breeding of virus and to duplicate be that immunocyte is destroyed and destroys, and emit more virus.New virus of proliferation is infecting more cell.Like this, virus is generation upon generation ofly duplicated, breeding, immunocyte be constantly dead.
Hiv virus is a kind of retrovirus that is different from general virus, has extremely strong rapid variation ability and has caused very big difficulty also for present specifics and vaccine development work.
Mainly comprise grinding the retroviral inhibitor of anti-HIV-1 at present: efabirenz, non-nucleoside reverse transcriptase inhibitor, proteinase inhibitor, HIV CCR5, CXCR4 acceptor inhibitor, HIV GP120 env blocker, disturb inductor, and anti-HIV membrane fusion inhibitor etc.Wherein develop early be to be primarily aimed at enzyme (reversed transcriptive enzyme or the proteolytic enzyme) inhibitor that plays a crucial role in the HIV-1 virus infection, but owing to the viral variants of resistance occurs medicine is, need medicine to keep continual and steady drug effect, and consider medicine potential toxic effect, this has limited the effect of existing inhibitor series clinical treatment greatly.Therefore need exploitation safety energetically, efficiently, interactional newtype drug does not take place with other anti-reverse transcription enzymophathy cytotoxic drugs.
HIV-1 transmembrane protein C end peptide inhibitor suppresses the poisoning intrusion somatocyte at the process of poisoning intrusion cell, belongs to anti-HIV membrane fusion inhibitor.
People such as Wild in 1992 propose the outer synexin gp41 of HIV-1 and have film fusion resistance, find polypeptide N51 (L6) C43, has high thermal stability, N polypeptide and C polypeptide serve as according to design with the aminoacid sequence of HR1, HR2 in the gp41 three end hairpin structures respectively, N polypeptide and C polypeptide come from the stable spiral tripolymer of conformation, anti-phase being arranged in parallel, the centre is connected with one section six hydrophilic amino acid residues (Ser-Gly-Gly-Arg-Gly-Gly).Continuous mutually N36 (L6) C34 and N34 (L6) C28 of proposing such as Bergeron in 1997.
Because C polypeptide and N polypeptide form antiparallel three end hairpin structures, and leptospira structure with seven amino acid repeated arrangement, be positioned at three drain tanks of the common composition of g point, e point of the adjacent N end polypeptide helical surface of hairpin structure inside, these three drain tanks are exactly the interactional with it critical sites of C end polypeptide.The C end polypeptide that present researchist is studied is exactly at these drain tanks design sites designs, its three end hairpin structures with HIV-1 virus gp41 is competed combining, and suppresses the purpose that virus is invaded thereby reach.
Peptide C 22 proposed by the invention, also be to design at the drain tank conformation of HIV-1 virus gp41 three end hairpin structures, can combine with the three end hairpin structures competition of HIV-1 virus gp41, thereby HIV-1 is played important effect in the process of melting the film intrusion, can be used as effective anti-HIV-1 membrane fusion inhibitor.
Summary of the invention
An object of the present invention is to provide a kind of peptide C 22 of isolating anti-HIV-1.
Another object of the present invention provides a kind of this peptide C 22 and expresses precursor.
Another object of the present invention provides the polynucleotide of this peptide C 22 of a kind of separated coding and peptide C 22 expression precursors.
Another object of the present invention provides a kind of pharmaceutical composition that contains the peptide C 22 of separative anti-HIV-1.
Another object of the present invention provides a kind of method that contains the peptide C 22 for preparing isolating anti-HIV-1.
