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HIV Molecular Immunology Database

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Found 4 matching records:

Displaying record number 484

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MAb ID M77
HXB2 Location Env(307-320)
DNA(7143..7184)
Env Epitope Map
Author Location gp120( IIIB)
Research Contact Advanced BioScience Laboratories, Rockville, MD, commercial
Epitope IRIQRGPGRAFVTI Epitope Alignment
IRIQRGPGRAFVTI epitope logo
Ab Type gp120 V3 // V3 glycan (V3g)
Neutralizing L
Species (Isotype) human(IgG)
Patient  
Immunogen HIV-1 infection
Keywords antibody binding site, escape, review, vaccine-induced immune responses, variant cross-reactivity

Notes

Showing 11 of 11 notes.

References

Showing 12 of 12 references.

Isolation Paper
Veronese1992 F. di Marzo Veronese, R. Rahman, R. Pal, C. Boyer, J. Romano, V. S. Kalyanaraman, B. C. Nair, R. C. Gallo, and M. G. Sarngadharan. Delineation of immunoreactive, conserved regions in the external envelope glycoprotein of the human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses, 8:1125-1132, 1992. PubMed ID: 1380259. Show all entries for this paper.

Cook1994 D. G. Cook, J. Fantini, S. L. Spitalnik, and F. Gonzalez-Scarano. Binding of Human Immunodeficiency Virus Type 1 HIV-1 gp120 to Galactosylceramide (GalCer): Relationship to the V3 Loop. Virol., 201:206-214, 1994. Antibodies against GalCer can block infection of CD4-negative cells from the brain and colon that are susceptible to HIV infection. This paper explores the ability of a panel of MAbs to inhibit binding of gp120 to GalCer, and also of the binding of GalCer to inhibit MAb-gp120 interaction. MAbs to the V3 loop and GalCer showed mutual inhibition of binding to gp120, and anti-CD4 binding site MAbs showed reduced inhibition. N- and C-terminal MAbs didn't influence GalCer binding. PubMed ID: 8184533. Show all entries for this paper.

Denisova1995 G. Denisova, J. Zwickel, and J. M. Gershoni. Binding of HIV-1 gp120 to an Anti-V3 Loop Antibody Reveals Novel Antigen-Induced Epitopes. FASEB J., 9:127-132, 1995. This paper describes the characterization of five antibodies that bind M77-epitopes that are only revealed upon M77-gp120 interaction. PubMed ID: 7529735. Show all entries for this paper.

Denisova1996 G. Denisova, B. Stern, D. Raviv, J. Zwickel, N. I. Smorodinsky, and J. M. Gershoni. Humoral Immune Response to Immunocomplexed HIV Envelope Glycoprotein 120. AIDS Res. Hum. Retroviruses, 12:901-909, 1996. Mice were injected with the gp120 in different configurations: free, complexed with CD4, and as an immunocomplex bound to a V3 loop MAb (M77) of the protein. Polyclonal sera, as well as monoclonal antibodies produced in each case, were analyzed. The free gp120 and gp120-CD4 complex immunogens stimulated responses were directed mainly toward conformational epitopes, but gp120 immunocomplexed with MAb M77 also produced numerous and varied MAbs directed toward linear epitopes that were presumably inaccessible on the gp120, gp120-CD4 proteins. PubMed ID: 8798975. Show all entries for this paper.

Denisova2000 G. F. Denisova, M. Zerwanitzer, D. A. Denisov, E. Spectorman, I. Mondor, Q. Sattentau, and J. M. Gershoni. Expansion of epitope cross-reactivity by anti-idiotype modulation of the primary humoral response. Mol. Immunol., 37:53-8, 2000. PubMed ID: 10781835. Show all entries for this paper.

Devico1995 A. L. DeVico, R. Rahman, J. Welch, R. Crowley, P. Lusso, M. G. Sarngadharan, and R. Pal. Monoclonal Antibodies Raised against Covalently Crosslinked Complexes of Human Immunodeficiency Virus Type 1 gp120 and CD4 Receptor Identify a Novel Complex-Dependent Epitope on gp120. Virology, 211:583-588, 1995. To explore the immunogenicity of regions of gp120 that are exposed due to conformational changes in gp120 upon CD4 binding, CD4 was covalently linked to gp120 and this complex was used as an immunogen for BALB/c mice. Two MAbs were produced, both of which bind preferentially to the gp120-CD4 complex, and are conformational. Competition assays indicate these MAbs bind to epitopes that are recognized by sera from HIV-1 infected humans. PubMed ID: 7544051. Show all entries for this paper.

