AIDS Weekly Plus
New Virology Study Findings Have Been Reported by Scientists at National Institute of Allergy and Infectious Diseases (NIAID)
February 18, 2013
2013 FEB 18 (NewsRx) -- By a News Reporter-Staff News Editor at AIDS Weekly -- Current study results on Virology have been published. According to news reporting originating from Bethesda, Maryland, by NewsRx correspondents, research stated, "The outer domain of the HIV-1 gp120 envelope glycoprotein contains the epitope for broadly neutralizing antibodies directed to the CD4-binding site, many of which are able to neutralize over 90% of circulating HIV-1 isolates. While the outer domain is conformationally more stable than other portions of the HIV-1 envelope, efforts to express the outer domain as an immunogen for eliciting broadly neutralizing antibodies have not been successful, potentially because natural outer domain variants do not bind strongly to antibodies such as VRC01."
Our news editors obtained a quote from the research from the National Institute of Allergy and Infectious Diseases (NIAID), "In this study, we optimized the antigenic properties of the HIV-1 Env outer domain to generate OD4.2.2, from the KER2018 strain of clade A HIV-1, enabling it to bind antibodies such as VRC01 with nanomolar affinity. The crystal structure of OD4.2.2 in complex with VRC-PG04 was solved at 3.0-A resolution and compared to known crystal structures including (i) the structure of core gp120 bound by VRC-PG04 and (ii) a circularly permutated version of the outer domain in complex with antibody PGT128. Much of the VRC-PG04 epitope was preserved in the OD4.2.2 structure, though with altered N and C termini conformations. Overall, roughly one-third of the outer domain structure appeared to be fixed in conformation, independent of alterations in termini, clade, or ligand, while other portions of the outer domain displayed substantial structural malleability."
According to the news editors, the research concluded: "The crystal structure of OD4.2.2 with VRC-PG04 provides atomic-level details for an HIV-1 domain recognized by broadly neutralizing antibodies and insights relevant to the rational design of an immunogen that could elicit such antibodies by vaccination."
For more information on this research see: Outer Domain of HIV-1 gp120: Antigenic Optimization, Structural Malleability, and Crystal Structure with Antibody VRC-PG04. The Journal of Virology, 2013;87(4):2294-306 (see also Virology).
The news editors report that additional information may be obtained by contacting M.G. Joyce, Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland, United States.
Keywords for this news article include: Antibodies, Bethesda, Maryland, HIV/AIDS, Virology, Immunology, RNA Viruses, Retroviridae, United States, Blood Proteins, HIV Infections, Immunoglobulins, Vertebrate Viruses, Primate Lentiviruses, North and Central America, Viral Sexually Transmitted Diseases.
Our reports deliver fact-based news of research and discoveries from around the world. Copyright 2013, NewsRx LLC