In a first aspect of the present invention, the present invention relates to a kind of isolated polypeptide C22, its aminoacid sequence is the aminoacid sequence shown in the SEQ ID NO:1, is expressed as follows:
Glu?Leu?Asp?Xaa?Trp?Ala?Xaa?Leu?Trp?Asn?Trp?Phe?Asn?Xaa?Thr?Asn
1 5 10 15
Trp?Xaa?Trp?Tyr?Xaa?Lys
20 。
More excellent, peptide C 22 of the present invention, its aminoacid sequence are the aminoacid sequence shown in the SEQ ID NO:2, are expressed as follows:
Glu?Leu?Asp?Lys?Trp?Ala?Ser?Leu?Trp?Asn?Trp?Phe?Asn?Ile?Thr?Asn
1 5 10 15
Trp?Leu?Trp?Tyr?Ile?Lys
20 。
In a second aspect of the present invention, the present invention relates to a kind of peptide C 22 and express precursor, the feature of its aminoacid sequence is to contain peptide C 22 of the present invention and gst fusion protein sequence respectively from aminoterminal to carboxyl terminal.
In a third aspect of the present invention, the present invention relates to a kind of isolating polynucleotide, its peptide C 22 of the present invention of can encoding.
In a fourth aspect of the present invention, the present invention relates to a kind of isolating polynucleotide, its peptide C 22 of the present invention of can encoding is expressed precursor.
In a fifth aspect of the present invention, the present invention relates to a kind of expression vector that codified peptide C 22 of the present invention is expressed precursor that contains.
In a sixth aspect of the present invention, the present invention relates to a kind of can be by above-mentioned expression vector institute transformed host cells.
In a seventh aspect of the present invention, the present invention relates to a kind of peptide C of the present invention 22 of significant quantity pharmaceutically and acceptable pharmaceutical composition pharmaceutically of containing.
In a eighth aspect of the present invention, the present invention relates to a kind of method for preparing peptide C 22 of the present invention that contains, it comprises step:
A) under expression condition, cultivate host cell, described host cell contains the polynucleotide sequence that above-mentioned peptide C 22 is expressed precursor, thus the unit's of giving expression to peptide C 22 is expressed precursor;
B) isolate described monomer peptide C 22 and express precursor;
C) cut described monomer peptide C 22 with the proteolytic enzyme enzyme and express precursor;
D) isolate monomer peptide C 22.
4th, 7,11,14,18,21 amino acids of peptide C 22 of the present invention on aminoacid sequence lay respectively at outside the HIV-1 on the synexin gp41C polypeptide and N polypeptide bonded drain tank, make peptide C 22 of the present invention effectively participate in the three end hairpin structures competition combination of HIV-1 virus gp41, thereby can be used as effective anti-HIV-1 membrane fusion inhibitor.The inventor discovers that the 11st amino acids of peptide C 22 of the present invention must be a tryptophane, and the 4th, 7,14,18,21 amino acids can be arbitrary amino acids, preferably the arbitrary amino acid except Cys, Met.
The inventor is through extensive and deep research, fusion rotein 6ST system expression anti-HIV-1 peptide C 22 is being used in discovery, can simplify the means of production of anti-HIV-1 polypeptide greatly, improves the yield of polypeptide, for example utilize the high expression level amount of GST system to obtain more albumen, and easily separated.
As used herein, " polypeptide of the present invention " refers to anti-HIV-1 peptide C 22, reaches corresponding monomer anti-HIV-1 peptide C 22 expression precursors.
Polypeptide of the present invention can be recombinant polypeptide or synthetic polypeptide, preferred recombinant polypeptide.Polypeptide of the present invention can be the product of chemosynthesis, or uses recombinant technology to produce from protokaryon or eucaryon host (for example, bacterium, yeast, higher plant, insect and mammalian cell).
Polynucleotide of the present invention can be dna form or rna form.DNA can be strand or two strands.
The Nucleotide full length sequence of anti-HIV-1 peptide C 22 of the present invention or its fragment can obtain with the method for pcr amplification method or synthetic usually.The method of at first available synthetic is synthesized relevant sequence, because polypeptide length of the present invention is shorter.