Finnegan2002 Catherine M. Finnegan, Werner Berg, George K. Lewis, and Anthony L. DeVico. Antigenic Properties of the Human Immunodeficiency Virus Transmembrane Glycoprotein during Cell-Cell Fusion. J. Virol., 76(23):12123-12134, Dec 2002. PubMed ID: 12414953. Show all entries for this paper.

Gorny2003 Miroslaw K. Gorny and Susan Zolla-Pazner. Human Monoclonal Antibodies that Neutralize HIV-1. In Bette T. M. Korber and et. al., editors, HIV Immunology and HIV/SIV Vaccine Databases 2003. pages 37--51. Los Alamos National Laboratory, Theoretical Biology \& Biophysics, Los Alamos, N.M., 2004. URL: http://www.hiv.lanl.gov/content/immunology/pdf/2003/zolla-pazner_article.pdf. LA-UR 04-8162. Show all entries for this paper.

Pal1992 R. Pal, F. di Marzo Veronese, B. C. Nair, R. Rahman, G. Hoke, S. W. Mumbauer, and M. G. Sarngadharan. Characterization of a Neutralizing Monoclonal Antibody to the External Glycoprotein of HIV-1. Intervirology, 86:86-93, 1992. PubMed ID: 1284059. Show all entries for this paper.

Veronese1993 F. di Marzo Veronese, M. S. Reitz, Jr., G. Gupta, M. Robert-Guroff, C. Boyer-Thompson, A. Louie, R. C. Gallo, and P. Lusso. Loss of a Neutralizing Epitope by a Spontaneous Point Mutation in the V3 Loop of HIV-1 Isolated from an Infected Laboratory Worker. J. Biol. Chem., 268:25894-25901, 1993. The MAb M77 cannot neutralize a virus isolated from a IIIB infected lab-worker that has a single point mutation in the defined linear epitope. M77 cannot bind to the mutant native gp120, but can bind to a peptide that carries the substitution. PubMed ID: 7503990. Show all entries for this paper.

Watkins1993 B. A. Watkins, M. S. Reitz, Jr., C. A. Wilson, K. Aldrich, A. E. Davis, and M. Robert-Guroff. Immune escape by human immunodeficiency virus type 1 from neutralizing antibodies: evidence for multiple pathways. J. Virol., 67:7493-7500, 1993. A neutralization resistance point mutation (HXB2 A281V) was studied using a variety of MAbs, and it was shown that this substitution affects a different epitope than a previously characterized neutralization escape mutant (A582T) (Reitz 1988, Wilson 1990). PubMed ID: 7693973. Show all entries for this paper.

Watkins1996 B. A. Watkins, A. E. Davis, S. Fiorentini, F. di Marzo Veronese, and M. S. Reitz, Jr. Evidence for Distinct Contributions of Heavy and Light Chains to Restriction of Antibody Recognition of the HIV-1 Principal Neutralization Determinant. J. Immunol., 156:1676-1683, 1996. PubMed ID: 8568275. Show all entries for this paper.


Displaying record number 670

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MAb ID 8F101
HXB2 Location Env Env Epitope Map
Author Location gp120
Research Contact Ranajiit Pal, Advanced BioScience Lab, Inc.
Epitope
Ab Type gp120 CD4i, gp120-CD4 complex
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords antibody binding site, antibody generation, kinetics

Vaccine Details

Vaccine type sCD4-gp120 complex
Vaccine strain B clade HXB2
Vaccine component gp120

Notes

Showing 3 of 3 notes.

References

Showing 3 of 3 references.

Isolation Paper
Devico1995 A. L. DeVico, R. Rahman, J. Welch, R. Crowley, P. Lusso, M. G. Sarngadharan, and R. Pal. Monoclonal Antibodies Raised against Covalently Crosslinked Complexes of Human Immunodeficiency Virus Type 1 gp120 and CD4 Receptor Identify a Novel Complex-Dependent Epitope on gp120. Virology, 211:583-588, 1995. To explore the immunogenicity of regions of gp120 that are exposed due to conformational changes in gp120 upon CD4 binding, CD4 was covalently linked to gp120 and this complex was used as an immunogen for BALB/c mice. Two MAbs were produced, both of which bind preferentially to the gp120-CD4 complex, and are conformational. Competition assays indicate these MAbs bind to epitopes that are recognized by sera from HIV-1 infected humans. PubMed ID: 7544051. Show all entries for this paper.

