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Displaying record number 503

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MAb ID 50.1 (R/V3-50.1, Fab 50.1)
HXB2 Location gp160(306-310)
DNA(7140..7154)
gp160 Epitope Map
Author Location gp120( MN)
Research Contact Mary White-Scharf, Repligen Corporation, Cambridge, MA
Epitope RIHIG Epitope Alignment
RIHIG epitope logo
Ab Type gp120 V3 // V3 glycan (V3g)
Neutralizing L
Species (Isotype) mouse(IgG1κ)
Patient  
Immunogen vaccine
Keywords antibody binding site, antibody generation, review, structure

Vaccine Details

Vaccine type peptide
Vaccine strain B clade MN
Vaccine component Env V3

Notes

Showing 22 of 22 notes.

References

Showing 23 of 23 references.

Isolation Paper
WhiteScharf1993 M. E. White-Scharf, B. J. Potts, L. M. Smith, K. A. Sokolowski, J. R. Rusche, and S. Silver. Broadly Neutralizing Monoclonal Antibodies to the V3 Region of HIV-1 Can Be Elicited by Peptide Immunization. Virology, 192:197-206, 1993. Using a V3 loop peptide as immunogen, a panel of 50 anti-V3 neutralizing monoclonal antibodies were generated. Four of them were characterized in detail in this paper. PubMed ID: 7685962. Show all entries for this paper.

Berman1997 P. W. Berman, A. M. Gray, T. Wrin, J. C. Vennari, D. J. Eastman, G. R. Nakamura, D. P. Francis, G. Gorse, and D. H. Schwartz. Genetic and Immunologic Characterization of Viruses Infecting MN-rgp120-Vaccinated Volunteers. J. Infect. Dis., 176:384-397, 1997. PubMed ID: 9237703. Show all entries for this paper.

Bou-Habib1994 D. C. Bou-Habib, G. Roderiquez, T. Oravecz, P. W. Berman, P. Lusso, and M. A. Norcross. Cryptic Nature of Envelope V3 Region Epitopes Protects Primary Monocytotropic Human Immunodeficiency Virus Type 1 from Antibody Neutralization. J. Virol., 68:6006-6013, 1994. This paper shows that antibodies to the tip of the V3 loop fail to neutralize primary isolate JR-CSF, and that the V3 loop is far more accessible on the JR-CSF derived T-cell tropic strain T-CSF. Anti-V3 antibodies successfully neutralize T-CSF. Weak binding of anti-V3 antibodies to the primary isolate JR-CSF suggests the V3 loop is accessible only in a minor fraction of proteins. PubMed ID: 8057475. Show all entries for this paper.

DSouza1991 M. P. D'Souza, P. Durda, C. V. Hanson, G. Milman, and Collaborating Investigators. Evaluation of Monoclonal Antibodies to HIV-1 by Neutralization and Serological Assays: An International Collaboration. AIDS, 5:1061-1070, 1991. PubMed ID: 1718320. Show all entries for this paper.

Fontenot1995 J. D. Fontenot, T. C. VanCott, B. S. Parekh, C. P. Pau, J. R. George, D. L. Birx, S. Zolla-Pazner, M. K. Gorny, and J. M. Gatewood. Presentation of HIV V3 Loop Epitopes for Enhanced Antigenicity, Immunogenicity and Diagnostic Potential. AIDS, 9:1121-1129, 1995. PubMed ID: 8519447. Show all entries for this paper.

Ghiara1993 J. B. Ghiara, E. A. Stura, R. L. Stanfield, A. T. Profy, and I. A. Wilson. Crystal Structure of the Principal Neutralization Site of HIV-1. Science, 264:82-85, 1993. Crysal structure of V3 loop peptides bound to Fabs 59.1 and 50.1 was determined. The GPGRAF motif forms a double turn. PubMed ID: 7511253. Show all entries for this paper.

Hoffman1999 T. L. Hoffman, C. C. LaBranche, W. Zhang, G. Canziani, J. Robinson, I. Chaiken, J. A. Hoxie, and R. W. Doms. Stable exposure of the coreceptor-binding site in a CD4-independent HIV-1 envelope protein. Proc. Natl. Acad. Sci. U.S.A., 96(11):6359--64, 25 May 1999. URL: http://www.pnas.org/cgi/content/full/96/11/6359. PubMed ID: 10339592. Show all entries for this paper.

