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• L25: In a review of Envelope binding MAbs in this database, V2-specific MAbs are noted to have some ability to neutralize HIV-1, but generally weakly with limited cross-reactivity. L25, L39, L40 and L78 are Fabs specific for a complex binding site involving V2 and elements of the sCD4 binding site regions; among these only L25 and L78 mediate weak neutralization of some TCLA strains. Gorny2003 (antibody binding site, variant cross-reactivity, review)
• L25: Neutralizes TCLA strains weakly, but not primary isolates. Parren1997
• L25: gp120 immobilized on solid phase by capture with anti-CD4 BS MAb L72 was used for selection of Fabs -- a single anti-V2-CD4 BS Fab was obtained with sensitivity to substitutions in the V2 and CD4 BS regions -- rodent anti-V2 MAb SC258 competes with L25. Ditzel1997

References

Showing 4 of 4 references.

Ditzel1995 H. J. Ditzel, J. M. Binley, J. P. Moore, J. Sodroski, N. Sullivan, L. S. W. Sawyer, R. M. Hendry, W.-P. Yang, C. F. Barbas III, and D. R. Burton. Neutralizing Recombinant Human Antibodies to a Conformational V2- and CD4-Binding Site-Sensitive Epitope of HIV-1 gp120 Isolated by Using an Epitope-Masking Procedure. J. Immunol., 154:893-906, 1995. A panel of Fabs was obtained from a library prepared from the bone marrow of a long-term asymptomatic HIV-1 seropositive male donor. Four Fabs recognize the CD4BS. An additional four Fabs were retrieved after epitope masking gp120 with the CD4BS Fabs at the screening stage. 3/4 of these Fabs bind to a V2 dependent conformational epitope. PubMed ID: 7529290. 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.

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.