In case obtained relevant sequence, just can come the relevant sequence of large batch of acquisition with recombination method.This normally is cloned into carrier with it, changes cell again over to, separates obtaining relevant sequence then from the host cell after the propagation by ordinary method.
Among the present invention, anti-HIV-1 peptide C 22 nucleotide sequences can be inserted in the recombinant expression vector.Term " recombinant expression vector " refers to bacterial plasmid well known in the art, phage, yeast plasmid, vegetable cell virus, mammalian cell virus or other carriers.In a word, as long as can duplicate in host and stablize, any plasmid and carrier can be used.A key character of expression vector is to contain replication orgin, promotor, marker gene and translation controlling elements usually.
Method well-known to those having ordinary skill in the art can be used to make up and contains anti-HIV-1 peptide C 22 encoding D AN sequences and suitable transcribing/the translate expression vector of control signal.These methods comprise extracorporeal recombinant DNA technology, DNA synthetic technology, the interior recombinant technology of body etc.Described dna sequence dna can effectively be connected on the suitable promotor in the expression vector, and is synthetic to instruct mRNA.The representative plum of these promotors has: colibacillary lac or trp promotor, true and promotor comprise CMV immediate early promoter, HSV thymus gland kinase promoter, early stage and late period the SV40 promotor and some other known may command gene in former expression promoter very and in cell or its virus in partnership.Expression vector also comprises ribosome bind site and the transcription terminator that translation initiation is used.
In addition, expression vector preferably comprises one or more selected marker groups, to be provided for selecting the phenotypic character of transformed host cells, cultivate Tetrahydrofolate dehydrogenase, neomycin resistance and the green fluorescent protein (GFP) of usefulness as eukaryotic cell, or be used for colibacillary tsiklomitsin or amicillin resistance.
Comprise the carrier of above-mentioned suitable dna sequence dna and suitable promotor or control sequence, can be used to transform appropriate host cell, so that it can marking protein.
Host cell can make prokaryotic cell prokaryocyte, as bacterial cell; Or eukaryotic cell such as low, as yeast cell; Or higher eucaryotic cells, as mammalian cell.Representative example has: intestinal bacteria, streptomyces; Eukaryotic cell such as yeast; Vegetable cell; The insect cell of fruit bat S2 or Sf9; Zooblasts such as CHO, COS cell.
Can carry out with the routine techniques that the ability technician knows with the recombinant DNA transformed host cell.When the host for prokaryotic organism such as intestinal bacteria is, the competent cell that can absorb DNA can be used CaCl in exponential growth after date results
2Method is handled, and used step is well-known in this area.Another kind method is to use MgCl
2If desired, transforming also the method for available electroporation carries out.When the host is an eukaryote, can select following DNA transfection method for use: coprecipitation of calcium phosphate method, conventional mechanical method such as microinjection, electroporation, liposome packing etc.
The transformant that obtains can be cultivated with ordinary method, expresses the polypeptide of coded by said gene of the present invention.According to used host cell, used substratum can be selected from various conventional substratum in the cultivation.Under the condition that is suitable for the host cell growth, cultivate.After host cell grows into suitable cell density, induce the promotor of selection with suitable method (as temperature transition or chemical induction), cell is cultivated for some time again.
The extracellular can be expressed or be secreted into to recombinant polypeptide in the above methods in cell or on cytolemma.If desired, can utilize its physics, chemical separating and purifying protein by various separation methods with other characteristics.These methods are well-known to those skilled in the art.The example of these methods includes, but are not limited to: conventional renaturation handles, handle (salt analysis method), centrifugal, the broken bacterium of infiltration, exceed with protein precipitant in, the combination of super centrifugal, sieve chromatography (gel-filtration), adsorption chromatography, ion exchange chromatography, high performance liquid chromatography (HPLC) and other various liquid chromatography (LC) technology and these methods.
