Abstract
The conserved, membrane-proximal external region (MPER) of the human immunodeficiency virus type-1 envelope glycoprotein 41 subunit is required for fusogenic activity. It has been proposed that MPER functions by disrupting the virion membrane. Supporting its critical role in viral entry as a membrane-bound entity, MPER constitutes the target for broadly neutralizing antibodies that have evolved mechanisms to recognize membrane-inserted epitopes. We have analyzed here the molecular mechanisms of membrane permeabilization induced by N-preTM and PreTM-C, two peptides derived from MPER sequences showing a tendency to associate with the bilayer interface or to transfer into the hydrocarbon core, respectively. Both peptides contained the full epitope sequence recognized by the 4E10 monoclonal antibody (MAb4E10), which was subsequently used to probe peptide accessibility from the water phase. Capacities of N-preTM and PreTM-C for associating with vesicles and inducing their permeabilization were comparable. Howe...
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