Finnegan2001 Catherine M. Finnegan, Werner Berg, George K. Lewis, and Anthony L. DeVico. Antigenic Properties of the Human Immunodeficiency Virus Envelope during Cell-Cell Fusion. J. Virol., 75(22):11096-11105, Nov 2001. PubMed ID: 11602749. Show all entries for this paper.

Finnegan2002 Catherine M. Finnegan, Werner Berg, George K. Lewis, and Anthony L. DeVico. Antigenic Properties of the Human Immunodeficiency Virus Transmembrane Glycoprotein during Cell-Cell Fusion. J. Virol., 76(23):12123-12134, Dec 2002. PubMed ID: 12414953. Show all entries for this paper.


Displaying record number 671

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MAb ID 8F102
HXB2 Location Env Env Epitope Map
Author Location gp120
Epitope
Ab Type gp120-CD4 complex
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type sCD4-gp120 complex
Vaccine strain B clade HXB2
Vaccine component gp120

Notes

Showing 1 of 1 note.

References

Showing 1 of 1 reference.

Devico1995 A. L. DeVico, R. Rahman, J. Welch, R. Crowley, P. Lusso, M. G. Sarngadharan, and R. Pal. Monoclonal Antibodies Raised against Covalently Crosslinked Complexes of Human Immunodeficiency Virus Type 1 gp120 and CD4 Receptor Identify a Novel Complex-Dependent Epitope on gp120. Virology, 211:583-588, 1995. To explore the immunogenicity of regions of gp120 that are exposed due to conformational changes in gp120 upon CD4 binding, CD4 was covalently linked to gp120 and this complex was used as an immunogen for BALB/c mice. Two MAbs were produced, both of which bind preferentially to the gp120-CD4 complex, and are conformational. Competition assays indicate these MAbs bind to epitopes that are recognized by sera from HIV-1 infected humans. PubMed ID: 7544051. Show all entries for this paper.


Displaying record number 687

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MAb ID M90
HXB2 Location Env Env Epitope Map
Author Location gp120( IIIB)
Research Contact Fulvia di Marzo Veronese
Epitope (Discontinuous epitope)
Subtype B
Ab Type gp120 C1
Neutralizing no
Species (Isotype) (IgG1)
Patient  
Immunogen vaccine
Keywords antibody binding site

Vaccine Details

Vaccine type protein
Vaccine component Env

Notes

Showing 9 of 9 notes.

References

Showing 11 of 11 references.

Isolation Paper
Veronese1992 F. di Marzo Veronese, R. Rahman, R. Pal, C. Boyer, J. Romano, V. S. Kalyanaraman, B. C. Nair, R. C. Gallo, and M. G. Sarngadharan. Delineation of immunoreactive, conserved regions in the external envelope glycoprotein of the human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses, 8:1125-1132, 1992. PubMed ID: 1380259. Show all entries for this paper.

Binley1998 J. M. Binley, R. Wyatt, E. Desjardins, P. D. Kwong, W. Hendrickson, J. P. Moore, and J. Sodroski. Analysis of the Interaction of Antibodies with a Conserved Enzymatically Deglycosylated Core of the HIV Type 1 Envelope Glycoprotein 120. AIDS Res. Hum. Retroviruses, 14:191-198, 1998. This paper helped showed the biological relevance of a deglycosylated variable loop deleted form of the core gp120. PubMed ID: 9491908. Show all entries for this paper.

Binley2000 J. Binley, R. Sanders, B. Clas, N. Schuelke, A. Master, Y. Guo, F. Kajumo, D. Anselma, P. Maddon, W. Olson, and J. Moore. A Recombinant Human Immunodeficiency virus type 1 envelope glycoprotein complex stabilized by an intramolecular disulfide bond between the gp120 and gp41 subunits is an antigenic mimic of the trimeric virion associated structure. J. Virol., 74:627-43, 1999. PubMed ID: 10623724. Show all entries for this paper.

Devico1995 A. L. DeVico, R. Rahman, J. Welch, R. Crowley, P. Lusso, M. G. Sarngadharan, and R. Pal. Monoclonal Antibodies Raised against Covalently Crosslinked Complexes of Human Immunodeficiency Virus Type 1 gp120 and CD4 Receptor Identify a Novel Complex-Dependent Epitope on gp120. Virology, 211:583-588, 1995. To explore the immunogenicity of regions of gp120 that are exposed due to conformational changes in gp120 upon CD4 binding, CD4 was covalently linked to gp120 and this complex was used as an immunogen for BALB/c mice. Two MAbs were produced, both of which bind preferentially to the gp120-CD4 complex, and are conformational. Competition assays indicate these MAbs bind to epitopes that are recognized by sera from HIV-1 infected humans. PubMed ID: 7544051. Show all entries for this paper.