In a preference, anti-HIV-1 peptide C 22 of the present invention is to be the formal representation of fusion rotein with monomer anti-HIV-1 peptide C 22 precursors, and then cuts processing through enzyme.Enzyme is cut the back and is cut product with methods such as sieve chromatography separation enzyme, can obtain C22 polypeptide of the present invention.
The present invention also provides a kind of pharmaceutical composition, and it contains the anti-HIV-1 peptide C 22 of the present invention and the pharmaceutically acceptable carrier of safe and effective amount.This class carrier comprises (but being not limited to): salt solution, damping fluid, water, glycerine, ethanol and combination thereof.Pharmaceutical preparation should be complementary with administering mode.In addition, polypeptide of the present invention also can use with the other treatment agent.
The invention has the advantages that:
1) peptide C 22 of the present invention's announcement can effectively participate in the proteic three end hairpin structures competition of HIV-1 virus gp41 combination, thereby can be used as effective anti-HIV-1 membrane fusion inhibitor.
2) monomer peptide C 22 of the present invention can be cut through a step enzyme by monomer peptide C 22 precursors of expressing and obtain.
Description of drawings
The pcr amplification product electrophoresis synoptic diagram of Fig. 1 peptide C 22 of the present invention, wherein be followed successively by thermograde C22PCR product from left to right, 100bpDNAMarker, showing 50-60 ℃ among the figure all has band, less 60,52 and 50 ℃ of band amounts that amplify, the band amount that amplifies about 56 ℃ is bigger.
Fig. 2: 15%SDS-PAGE identifies the GST-C22 fusion rotein synoptic diagram that obtains through expression.
Embodiment
Below in conjunction with specific embodiment, further set forth the present invention.Should be understood that these embodiment only to be used to the present invention is described and be not used in and limit the scope of the invention.The experimental technique of unreceipted actual conditions in the following fact Example is usually according to normal condition.
Material and method
1. enzyme and chemical reagent: Thiadiazolidine isomerase (GST) amalgamation and expression and purification system are available from Pharmacia company; The PCR test kit is available from Takara company; Restriction enzyme and T4 ligase enzyme are available from MBI company; It is Promega company product that DNA reclaims test kit; Proteolytic enzyme Enterokinase is available from NBI company; All the other reagent are homemade analytical pure product.
2. bacterial strain and carrier: intestinal bacteria (E.coli) DH5 α, DH10b, BL21 are this laboratory preservation.Plasmid pGEX-4T-1 is available from Amershem company.
3. carrier DNA, library, primer and determined dna sequence: the widow closes that the thuja acid primer is synthetic gives birth to worker company by Shanghai respectively and lottery industry biotech firm in Shanghai finishes, and determined dna sequence is finished by Shanghai Bo Ya company.
4. instrument: PCR instrument, proteins gel electrophoresis instrument, gel imaging instrument, FPLC are Bio-Rad company product, and HPLC is the Agilent of Agilent company 1100 types
Embodiment 1 peptide C 22 clones' of the present invention preparation
1.1 the acquisition of peptide C 22 nucleotide chains
Design C22 strand oligonucleotide template and forward and reverse primer respectively, obtain C22 nucleotide chain (SEQID NO:3) with the PCR reaction.
Design template and primer are as follows:
Templet?for?C22
5’GAA?TTG?GAT?AAA?TGG?GCG?TCG?CTG?TGG?AAT?TGG?TTT?AAT?ATT?ACC?AAT?TGG?CTG?TGG?TAT
ATT?AAA?3’
5’primer?for?C22(EcoRI)
5’GC?GAA?TTC?GAC?GAC?GAC?GAC?AAA?GAA?TTG?GAT?AAA?TGG?GCG?3’(SEQ?ID?NO：4)。
3’primer?for?C22(XhoI)
5’CCG?CTC?GAG?TTA?TTT?AAT?ATA?CCA?CAG?CCA?3’(SEQ?ID?NO：5)。
(50mM KCl, 10mM Tris-HCl, pH8.3,2.0mM MgCl2,200 μ M dNTPs) add each 100pmole of amplimer in 50 μ l reaction systems.Fully beginning PCR circulation behind the mixing: 95 sex change 1 minute, 94 ℃ of sex change 5 minutes, 55 ℃ or 58 ℃ of annealing 1 minute, 72 ℃ were extended 1 minute, and carried out 30 circulations altogether.At last 72 ℃ of insulations 10 minutes.The PCR product is identified through 2% agarose gel electrophoresis, is used for the clone after the recovery.As shown in Figure 1.
