HIV molecular immunology database

 

Search Antibody Database

Found 3 matching records:

Displaying record number 431

Download this epitope record as JSON.

MAb ID 178.1 (178.1.1)
HXB2 Location gp160(305-309)
DNA(7137..7151)
gp160 Epitope Map
Author Location gp120(305-309 BH10)
Research Contact C. Thiriart, Smith Kline and MRC AIDS reagent project
Epitope KSIRI Epitope Alignment
KSIRI epitope logo
Ab Type gp120 V3 // V3 glycan (V3g)
Neutralizing L
Species (Isotype) mouse(IgG2a)
Patient  
Immunogen vaccine
Keywords antibody binding site, antibody interactions, contact residues, dendritic cells, neutralization, novel epitope, optimal epitope

Vaccine Details

Vaccine type protein
Vaccine strain B clade IIIB
Vaccine component Env

Notes

Showing 7 of 7 notes.

References

Showing 6 of 6 references.

Back1993 N. K. T. Back, L. Smit, M. Schutten, P. L. Nara, M. Tersmette, and J. Goudsmit. Mutations in Human Immunodeficiency Virus Type 1 gp41 Affect Sensitivity to Neutralization by gp120 Antibodies. J. Virol., 67:6897-6902, 1993. Three closely related clones were derived from a neutralization resistant IIIB isolate that had been passaged in a chimpanzee. gp41 mutations were shown to profoundly alter the ability of V3 loop MAbs 5023 and 178.1 to neutralize. Critical substitutions in gp41 were 668 and 675, close to the immunogenic domain 662-668, or ELDKWAS. Less profound inhibition was observed for the anti-CD4 binding site MAb GP13. PubMed ID: 8411395. 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.

Holl2006 Vincent Holl, Maryse Peressin, Thomas Decoville, Sylvie Schmidt, Susan Zolla-Pazner, Anne-Marie Aubertin, and Christiane Moog. Nonneutralizing Antibodies Are Able To Inhibit Human Immunodeficiency Virus Type 1 Replication in Macrophages and Immature Dendritic Cells. J. Virol., 80(12):6177-6181, Jun 2006. PubMed ID: 16731957. Show all entries for this paper.

Langedijk1992 J. P. M. Langedijk, N. K. T. Back, E. Kinney-Thomas, C. Bruck, M. Francotte, J. Goudsmit, and R. H. Meloen. Comparison and Fine Mapping of Both High and Low Neutralizing Monoclonal Antibodies against the Principal Neutralization Domain of HIV-1. Arch. Virol., 126:129-146, 1992. PubMed ID: 1381908. Show all entries for this paper.

Moore1993a J. P. Moore and D. D. Ho. Antibodies to discontinuous or conformationally sensitive epitopes on the gp120 glycoprotein of human immunodeficiency virus type 1 are highly prevalent in sera of infected humans. J. Virol., 67:863-875, 1993. CD4BS antibodies are prevalent in HIV-1-positive sera, while neutralizing MAbs to C4, V2, and V3 and MAbs to linear epitopes are less common. Most linear epitope MAbs in human sera are directed against the V3 region, and cross-reactive MAbs tend to be directed against discontinuous epitopes. PubMed ID: 7678308. Show all entries for this paper.

Thiriart1989 C. Thiriart, M. Francotte, J. Cohen, C. Collignon, A. Delers, S. Kummert, C. Molitor, D. Gilles, P. Roelants, F. Van Wijnendaele, M. De Wilde, and C. Bruck. Several Antigenic Determinants Exposed on the gp120 Moiety of HIV-1 gp160 Are Hidden on the Mature gp120. J. Immunol., 143:1832-1836, 1989. PubMed ID: 2476484. Show all entries for this paper.


Displaying record number 430

Download this epitope record as JSON.

MAb ID 5023A (5023, NEA-9205, NEA 9205)
HXB2 Location gp160(311-317)
DNA(7155..7175)
gp160 Epitope Map
Author Location gp120(311-317 BH10)
Research Contact Paul Durda, Du Pont de Nemours and Co
Epitope RGPGRAF Epitope Alignment
RGPGRAF epitope logo
Ab Type gp120 V3 // V3 glycan (V3g)
Neutralizing L
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords antibody binding site, antibody generation, binding affinity

Vaccine Details

Vaccine type peptide
Vaccine strain B clade BH10
Vaccine component Env V3

Notes

Showing 5 of 5 notes.

References

Showing 5 of 5 references.

Back1993 N. K. T. Back, L. Smit, M. Schutten, P. L. Nara, M. Tersmette, and J. Goudsmit. Mutations in Human Immunodeficiency Virus Type 1 gp41 Affect Sensitivity to Neutralization by gp120 Antibodies. J. Virol., 67:6897-6902, 1993. Three closely related clones were derived from a neutralization resistant IIIB isolate that had been passaged in a chimpanzee. gp41 mutations were shown to profoundly alter the ability of V3 loop MAbs 5023 and 178.1 to neutralize. Critical substitutions in gp41 were 668 and 675, close to the immunogenic domain 662-668, or ELDKWAS. Less profound inhibition was observed for the anti-CD4 binding site MAb GP13. PubMed ID: 8411395. 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.