Huang2005 Chih-chin Huang, Min Tang, Mei-Yun Zhang, Shahzad Majeed, Elizabeth Montabana, Robyn L. Stanfield, Dimiter S. Dimitrov, Bette Korber, Joseph Sodroski, Ian A. Wilson, Richard Wyatt, and Peter D. Kwong. Structure of a V3-Containing HIV-1 gp120 Core. Science, 310(5750):1025-1028, 11 Nov 2005. PubMed ID: 16284180. Show all entries for this paper.

LaCasse1998 R. A. LaCasse, K. E. Follis, T. Moudgil, M. Trahey, J. M. Binley, V. Planelles, S. Zolla-Pazner, and J. H. Nunberg. Coreceptor utilization by human immunodeficiency virus type 1 is not a primary determinant of neutralization sensitivity. J. Virol., 72:2491-5, 1998. A T-cell line-adapted (TCLA) derivative of SI primary isolate 168P acquired the ability to to be neutralized by anti-V3 MAbs 257-D, 268-D and 50.1. The primary isolate could use either CCR5 or CXCR4, and was not neutralized when infection was directed via either pathway, but the TCLA derivative uses CXCR4 only and is neutralized. Thus coreceptor usage is not the primary determinant of differential neutralization sensitivity in primary versus TCLA strains. PubMed ID: 9499111. Show all entries for this paper.

Moore1994b J. P. Moore, F. E. McCutchan, S.-W. Poon, J. Mascola, J. Liu, Y. Cao, and D. D. Ho. Exploration of Antigenic Variation in gp120 from Clades A through F of Human Immunodeficiency Virus Type 1 by Using Monoclonal Antibodies. J. Virol., 68:8350-8364, 1994. Four of five anti-V3 MAbs were slightly cross-reactive within clade B, but not very reactive outside clade B. Two discontinuous CD4 binding site Mabs appear to be pan-reactive. Anti-V2 MAbs were only sporadically reactive inside and outside of clade B. PubMed ID: 7525988. Show all entries for this paper.

Pantophlet2008 Ralph Pantophlet, Terri Wrin, Lisa A. Cavacini, James E. Robinson, and Dennis R. Burton. Neutralizing Activity of Antibodies to the V3 Loop Region of HIV-1 gp120 Relative to Their Epitope Fine Specificity. Virology, 381(2):251-260, 25 Nov 2008. PubMed ID: 18822440. Show all entries for this paper.

Park2000 E. J. Park, M. K. Gorny, S. Zolla-Pazner, and G. V. Quinnan. A global neutralization resistance phenotype of human immunodeficiency virus type 1 is determined by distinct mechanisms mediating enhanced infectivity and conformational change of the envelope complex. J. Virol., 74:4183-91, 2000. PubMed ID: 10756031. Show all entries for this paper.

Potts1993 B. J. Potts, K. G. Field, Y. Wu, M. Posner, L. Cavacini, and M. White-Scharf. Synergistic Inhibition of HIV-1 by CD4 Binding Domain Reagents and V3-Directed Monoclonal Antibodies. Virology, 197:415-419, 1993. Four anti-V3 loop MAbs, (59.1, 83.1, 50.1, and 58.2), were evaluated for their affinity, neutralization potencies, and their ability to synergize F105 or sCD4 neutralization. The most important parameter for synergy was the capacity to neutralize a given virus independently. PubMed ID: 8212576. Show all entries for this paper.

Rini1993 J. M. Rini, E. A. Stura, P. A. Salinas, A. T. Profy, and I. A. Wilson. Crystal Structure of a Human Immunodeficiency Virus Type 1 Neutralizing Antibody, 50.1, in Complex with its V3 Loop Peptide Antigen. Proc. Natl. Acad. Sci. U.S.A., 90:6325-6329, 1993. The V3 antigenic site is stretched out, not the $\beta$ turn seen as the primary determinant in other published anti-V3 peptide Fab structures. PubMed ID: 8327513. Show all entries for this paper.

