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Displaying record number 690

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MAb ID L100
HXB2 Location Env Env Epitope Map
Author Location gp120( HXBc2)
Ab Type gp120 C1-C2
Species (Isotype) human(IgG1)
Immunogen HIV-1 infection
Keywords antibody binding site, variant cross-reactivity


Showing 3 of 3 notes.


Showing 4 of 4 references.

Isolation 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.

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.

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