Langedijk1991 J. P. M. Langedijk, N. K. T. Back, P. J. Durda, J. Goudsmit, and R. H. Meloen. Neutralizing activity of anti-peptide antibodies against the principal neutralization domain of human immunodeficiency virus type 1. J. Gen. Virol., 72:2519-2526, 1991. MAbs were raised against RIQRGPGRAFVTIGK by immunizing mice. Fine structure of MAb binding sites was mapped using pepscan. Preservation of the $\beta$ turn at the tip of the loop was critical. PubMed ID: 1919529. Show all entries for this paper.

Rovinski1995 B. Rovinski, L. Rodrigues, S. X. Cao, F. L. Yao, U. McGuinness, C. Sia, G. Cates, S. Zolla-Pazner, S. Karwowska, T. J. Matthews, C. B. McDanal, J. Mascola, and M. H. Klein. Induction of HIV Type 1 Neutralizing and Env-CD4 Blocking Antibodies by Immunization with Genetically Engineered HIV Type 1-Like Particles Containing Unprocessed gp160 Glycoproteins. AIDS Res. Hum. Retroviruses, 11:1187-1195, 1995. PubMed ID: 8573374. Show all entries for this paper.

Schonning1998 K. Schonning, A. Bolmstedt, J. Novotny, O. S. Lund, S. Olofsson, and J. E. Hansen. Induction of Antibodies against Epitopes Inaccessible on the HIV Type 1 Envelope Oligomer by Immunization with Recombinant Monomeric Glycoprotein 120. AIDS Res. Hum. Retroviruses, 14:1451-1456, 1998. PubMed ID: 9824323. Show all entries for this paper.


Displaying record number 621

Download this epitope record as JSON.

MAb ID GP13 (ARP3054)
HXB2 Location Env Env Epitope Map
Author Location gp120
Epitope
Ab Type gp120 CD4BS
Neutralizing L
Species (Isotype) human(IgG1)
Patient 1171
Immunogen HIV-1 infection
Keywords antibody binding site, antibody interactions, antibody sequence, assay or method development, binding affinity, enhancing activity, escape, review, subtype comparisons, variant cross-reactivity

Notes

Showing 12 of 12 notes.

References

Showing 12 of 12 references.

Isolation Paper
Schutten1993 M. Schutten, A. McKnight, R. C. Huisman, M. Thali, J. A. McKeating, J. Sodroski, J. Goudsmit, and A. D. Osterhaus. Further Characterization of an Antigenic Site of HIV-1 gp120 Recognized by Virus Neutralizing Human Monoclonal Antibodies. AIDS, 7:919-923, 1993. Three human anti-CD4 binding site MAbs were characterized. Amino acid substitutions that block MAb binding were similar but slightly different than those found in murine anti-CD4 binding site MAbs. PubMed ID: 7689324. Show all entries for this paper.

Back1993 N. K. T. Back, L. Smit, M. Schutten, P. L. Nara, M. Tersmette, and J. Goudsmit. Mutations in Human Immunodeficiency Virus Type 1 gp41 Affect Sensitivity to Neutralization by gp120 Antibodies. J. Virol., 67:6897-6902, 1993. Three closely related clones were derived from a neutralization resistant IIIB isolate that had been passaged in a chimpanzee. gp41 mutations were shown to profoundly alter the ability of V3 loop MAbs 5023 and 178.1 to neutralize. Critical substitutions in gp41 were 668 and 675, close to the immunogenic domain 662-668, or ELDKWAS. Less profound inhibition was observed for the anti-CD4 binding site MAb GP13. PubMed ID: 8411395. Show all entries for this paper.

Bagley1994 J. Bagley, P. J. Dillon, C. Rosen, J. Robinson, J. Sodroski, and W. A. Marasco. Structural Characterization of Broadly Neutralizing Human Monoclonal Antibodies Against the CD4 Binding Site of HIV-1 gp120. Mol. Immunol., 31(15):1149-1160, 1994. This paper is a detailed study of the V-D-J heavy chain usage and V-J light chain usage for the three monoclonals that bind to the HIV-1 envelope CD4 binding site: F105, 15e and 21h. Different germline genes were used, and there was evidence for antigen-drive clonal selection of somatic mutations. Eight positions in the heavy chain and two in the light chain complementarity determining positions were identical in the three Mabs. PubMed ID: 7935503. Show all entries for this paper.

