Analysis of HIV-1 Matrix-Envelope Cytoplasmic Tail Interactions

Journal of Virology
Ayna AlfadhliEric Barklis

Abstract

The matrix (MA) domains of HIV-1 precursor Gag (PrGag) proteins direct PrGag proteins to plasma membrane (PM) assembly sites where envelope (Env) protein trimers are incorporated into virus particles. MA targeting to PM sites is facilitated by its binding to phosphatidylinositol-(4,5)-bisphosphate [PI(4,5)P2], and MA binding to cellular RNAs appears to serve a chaperone function that prevents MA from associating with intracellular membranes prior to arrival at the PI(4,5)P2-rich PM. Investigations have shown genetic evidence of an interaction between MA and the cytoplasmic tails (CTs) of Env trimers that contributes to Env incorporation into virions, but demonstrations of direct MA-CT interactions have proven more difficult. In direct binding assays, we show here that MA binds to Env CTs. Using MA mutants, matrix-capsid (MACA) proteins, and MA proteins incubated in the presence of inositol polyphosphate, we show a correlation between MA trimerization and CT binding. RNA ligands with high affinities for MA reduced MA-CT binding levels, suggesting that MA-RNA binding interferes with trimerization and/or directly or indirectly blocks MA-CT binding. Rough-mapping studies indicate that C-terminal CT helices are involved in MA bindin...Continue Reading

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Citations

Apr 11, 2020·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Alexej Dick, Simon Cocklin
Aug 17, 2020·Journal of Virology·Jan PrchalTomáš Ruml
Jan 25, 2021·The Journal of Biological Chemistry·Gunnar N EastepJamil S Saad
Feb 9, 2021·Advanced Science·Jon Ander Nieto-GaraiMaier Lorizate
Aug 6, 2021·Scientific Reports·Halilibrahim CiftciHasan DeMirci

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