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Shedding-Resistant HIV-1 Envelope Glycoproteins Adopt Downstream Conformations That Remain Responsive to Conformation-Preferring Ligands

Maolin Lu, Xiaochu Ma, Nick Reichard, Daniel S. Terry, James Arthos, Amos B. Smith, Joseph Sodroski, Scott C. Blanchard, Walther Mothes

2020Journal of Virology42 citationsDOIOpen Access PDF

Abstract

The HIV-1 envelope glycoprotein (Env) opens in response to receptor CD4 binding from a pretriggered (state 1) conformation through a necessary intermediate to the three-CD4-bound conformation. The application of smFRET to test the conformational state of existing Env constructs and ligand complexes used for high-resolution structures recently revealed that they correspond to the downstream conformations. The structure of the pretriggered Env conformation, preferentially recognized by broadly neutralizing antibodies, remains unknown. Here, we identify experimental conditions that stabilize membrane-bound and shedding-resistant virus Env trimers in state 1, potentially facilitating structural characterization of this unknown conformational state.

Topics & Concepts

Gp41Förster resonance energy transferBiologyGlycoproteinConformational changeTrimerProtein structureViral envelopeBiophysicsViral matrix proteinViral entryCleavage (geology)Cell biologyStereochemistryBiochemistryVirusChemistryVirologyViral replicationAntibodyFluorescenceDimerGeneticsPhysicsQuantum mechanicsPaleontologyOrganic chemistryFracture (geology)EpitopeHIV Research and TreatmentHIV/AIDS drug development and treatmentHerpesvirus Infections and Treatments
Shedding-Resistant HIV-1 Envelope Glycoproteins Adopt Downstream Conformations That Remain Responsive to Conformation-Preferring Ligands | Litcius