With reference to the intestinal bacteria preference codon, chemosynthesis HIV-1 gp41 C end peptide C 22 nucleotide chains.
1.2 peptide C 22 clones
The C22PCR fragment that obtains is used restriction enzymes double zyme cutting, be connected, use ligase enzyme with the carrier of same double digestion.The carrier that connects transforms as competent cell.The dna fragmentation that will transform joins (50 μ l competent cells need 25ngDNA) in the pipe that competent cell is housed, and volume should not surpass 5% of competent cell, rotates mixing content several times gently.Ice bath 30 minutes; Pipe is put into 42 ℃ of water-baths, regularly 90 seconds heat-shockeds; Fast pipe is transferred to ice bath 90 seconds, made the cell cooling; Every pipe adds 800 μ lLB substratum, and 37 ℃ of slow shaking 45 minutes make the antibiotics resistance marker gene of bacteria resuscitation and expression plasmid coding; Low-speed centrifugal 2 minutes removes supernatant, stays about 100 μ l substratum in Eppendorf tube, resuspended thalline; With glass shop bacterium device that bacterium liquid is even on the agar plate upper berth; Flat board is inverted in 37 ℃ of constant incubators, bacterium colony can occurs after 12-16 hour.The picking positive colony is identified behind the coated plate.
The expression and purification of embodiment 2 peptide Cs 22 of the present invention
The clone who identified shakes bacterium, carries out abduction delivering when the OD value reaches between the 0.5-0.8, induces for 30 degrees centigrade and spends the night, 8000g10 minute collection bacterium.Every 500mL substratum gained thalline adds 20mL2%triton in PBS, 20uLDDT, each 100uL of N,O-Diacetylmuramidase and PMSF.The broken bacterium of power ultrasonic with 500W.Behind the broken bacterium 13000g20 minute centrifugal, get supernatant.The combination of last GlutathioneSepharose 4B post uses 1 * PBS flushing back to use the reduced glutathione wash-out again, then obtains the GST-C22 fusion rotein.As shown in Figure 2.The gained fusion rotein can obtain peptide C 22 after proteolytic enzyme Enterokinase enzyme is cut.
Embodiment 3: peptide C 22 physical and chemical parameters of the present invention
Through SDS-PAGE electrophoresis and standard molecule discharge curve, recording peptide C 22 iso-electric points of the present invention is 6.17.Molecular weight is 2812.22.
Sequence table
＜110〉Tongji University
＜120〉the anti-HIV-1 peptide C 22, its encoding sequence and preparation method thereof
<130>040285
<160>5
<170>PatentIn?version?3.1
<210>1
<211>22
<212>PRT
＜213〉artificial sequence
<220>
<221>misc_feature
<223>4，7，14，18，21
<400>1
Glu?Leu?Asp?Xaa?Trp?Ala?Xaa?Leu?Trp?Asn?Trp?Phe?Asn?Xaa?Thr?Asn
1 5 10 15
Trp?Xaa?Trp?Tyr?Xaa?Lys
20
<210>2
<211>22
<212>PRT
＜213〉artificial sequence
<400>2
Glu?Leu?Asp?Lys?Trp?Ala?Ser?Leu?Trp?Asn?Trp?Phe?Asn?Ile?Thr?Asn
1 5 10 15
Trp?Leu?Trp?Tyr?Ile?Lys
20
<210>3
<211>66
<212>DNA
＜213〉artificial sequence
<400>3
gaattggata?aatgggcgtc?gctgtggaat?tggtttaata?ttaccaattg?gctgtggtat 60
attaaa 66
<210>4
<211>41
<212>DNA
＜213〉primer
<400>4
gcgaattcga?cgacgacgac?aaagaattgg?ataaatgggc?g 41
<210>5
<211>30
<212>DNA
＜213〉primer
<400>5
ccgctcgagt?tatttaatat?accacagcca 30
Claims (9)
1. isolated polypeptide C22, its aminoacid sequence is the aminoacid sequence shown in the SEQ ID NO:1.
