Biochemistry, Biophysics, and Structural Biology Commons^™

Membrane Structure Correlates To Function Of Llp2 On The Cytoplasmic Tail Of Hiv-1 Gp41 Protein, Alexander Boscia, Zachary Benamram, Jonathan Michel, Michael Jablin, Jonathan D. Steckbeck, Ronald C. Montelaro, John F. Nagle, Prof. Stephanie Tristram-Nagle Ph.D.

Prof. Stephanie Tristram-Nagle Ph.D.

Mutation studies previously showed that the lentivirus lytic peptide (LLP2) sequence of the cytoplasmic C-terminal tail of the HIV-1 gp41 envelope protein inhibited viral-initiated T-cell death and T-cell syncytium formation, at which time in the HIV life cycle the gp41 protein is embedded in the T-cell membrane. In striking contrast, the mutants did not affect virion infectivity, during which time the gp41 protein is embedded in the HIV envelope membrane. To examine the role of LLP2/membrane interactions, we applied synchrotron X-radiation to determine structure of hydrated membranes. We focused on WT LLP2 peptide (þlus three charge) and MX2 mutant (negative …