Bolmstedt1996 A. Bolmstedt, S. Sjolander, J. E. Hansen, L. Akerblom, A. Hemming, S. L. Hu, B. Morein, and S. Olofsson. Influence of N-Linked Glycans in V4-V5 Region of Human Immunodeficiency Virus Type 1 Glycoprotein gp160 on Induction of a Virus-Neutralizing Humoral Response. J. Acquir. Immune Defic. Syndr. Hum. Retrovirol., 12:213-220, 1996. Because N-linked glycans on viral glycoproteins can protect otherwise accessible neutralization epitopes of the viral envelope from neutralizing antibodies, the aim of this study was to explore the possibility of achieving a more broadly neutralizing immune response with a gp160 depleted of three N-linked glycans in the CD4-binding domain. Mutant and wild type gp160 were formulated into immunostimulating complexes (iscoms), and guinea pigs were vaccinated. Both preparations induced high serum antibody response to native gp120 and V3 peptides. The sera from animals immunized with the mutated glycoprotein lacking CD4 glycosylation sites did not neutralize nonrelated HIV strains better than did sera from animals immunized with wild type glycoprotein, but animals immunized with mutant gp160 neutralized mutant virus better than wild type virus, and vice versa. PubMed ID: 8673525. 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.

Schutten1995 M. Schutten, A. C. Andeweg, M. L. Bosch, and A. D. Osterhaus. Enhancement of Infectivity of a Non-Syncytium Inducing HIV-1 by sCD4 and by Human Antibodies that Neutralize Syncytium Inducing HIV-1. Scand. J. Immunol., 41:18-22, 1995. PubMed ID: 7824885. Show all entries for this paper.

Schutten1995a M. Schutten, J. P. Langedijk, A. C. Andeweg, R. C. Huisman, R. H. Meloen, and A. D. Osterhaus. Characterization of a V3 Domain-Specific Neutralizing Human Monoclonal Antibody That Preferentially Recognizes Non-Syncytium-Inducing Human Immunodeficiency Virus Type 1 Strains. J. Gen. Virol., 76:1665-1673, 1995. Characterization of HuMAb MN215. PubMed ID: 9049372. Show all entries for this paper.

Schutten1996 M. Schutten, K. Tenner-Racz, P. Racz, D. W. van Bekkum, and A. D. Osterhaus. Human antibodies that neutralize primary human immunodeficiency virus type 1 in vitro do not provide protection in an in vivo model. J. Gen. Virol., 77:1667-75, Aug 1996. PubMed ID: 8760413. Show all entries for this paper.

Schutten1997 M. Schutten, A. C. Andeweg, G. F. Rimmelzwaan, and A. D. Osterhaus. Modulation of primary human immunodeficiency virus type 1 envelope glycoprotein-mediated entry by human antibodies. J. Gen. Virol., 78:999-1006, 1997. A series of HIV-1 envelope glycoproteins from related primary virus isolates of different SI phenotypes, together with chimeras of these proteins, were tested in an envelope trans-complementation assay for their sensitivity to either antibody mediated inhibition or enhancement of HIV-1 entry. In contrast to the inhibition of HIV-1 entry, antibody mediated enhancement was not temperature dependent and could not be mediated by F(ab) fragments, implicating cross-linking as an important step. Enhancement or inhibition seemed to be determined by virus isolate rather than by the specificity of the antiserum used. 2F5 was the only MAb that inhibited the entry of all viruses. PubMed ID: 9152416. Show all entries for this paper.

Vella2002 Cherelyn Vella, Natalie N. Zheng, Philippa Easterbrook, and Rod S. Daniels. Herpesvirus saimiri-Immortalized Human Lymphocytes: Novel Hosts for Analyzing HIV Type 1 in Vitro Neutralization. AIDS Res. Hum. Retroviruses, 18(13):933-946, 1 Sep 2002. PubMed ID: 12230936. Show all entries for this paper.

Wisnewski1996 A. Wisnewski, L. Cavacini, and M. Posner. Human antibody variable region gene usage in HIV-1 infection. J. Acquir. Immune Defic. Syndr. Hum. Retrovirol., 11:31-38, 1996. PubMed ID: 8528730. Show all entries for this paper.

Gorny2009 Miroslaw K. Gorny, Xiao-Hong Wang, Constance Williams, Barbara Volsky, Kathy Revesz, Bradley Witover, Sherri Burda, Mateusz Urbanski, Phillipe Nyambi, Chavdar Krachmarov, Abraham Pinter, Susan Zolla-Pazner, and Arthur Nadas. Preferential Use of the VH5-51 Gene Segment by the Human Immune Response to Code for Antibodies against the V3 Domain of HIV-1. Mol. Immunol., 46(5):917-926, Feb 2009. PubMed ID: 18952295. Show all entries for this paper.


Questions or comments? Contact us at immuno@lanl.gov
 
Managed by Triad National Security, LLC for the U.S. Department of Energy’s National Nuclear Security Administration
Copyright © 2022 Triad National Security, LLC | Disclaimer/Privacy

Dept of Health & Human Services Los Alamos National Institutes of Health