Robert-Guroff1994 M. Robert-Guroff, A. Louie, M. Myagkikh, F. Michaels, M. P. Kieny, M. E. White-Scharf, B. Potts, D. Grogg, and M. S. Reitz, Jr. Alteration of V3 Loop Context within the Envelope of Human Immunodeficiency Virus Type 1 Enhances Neutralization. J. Virol., 68:3459-3466, 1994. MN-V3 loop inserted into a HBX2 background results in enhanced neutralization of anti-MN V3 MAb 50.1 and human HIV+ sera when the chimeric virus was compared to MN. Enhanced affinity, and greater proportions of labeled infected H9 cells by FACS analysis, were also observed using two anti-MN V3 MAbs, 50.1 and 83.1. PubMed ID: 7514675. Show all entries for this paper.

Seligman1996 S. J. Seligman, J. M. Binley, M. K. Gorny, D. R. Burton, S. Zolla-Pazner, and K. A. Sokolowski. Characterization by Serial Deletion Competition ELISAs of HIV-1 V3 Loop Epitopes Recognized by Monoclonal Antibodies. Mol. Immunol., 33:737-745, 1996. PubMed ID: 8811069. Show all entries for this paper.

Sirois2007 Suzanne Sirois, Mohamed Touaibia, Kuo-Chen Chou, and Rene Roy. Glycosylation of HIV-1 gp120 V3 Loop: Towards the Rational Design of a Synthetic Carbohydrate Vaccine. Curr. Med. Chem., 14(30):3232-3242, 2007. PubMed ID: 18220757. Show all entries for this paper.

Stanfield1999 R. Stanfield, E. Cabezas, A. Satterthwait, E. Stura, A. Profy, and I. Wilson. Dual Conformations for the HIV-1 gp120 V3 Loop in Complexes with Different Neutralizing Fabs. Structure, 7:131-142, 1999. PubMed ID: 10368281. Show all entries for this paper.

Stanfield2005 Robyn L. Stanfield and Ian A. Wilson. Structural Studies of Human HIV-1 V3 Antibodies. Hum Antibodies, 14(3-4):73-80, 2005. PubMed ID: 16720977. Show all entries for this paper.

VanCott1994 T. C. VanCott, F. R. Bethke, V. R. Polonis, M. K. Gorny, S. Zolla-Pazner, R. R. Redfield, and D. L. Birx. Dissociation Rate of Antibody-gp120 Binding Interactions Is Predictive of V3-Mediated Neutralization of HIV-1. J. Immunol., 153:449-459, 1994. Using surface plasmon resonance it was found that the rate of the dissociation of the MAb-gp120 complex, but not the association rate, correlated with MAbs ability to neutralize homologous virus (measured by 50\% inhibition of p24 production). Association constants were similar for all MAbs tested, varying less than 4-fold. Dissociation rate constants were quite variable, with 100-fold differences observed. PubMed ID: 7515931. Show all entries for this paper.

VanCott1995 T. C. VanCott, F. R. Bethke, D. S. Burke, R. R. Redfield, and D. L. Birx. Lack of Induction of Antibodies Specific for Conserved, Discontinuous Epitopes of HIV-1 Envelope Glycoprotein by Candidate AIDS Vaccines. J. Immunol., 155:4100-4110, 1995. The Ab response in both HIV-1 infected and uninfected volunteers immunized with HIV-1 rec envelope subunit vaccines (Genentech gp120IIIB, MicroGeneSys gp160IIIB, or ImmunoAG gp160IIIB) preferentially induced Abs reactive only to the denatured form of gp120. This may explain the inability of the vaccinee sera to neutralize primary HIV-1 isolates. PubMed ID: 7561123. Show all entries for this paper.

York2001 J. York, K. E. Follis, M. Trahey, P. N. Nyambi, S. Zolla-Pazner, and J. H. Nunberg. Antibody binding and neutralization of primary and T-cell line-adapted isolates of human immunodeficiency virus type 1. J. Virol., 75(6):2741--52, Mar 2001. URL: http://jvi.asm.org/cgi/content/full/75/6/2741. PubMed ID: 11222697. Show all entries for this paper.

