Important note: Information in this article was accurate in June 2003. The state of the art June have changed since the publication date. |
AIDSWEEKLY Plus; Monday, June 23, 2003
Michael Greer, Senior Medical Writer
"IgG1 b12 is a broadly neutralizing antibody against human immunodeficiency virus type 1 (HIV-1)," explained Michael B. Zwick and colleagues at the Scripps Research Institute in La Jolla, California, and Simon Fraser University in Burnaby, British Columbia, Canada. "The epitope recognized by b12 overlaps the CD4 receptor-binding site (CD4bs) on gp120 and has been a target for vaccine design."
Zwick and coauthors identified several residues that play crucial roles in the interaction between b12 and the HIV coat protein gp120.
The researchers performed "extensive mutational analysis" of b12's antigen-binding site. Most of the mutations tested were located in the antibody's H3 region, they noted.
A Trp residue at the top of the H3 loop and several residues at the loop base were apparently essential to gp120 binding, according to the report. In additon, study data confirmed the putative roles played by a Tyr residue at the apex of the H2 loop and several L1 Arg resiudes in this process.
Somatic mutation was necessary for the development of many structural features heavily involved in the b12-gp120 interaction (Molecular features of the broadly neutralizing immunoglobulin G1 b12 required for recognition of human immunodeficiency virus type 1 gp120. J Virol. 2003 May;77(10):5863-76.
"The paratope map of b12 may facilitate the design of molecules that are able to elicit b12-like activities," Zwick and colleagues concluded.
The corresponding author for this report is Dennis R. Burton, Department of Immunology (IMM-2), The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, CA 92037, USA. E-mail: burton@scripps.edu.
Key points reported in this study include:
The structure of the broadly neutralizing immunoglobulin G antibody b12 has been characterized
Key residues in the interaction between b12 and the HIV coat protein gp120 have been identified
This information may aid the development of b12-based HIV vaccines
This article was prepared by AIDS Weekly editors from staff and other reports.
Reference
Zwick MB, Parren PW, Saphire EO, et al., "Molecular features of the broadly neutralizing immunoglobulin G1 b12 required for recognition of human immunodeficiency virus type 1 gp120", J Virol. 2003 May;77(10):5863-76.
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