Download full-text PDF |
Source |
|---|
Publication Analysis
Top Keywords
Similar Publications
Neutralizing antibodies elicited in macaques recognize V3 residues on altered conformations of HIV-1 Env trimer.
NPJ Vaccines
December 2024
Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA, USA.
Eliciting broadly neutralizing antibodies that protect against diverse HIV-1 strains is a primary goal of AIDS vaccine research. We characterized Ab1456 and Ab1271, two heterologously-neutralizing antibodies elicited in non-human primates by priming with an engineered V3-targeting SOSIP Env immunogen and boosting with increasingly native-like SOSIP Envs derived from different strain backgrounds. Structures of Env trimers in complex with these antibodies revealed V3 targeting, but on conformational states of Env distinct from the typical closed, prefusion trimeric SOSIP structure.
View Article and Find Full Text PDFConformational flexibility of HIV-1 envelope glycoproteins modulates transmitted/founder sensitivity to broadly neutralizing antibodies.
Nat Commun
August 2024
Division of Infectious Diseases and International Medicine, Department of Medicine, University of Minnesota, Minneapolis, MN, USA.
Article Synopsis
- The study focuses on HIV-1 envelope glycoproteins (Envs), which usually exist in a closed form, making it challenging to access their internal structures, crucial for designing vaccines that elicit broadly neutralizing antibodies (bnAbs).* -
- Researchers discovered that 6 out of 13 transmitted/founder (T/F) HIV-1 strains showed incompletely closed Env conformations that allow better access to internal epitopes, indicating potential targets for more effective immunogen designs.* -
- Using advanced cryo-electron microscopy, the team revealed structural movements in these incompletely closed Envs and demonstrated that a specific bnAb, N6, is effective against various Env forms, enhancing its antiviral efficacy against resistant
Applying Flow Virometry to Study the HIV Envelope Glycoprotein and Differences Across HIV Model Systems.
Viruses
June 2024
Department of Biological Sciences, University of Toronto Scarborough, Toronto, ON M1C 1A4, Canada.
Article Synopsis
- The HIV envelope glycoprotein (Env) is crucial for viral binding and immune responses but is difficult to target due to its complex structure and variability.
- Flow virometry (FV) allows researchers to study HIV virions at the single-particle level using a range of monoclonal antibodies, demonstrating its effectiveness in characterizing Env.
- The study highlights that both the production method of the virus and the addition of soluble CD4 can significantly influence the detection and conformation of Env on HIV virions.
Alternative substitutions of N332 in HIV-1 gp120 differentially affect envelope glycoprotein function and viral sensitivity to broadly neutralizing antibodies targeting the V3-glycan.
mBio
April 2024
Division of Infectious Diseases and International Medicine, Department of Medicine, University of Minnesota, Minneapolis, Minnesota, USA.
Unlabelled: The envelope glycoprotein (Env) trimer on the surface of human immunodeficiency virus type I (HIV-1) mediates viral entry into host CD4 T cells and is the sole target of neutralizing antibodies. Broadly neutralizing antibodies (bnAbs) that target gp120 V3-glycan of HIV-1 Env trimer are potent and block the entry of diverse HIV-1 strains. Most V3-glycan bnAbs interact, to a different extent, with a glycan attached to N332, but Asn at this position is not absolutely conserved or required for HIV-1 entry based on the prevalence of N332 in different circulating HIV-1 strains from diverse clades.
View Article and Find Full Text PDFInhibition of human immunodeficiency virus (HIV-1) infectivity by expression of poorly or broadly neutralizing antibodies against Env in virus-producing cells.
J Virol
February 2024
Department of Cancer Immunology and Virology, Dana-Farber Cancer Institute, Boston, Massachusetts, USA.
The human immunodeficiency virus (HIV-1) envelope (Env) glycoprotein precursor (gp160) trimerizes, is modified by high-mannose glycans in the endoplasmic reticulum, and is transported via Golgi and non-Golgi secretory pathways to the infected cell surface. In the Golgi, gp160 is partially modified by complex carbohydrates and proteolytically cleaved to produce the mature functional Env trimer, which is preferentially incorporated into virions. Broadly neutralizing antibodies (bNAbs) generally recognize the cleaved Env trimer, whereas poorly neutralizing antibodies (pNAbs) bind the conformationally flexible gp160.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!