2. peptide C 22 according to claim 1, its aminoacid sequence are the aminoacid sequence shown in the SEQ ID NO:2.
3. isolating polynucleotide is characterized in that described polynucleotide encoding claim 1 or 2 described peptide Cs 22.
4. a peptide C 22 is expressed precursor, it is characterized in that, contains claim 1 or 2 described peptide C 22 sequences and gst fusion protein sequences respectively from aminoterminal to carboxyl terminal.
5. isolating polynucleotide is characterized in that the described peptide C 22 expression precursors of described polynucleotide encoding claim 4.
6. an expression vector is characterized in that, it contains the described dna sequence dna of claim 5.
7. a host cell is characterized in that, it is transformed by the described expression vector of claim 6.
8. a pharmaceutical composition is characterized in that, it contains the claim 1 of significant quantity pharmaceutically or 2 described peptide Cs 22 and acceptable carrier pharmaceutically.
9. a method for preparing peptide C 22 is characterized in that, comprises step:
1) under expression condition, cultivate host cell, described host cell contains the described peptide C 22 of coding claim 5 expresses the polynucleotide sequence of precursor, expresses precursor thereby give expression to the described unit of claim 4 peptide C 22;
2) isolate described monomer peptide C 22 and express precursor;
3) cut described monomer peptide C 22 with the proteolytic enzyme enzyme and express precursor;
4) isolate monomer peptide C 22.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CNA2005100235421A CN1810830A (en) | 2005-01-24 | 2005-01-24 | HIV-1 yesisting polypeptide C22, its coding sequence and prepn process |
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|---|---|---|---|
| CNA2005100235421A CN1810830A (en) | 2005-01-24 | 2005-01-24 | HIV-1 yesisting polypeptide C22, its coding sequence and prepn process |
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|---|---|
| CN1810830A true CN1810830A (en) | 2006-08-02 |
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|---|---|---|---|
| CNA2005100235421A Pending CN1810830A (en) | 2005-01-24 | 2005-01-24 | HIV-1 yesisting polypeptide C22, its coding sequence and prepn process |
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Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2009042895A3 (en) * | 2007-09-26 | 2009-09-03 | Dana-Farber Cancer Institute, Inc. | Reagents for inducing an immune response |
| CN101235083B (en) * | 2007-02-02 | 2012-05-23 | 同济大学 | HIV-I resisting polypeptide, coded sequence and use thereof |
| CN101838318B (en) * | 2007-02-02 | 2012-09-05 | 同济大学 | Anti-HIV-I polypeptide and coding sequence and use thereof |
-
2005
- 2005-01-24 CN CNA2005100235421A patent/CN1810830A/en active Pending
Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN101235083B (en) * | 2007-02-02 | 2012-05-23 | 同济大学 | HIV-I resisting polypeptide, coded sequence and use thereof |
| CN101838318B (en) * | 2007-02-02 | 2012-09-05 | 同济大学 | Anti-HIV-I polypeptide and coding sequence and use thereof |
| WO2009042895A3 (en) * | 2007-09-26 | 2009-09-03 | Dana-Farber Cancer Institute, Inc. | Reagents for inducing an immune response |
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