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Displaying record number 2031

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MAb ID 3B3 (Fab 3B3)
HXB2 Location Env Env Epitope Map
Author Location gp120
Research Contact Dennis Burton, Scripps, San Diego, CA, USA
Epitope
Ab Type gp120 CD4BS
Neutralizing L P
Species (Isotype)  
Patient Donor b
Immunogen in vitro stimulation or selection
Keywords antibody generation, binding affinity, glycosylation, immunotoxin, neutralization, structure

Notes

Showing 5 of 5 notes.

References

Showing 6 of 6 references.

Isolation Paper
Barbas1994 Carlos F. Barbas, III, Dana Hu, Nancy Dunlop, Lynette Sawyer, Doug Cababa, R. Michael Hendry, Peter L. Nara, and Dennis R. Burton. In Vitro Evolution of a Neutralizing Human Antibody to Human Immunodeficiency Virus Type 1 to Enhance Affinity and Broaden Strain Cross-Reactivity. Proc. Natl. Acad. Sci. U.S.A., 91(9):3809-3813, 26 Apr 1994. PubMed ID: 8170992. Show all entries for this paper.

Clark2009 K. Reed Clark and Scott T. R. Walsh. Crystal Structure of a 3B3 Variant---Broadly Neutralizing HIV-1 scFv Antibody. Protein Sci., 18(12):2429-2441, Dec 2009. PubMed ID: 19785005. Show all entries for this paper.

Ma2011 Ben-Jiang Ma, S. Munir Alam, Eden P. Go, Xiaozhi Lu, Heather Desaire, Georgia D. Tomaras, Cindy Bowman, Laura L. Sutherland, Richard M. Scearce, Sampa Santra, Norman L. Letvin, Thomas B. Kepler, Hua-Xin Liao, and Barton F. Haynes. Envelope Deglycosylation Enhances Antigenicity of HIV-1 gp41 Epitopes for Both Broad Neutralizing Antibodies and Their Unmutated Ancestor Antibodies. PLoS Pathog., 7(9):e1002200, Sep 2011. PubMed ID: 21909262. Show all entries for this paper.

McHugh2002 Louise McHugh, Stella Hu, B. K. Lee, Kenneth Santora, Paul E. Kennedy, Edward A. Berger, Ira Pastan, and Dean H. Hamer. Increased Affinity and Stability of an Anti-HIV-1 Envelope Immunotoxin by Structure-Based Mutagenesis. J. Biol. Chem., 277(37):34383-34390, 13 Sep 2002. PubMed ID: 12119300. 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.


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