Ditzel1997 H. J. Ditzel, P. W. Parren, J. M. Binley, J. Sodroski, J. P. Moore, C. F. Barbas, III, and D. R. Burton. Mapping the Protein Surface of Human Immunodeficiency Virus Type 1 gp120 Using Human Monoclonal Antibodies from Phage Display Libraries. J. Mol. Biol., 267:684-695, 1997. (Genbank: U82767 U82768 U82769 U82770 U82771 U82772 U82942 U82943 U82944 U82945 U82946 U82947 U82948 U82949 U82950 U82951 U82952 U82961 U82962) Recombinant monoclonal antibodies from phage display libraries provide a method for Env surface epitope mapping. Diverse epitopes are accessed by presenting gp120 to the library in different forms, such as sequential masking of epitopes with existing MAbs or sCD4 prior to selection or by selection on peptides. Fabs identified by these methods have specificities associated with epitopes presented poorly on native multimeric envelope. PubMed ID: 9126846. Show all entries for this paper.

Koefoed2005 Klaus Koefoed, Lauge Farnaes, Meng Wang, Arne Svejgaard, Dennis R. Burton, and Henrik J. Ditzel. Molecular Characterization of the Circulating Anti-HIV-1 gp120-Specific B Cell Repertoire using Antibody Phage Display Libraries Generated from Pre-Selected HIV-1 gp120 Binding PBLs. J. Immunol. Methods, 297(1-2):187-201, Feb 2005. PubMed ID: 15777942. Show all entries for this paper.

Moore1996 J. P. Moore and J. Sodroski. Antibody cross-competition analysis of the human immunodeficiency virus type 1 gp120 exterior envelope glycoprotein. J. Virol., 70:1863-1872, 1996. 46 anti-gp120 monomer MAbs were used to create a competition matrix, and MAb competition groups were defined. The data suggests that there are two faces of the gp120 glycoprotein: a face occupied by the CD4BS, which is presumably also exposed on the oligomeric envelope glycoprotein complex, and a second face which is presumably inaccessible on the oligomer and interacts with a number of nonneutralizing antibodies. PubMed ID: 8627711. Show all entries for this paper.

Pantophlet2003b Ralph Pantophlet, Ian A. Wilson, and Dennis R. Burton. Hyperglycosylated Mutants of Human Immunodeficiency Virus (HIV) Type 1 Monomeric gp120 as Novel Antigens for HIV Vaccine Design. J. Virol., 77(10):5889-8901, May 2003. PubMed ID: 12719582. Show all entries for this paper.

Veronese1993 F. di Marzo Veronese, M. S. Reitz, Jr., G. Gupta, M. Robert-Guroff, C. Boyer-Thompson, A. Louie, R. C. Gallo, and P. Lusso. Loss of a Neutralizing Epitope by a Spontaneous Point Mutation in the V3 Loop of HIV-1 Isolated from an Infected Laboratory Worker. J. Biol. Chem., 268:25894-25901, 1993. The MAb M77 cannot neutralize a virus isolated from a IIIB infected lab-worker that has a single point mutation in the defined linear epitope. M77 cannot bind to the mutant native gp120, but can bind to a peptide that carries the substitution. PubMed ID: 7503990. Show all entries for this paper.

Wyatt1997 R. Wyatt, E. Desjardin, U. Olshevsky, C. Nixon, J. Binley, V. Olshevsky, and J. Sodroski. Analysis of the Interaction of the Human Immunodeficiency Virus Type 1 gp120 Envelope Glycoprotein with the gp41 Transmembrane Glycoprotein. J. Virol., 71:9722-9731, 1997. This study characterized the binding of gp120 and gp41 by comparing Ab reactivity to soluble gp120 and to a soluble complex of gp120 and gp41 called sgp140. The occlusion of gp120 epitopes in the sgp140 complex provides a guide to the gp120 domains that interact with gp41, localizing them in C1 and C5 of gp120. Mutations that disrupt the binding of the occluded antibodies do not influence NAb binding or CD4 binding, thus if the gp41 binding domain is deleted, the immunologically desirable features of gp120 for vaccine design are still intact. PubMed ID: 9371638. Show all entries for this paper.

Yang2000 Xinzhen Yang, Michael Farzan, Richard Wyatt, and Joseph Sodroski. Characterization of Stable, Soluble Trimers Containing Complete Ectodomains of Human Immunodeficiency Virus Type 1 Envelope Glycoproteins. J. Virol., 74(12):5716-5725, Jun 2000. PubMed ID: 10823881. Show all entries for this paper.


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