Zhang2002 Peng Fei Zhang, Peter Bouma, Eun Ju Park, Joseph B. Margolick, James E. Robinson, Susan Zolla-Pazner, Michael N. Flora, and Gerald V. Quinnan, Jr. A Variable Region 3 (V3) Mutation Determines a Global Neutralization Phenotype and CD4-Independent Infectivity of a Human Immunodeficiency Virus Type 1 Envelope Associated with a Broadly Cross-Reactive, Primary Virus-Neutralizing Antibody Response. J. Virol., 76(2):644-655, Jan 2002. PubMed ID: 11752155. Show all entries for this paper.


Displaying record number 501

Download this epitope record as JSON.

MAb ID 59.1 (R/V3-59.1)
HXB2 Location gp160(312-317)
DNA(7158..7175)
gp160 Epitope Map
Author Location gp120(308-313 MN)
Research Contact Mary White-Scharf and A. Profy, Repligen Corporation
Epitope GPGRAF Epitope Alignment
GPGRAF epitope logo
Ab Type gp120 V3 // V3 glycan (V3g)
Neutralizing L
Species (Isotype) mouse(IgG1)
Patient  
Immunogen vaccine
Keywords antibody binding site, antibody generation, review, structure

Vaccine Details

Vaccine type peptide
Vaccine strain B clade MN
Vaccine component Env V3

Notes

Showing 15 of 15 notes.

References

Showing 15 of 15 references.

Isolation Paper
WhiteScharf1993 M. E. White-Scharf, B. J. Potts, L. M. Smith, K. A. Sokolowski, J. R. Rusche, and S. Silver. Broadly Neutralizing Monoclonal Antibodies to the V3 Region of HIV-1 Can Be Elicited by Peptide Immunization. Virology, 192:197-206, 1993. Using a V3 loop peptide as immunogen, a panel of 50 anti-V3 neutralizing monoclonal antibodies were generated. Four of them were characterized in detail in this paper. PubMed ID: 7685962. Show all entries for this paper.

DSouza1991 M. P. D'Souza, P. Durda, C. V. Hanson, G. Milman, and Collaborating Investigators. Evaluation of Monoclonal Antibodies to HIV-1 by Neutralization and Serological Assays: An International Collaboration. AIDS, 5:1061-1070, 1991. PubMed ID: 1718320. Show all entries for this paper.

Potts1993 B. J. Potts, K. G. Field, Y. Wu, M. Posner, L. Cavacini, and M. White-Scharf. Synergistic Inhibition of HIV-1 by CD4 Binding Domain Reagents and V3-Directed Monoclonal Antibodies. Virology, 197:415-419, 1993. Four anti-V3 loop MAbs, (59.1, 83.1, 50.1, and 58.2), were evaluated for their affinity, neutralization potencies, and their ability to synergize F105 or sCD4 neutralization. The most important parameter for synergy was the capacity to neutralize a given virus independently. PubMed ID: 8212576. Show all entries for this paper.

Ghiara1993 J. B. Ghiara, E. A. Stura, R. L. Stanfield, A. T. Profy, and I. A. Wilson. Crystal Structure of the Principal Neutralization Site of HIV-1. Science, 264:82-85, 1993. Crysal structure of V3 loop peptides bound to Fabs 59.1 and 50.1 was determined. The GPGRAF motif forms a double turn. PubMed ID: 7511253. Show all entries for this paper.

Bou-Habib1994 D. C. Bou-Habib, G. Roderiquez, T. Oravecz, P. W. Berman, P. Lusso, and M. A. Norcross. Cryptic Nature of Envelope V3 Region Epitopes Protects Primary Monocytotropic Human Immunodeficiency Virus Type 1 from Antibody Neutralization. J. Virol., 68:6006-6013, 1994. This paper shows that antibodies to the tip of the V3 loop fail to neutralize primary isolate JR-CSF, and that the V3 loop is far more accessible on the JR-CSF derived T-cell tropic strain T-CSF. Anti-V3 antibodies successfully neutralize T-CSF. Weak binding of anti-V3 antibodies to the primary isolate JR-CSF suggests the V3 loop is accessible only in a minor fraction of proteins. PubMed ID: 8057475. Show all entries for this paper.

