Work

CD4-binding-Site Recognition by VH1-46 Germline-derived HIV-1 Neutralizers

Year: 2014

Type: article

Abstract: Results: The gp120 and gp145 binds to Siglec-1 with high affinity, 4.13 nM ( JRFL gp120), 0.28-2.9nM ( JRFL gp145) and 0.44-8.26nM (SF162 gp145).Importantly, we found that the interaction of env protein to Siglec-1 took place through the V2 loop (4.34 nM JRFL V2; 1.96 nM SF162 V2).The presence of SA completely blocked the interaction of the env and the V2 loop protein with Siglec-1, suggesting thereby that the interaction occurred via a SA motif.Conclusions: The binding of gp120, gp145, and V2 loop to Siglec-1 is a high affinity interaction.Binding occurs through the V2 loop and requires sialic acid.This suggests that the vaccine design should aim to induce antibodies against V2-sialic acid complexes to prevent HIV-1 infections.

Source: AIDS Research and Human Retroviruses

DOI: 10.1089/aid.2014.5231.abstract

Authors: Priyamvada Acharya, Tongqing Zhou, Cinque Soto, Lei Chen, Timothy S. Luongo, Stephanie Moquin, Ivelin S. Georgiev, Stephen D. Schmidt, Mark K. Louder, M. Gordon Joyce, Yongping Yang, Baoshan Zhang, Johannes Scheid, Michel C. Nussenzweig, John R. Mascola, Peter D. Kwong

Institutions: National Institutes of Health, National Institute of Allergy and Infectious Diseases, Rockefeller University

Language: English

Topic: HIV Research and Treatment

Subfield: Virology

Field: Immunology and Microbiology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: green

OpenAlex ID: W2313689840

FWCI:

Cites:

Cited by: 1

Related to: 10