Molecular recognition of the native HIV-1 MPER revealed by STED microscopy of single virions.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 30622256.
- Also identified by DOI 10.1038/s41467-018-07962-9 and PMC identifier 6325134.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
Antibodies against the Membrane-Proximal External Region (MPER) of the Env gp41 subunit neutralize HIV-1 with exceptional breadth and potency. Due to the lack of knowledge on the MPER native structure and accessibility, different and exclusive models have been proposed for the molecular mechanism of MPER recognition by broadly neutralizing antibodies. Here, accessibility of antibodies to the native Env MPER on single virions has been addressed through STED microscopy. STED imaging of fluorescently labeled Fabs reveals a common pattern of native Env recognition for HIV-1 antibodies targeting MPER or the surface subunit gp120. In the case of anti-MPER antibodies, the process evolves with extra contribution of interactions with the viral lipid membrane to binding specificity. Our data provide biophysical insights into the recognition of the potent and broadly neutralizing MPER epitope on HIV virions, and as such is of importance for the design of therapeutic interventions.
Medical subject headings
- Antibodies, Neutralizing
- HIV Antibodies
- HIV Envelope Protein gp41
- HIV-1
- Protein Binding