DSouza1994 M. P. D'Souza, S. J. Geyer, C. V. Hanson, R. M. Hendry, G. Milman, and Collaborating Investigators. Evaluation of Monoclonal Antibodies to HIV-1 Envelope by Neutralization and Binding Assays: An International Collaboration. AIDS, 8:169-181, 1994. PubMed ID: 7519019. Show all entries for this paper.

Seligman1996 S. J. Seligman, J. M. Binley, M. K. Gorny, D. R. Burton, S. Zolla-Pazner, and K. A. Sokolowski. Characterization by Serial Deletion Competition ELISAs of HIV-1 V3 Loop Epitopes Recognized by Monoclonal Antibodies. Mol. Immunol., 33:737-745, 1996. PubMed ID: 8811069. Show all entries for this paper.

Ghiara1997 J. B. Ghiara, D. C. Ferguson, A. C. Satterthwait, H. J. Dyson, and I. A. Wilson. Structure-Based Design of a Constrained Peptide Mimic of the HIV-1 V3 Loop Neutralization Site. J. Mol. Biol., 266:31-39, 1997. PubMed ID: 9054968. Show all entries for this paper.

Smith1998 A. D. Smith, S. C. Geisler, A. A. Chen, D. A. Resnick, B. M. Roy, P. J. Lewi, E. Arnold, and G. F. Arnold. Human Rhinovirus Type 14: Human Immunodeficiency Virus Type 1 (HIV-1) V3 Loop Chimeras from a Combinatorial Library Induce Potent Neutralizing Antibody Responses against HIV-1. J. Virol., 72:651-659, 1998. The tip of the MN V3 loop, IGPGRAFYTTKN, was inserted into cold-causing human rhinovirus 14 (HRV14) and chimeras were immunoselected using MAbs 447-52-D, 694/98-D, NM-01, and 59.1, for good presentation of the V3 antigenic region. The selected chimeric viruses were neutralized by anti-V3 loop MAbs. The chimeric viruses elicited potent NAbs against ALA-1 and MN in guinea pigs. PubMed ID: 9420270. Show all entries for this paper.

Stanfield1999 R. Stanfield, E. Cabezas, A. Satterthwait, E. Stura, A. Profy, and I. Wilson. Dual Conformations for the HIV-1 gp120 V3 Loop in Complexes with Different Neutralizing Fabs. Structure, 7:131-142, 1999. PubMed ID: 10368281. Show all entries for this paper.

York2001 J. York, K. E. Follis, M. Trahey, P. N. Nyambi, S. Zolla-Pazner, and J. H. Nunberg. Antibody binding and neutralization of primary and T-cell line-adapted isolates of human immunodeficiency virus type 1. J. Virol., 75(6):2741--52, Mar 2001. URL: http://jvi.asm.org/cgi/content/full/75/6/2741. PubMed ID: 11222697. Show all entries for this paper.

Huang2005 Chih-chin Huang, Min Tang, Mei-Yun Zhang, Shahzad Majeed, Elizabeth Montabana, Robyn L. Stanfield, Dimiter S. Dimitrov, Bette Korber, Joseph Sodroski, Ian A. Wilson, Richard Wyatt, and Peter D. Kwong. Structure of a V3-Containing HIV-1 gp120 Core. Science, 310(5750):1025-1028, 11 Nov 2005. PubMed ID: 16284180. Show all entries for this paper.

Stanfield2005 Robyn L. Stanfield and Ian A. Wilson. Structural Studies of Human HIV-1 V3 Antibodies. Hum Antibodies, 14(3-4):73-80, 2005. PubMed ID: 16720977. Show all entries for this paper.

Sirois2007 Suzanne Sirois, Mohamed Touaibia, Kuo-Chen Chou, and Rene Roy. Glycosylation of HIV-1 gp120 V3 Loop: Towards the Rational Design of a Synthetic Carbohydrate Vaccine. Curr. Med. Chem., 14(30):3232-3242, 2007. PubMed ID: 18220757. Show all entries for this paper.

Pantophlet2008 Ralph Pantophlet, Terri Wrin, Lisa A. Cavacini, James E. Robinson, and Dennis R. Burton. Neutralizing Activity of Antibodies to the V3 Loop Region of HIV-1 gp120 Relative to Their Epitope Fine Specificity. Virology, 381(2):251-260, 25 Nov 2008. PubMed ID: 18822440. Show all entries for this paper.


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