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Vaccine Details

Notes

Showing 5 of 5 notes.

• m6: The increase in the on-rate of this Ab was used to assess the degree to which stabilization 'preformed' the variant gp120 cores in the CD4-bound state. Zhou2007 (kinetics)
• m6: Novel approaches based on sequential (SAP) and competitive (CAP) antigen panning methodologies, and use of antigens with increased exposure of conserved epitopes, for enhanced identification of broadly cross-reactive neutralizing Abs are reviewed. Abs identified by these methods are described. Zhang2007 (review)
• m6: The structure of the V3 region in the context of gp120 core complexed to the CD4 receptor and to the m6 Ab was attempted to be determined by X-ray resolution, but only the structure for V3 complexed with CD4 and X5 Ab was solved. Huang2005 (structure)
• M6: A comparison of 25 gp120 specific, conformation dependent MAbs was done -- M6 is part of a group of MAbs labeled A1 -- all A1 MAbs were broadly cross-reactive with gp160 from B-clade R5, X4, and R5X4 viruses, blocked CD4 binding, were sensitive to mutations in gp120 positions 368 and 370 that directly contact CD4. Sugiura1999
• M6: Generated during a study of the influence of the oligomeric structure of Env in determining the repertoire of the Ab response. Earl1994

References

Showing 5 of 5 references.

Earl1994 P. L. Earl, C. C. Broder, D. Long, S. A. Lee, J. Peterson, S. Chakrabarti, R. W. Doms, and B. Moss. Native oligomeric human immunodeficiency virus type 1 Envelope glycoprotein elicits diverse monoclonal antibody reactivities. J. Virol., 68:3015-3026, 1994. In a study of the repertoire of response to oligomeric versus monomeric Env protein, 138 murine MAbs were generated in response to an immunogen that was a gp120/bp41 oligomeric molecule that was not cleaved due to a mutation in the cleavage site. The oligomeric molecule was found to elicit a response that was very different than the monomer. Most MAbs were conformational, many were to gp41 or if in gp120, to the CD4 BS. Few MAbs to linear V3 epitopes were produced in response to oligomeric protein, though this was a common specificity in response to immunization with gp120 monomeric protein. PubMed ID: 7512157. Show all entries for this paper.

Sugiura1999 W. Sugiura, C. C. Broder, B. Moss, and P. L. Earl. Characterization of conformation-dependent anti-gp120 murine monoclonal antibodies produced by immunization with monomeric and oligomeric human immunodeficiency virus type 1 envelope proteins. Virology, 254:257-67, 1999. PubMed ID: 9986792. 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.

Zhang2007 Mei-Yun Zhang and Dimiter S. Dimitrov. Novel Approaches for Identification of Broadly Cross-Reactive HIV-1 Neutralizing Human Monoclonal Antibodies and Improvement of Their Potency. Curr. Pharm. Des., 13(2):203-212, 2007. PubMed ID: 17269928. Show all entries for this paper.

Zhou2007 Tongqing Zhou, Ling Xu, Barna Dey, Ann J. Hessell, Donald Van Ryk, Shi-Hua Xiang, Xinzhen Yang, Mei-Yun Zhang, Michael B. Zwick, James Arthos, Dennis R. Burton, Dimiter S. Dimitrov, Joseph Sodroski, Richard Wyatt, Gary J. Nabel, and Peter D. Kwong. Structural Definition of a Conserved Neutralization Epitope on HIV-1 gp120. Nature, 445(7129):732-737, 15 Feb 2007. PubMed ID: 17301785. Show all entries for this paper.