HIV molecular immunology database

 

Search Antibody Database

Found 1 matching record:

Displaying record number 466

Download this epitope record as JSON.

MAb ID DO142-10 (DO 142-10, DO142)
HXB2 Location gp160(305-320)
DNA(7137..7184)
gp160 Epitope Map
Author Location gp120( MN)
Epitope KRIHIGPGRAFYTT Epitope Alignment
KRIHIGPGRAFYTT epitope logo
Ab Type gp120 V3 // V3 glycan (V3g)
Neutralizing L
Species (Isotype) human(IgG1)
Patient  
Immunogen HIV-1 infection
Keywords antibody binding site, antibody generation, antibody sequence, binding affinity, enhancing activity, review, variant cross-reactivity

Notes

Showing 11 of 11 notes.

References

Showing 11 of 11 references.

Isolation 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.

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.

Parren1997 P. W. Parren, M. C. Gauduin, R. A. Koup, P. Poignard, Q. J. Sattentau, P. Fisicaro, and D. R. Burton. Erratum to Relevance of the Antibody Response against Human Immunodeficiency Virus Type 1 Envelope to Vaccine Design. Immunol. Lett., 58:125-132, 1997. corrected and republished article originally printed in Immunol. Lett. 1997 Jun;57(1-3):105-112. PubMed ID: 9271324. Show all entries for this paper.

Parren1997c P. W. Parren and D. Burton. Antibodies Against HIV-1 from Phage Display Library: Mapping of an Immune Response and Progress toward Antiviral Immunotherapy. Chem. Immunol., 65:18-56, 1997. Editor, J. D. Capra. An excellent review of the potential for antiviral immune therapy using anti-HIV human monoclonal antibodies, emphasizing phage display library technology, and application to HIV. Fabs to gp120 and gp41 are summarized. The methodology of selection for enhanced affinity is discussed, and affinity shown to be related to neutralization. Fabs expressed in phage display libraries were generally converted to IgG molecules only if they show neutralization potential in vitro, and this conversion to an IgG enhances neutralizing potential for immunotherapeutics. The use of phage display libraries to assess vaccines is discussed. gp120, gp160 and gp140-oligomeric vaccines were compared as antigen for selection from phage display libraries. Despite the fact that CD4BS, V3 loop, and CD4BS-V2 loop directed Abs were obtained in vaccinees, none of these vaccines efficiently selected neutralizing Abs from long-term asymptomatic donors in phage display libraries. The protein with the best potential using this method was found to be native oligomeric HIV-1 Envelope expressed on infected cells. The possibility of using 2G12, IgG1 b12 and 2F5 in combination for immunotherapy is discussed. PubMed ID: 9018871. Show all entries for this paper.

Parren1998 P. W. Parren, I. Mondor, D. Naniche, H. J. Ditzel, P. J. Klasse, D. R. Burton, and Q. J. Sattentau. Neutralization of human immunodeficiency virus type 1 by antibody to gp120 is determined primarily by occupancy of sites on the virion irrespective of epitope specificity. J. Virol., 72:3512-9, 1998. The authors propose that the occupancy of binding sites on HIV-1 virions is the major factor in determining neutralization, irrespective of epitope specificity. Neutralization was assayed T-cell-line-adapted HIV-1 isolates. Binding of Fabs to monomeric rgp120 was not correlated with binding to functional oligomeric gp120 or neutralization, while binding to functional oligomeric gp120 was highly correlated with neutralization. The ratios of oligomer binding/neutralization were similar for antibodies to different neutralization epitopes, with a few exceptions. PubMed ID: 9557629. Show all entries for this paper.

Sullivan1998b N. Sullivan, Y. Sun, J. Binley, J. Lee, C. F. Barbas III, P. W. H. I. Parren, D. R. Burton, and J. Sodroski. Determinants of human immunodeficiency virus type 1 envelope glycoprotein activation by soluble CD4 and monoclonal antibodies. J. Virol., 72:6332-8, 1998. PubMed ID: 9658072. Show all entries for this paper.

Kwong2002 Peter D. Kwong, Michael L. Doyle, David J. Casper, Claudia Cicala, Stephanie A. Leavitt, Shahzad Majeed, Tavis D. Steenbeke, Miro Venturi, Irwin Chaiken, Michael Fung, Hermann Katinger, Paul W. I. H. Parren, James Robinson, Donald Van Ryk, Liping Wang, Dennis R. Burton, Ernesto Freire, Richard Wyatt, Joseph Sodroski, Wayne A. Hendrickson, and James Arthos. HIV-1 Evades Antibody-Mediated Neutralization through Conformational Masking of Receptor-Binding Sites. Nature, 420(6916):678-682, 12 Dec 2002. Comment in Nature. 2002 Dec 12;420(6916):623-4. PubMed ID: 12478295. 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.

McCann2005 C. M. Mc Cann, R. J. Song, and R. M. Ruprecht. Antibodies: Can They Protect Against HIV Infection? Curr. Drug Targets Infect. Disord., 5(2):95-111, Jun 2005. PubMed ID: 15975016. Show all entries for this paper.

Kramer2007 Victor G. Kramer, Nagadenahalli B. Siddappa, and Ruth M. Ruprecht. Passive Immunization as Tool to Identify Protective HIV-1 Env Epitopes. Curr. HIV Res., 5(6):642-55, Nov 2007. PubMed ID: 18045119. 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