Interactions of normal and mutant vesicular stomatitis virus matrix proteins with the plasma membrane and nucleocapsids

Abstract

We demonstrated recently that a fraction of the matrix (M) protein of vesicular stomatitis virus (VSV) binds tightly to cellular membranes in vivo when expressed in the absence of other VSV proteins. This membraneassociated M protein was functional in binding purified VSV nucleocapsids in vitro. Here we show that the membrane-associated M protein is largely associated with a membrane fraction having the density of plasma membranes, indicating membrane specificity in the binding. In addition, we analyzed truncated forms of M protein to identify regions responsible for membrane association and nucleocapsid binding. Truncated M protein lacking the amino-terminal basic domain still associated with cellular membranes, although not as tightly as wild-type M protein, and could not bind nucleocapsids. In contrast, deletion of the carboxy-terminal 14 amino acids did not disrupt stable membrane association or nucleocapsid interaction. These results suggest that the amino terminus of M protein either interacts directly with membranes and nucleocapsids or stabilizes a conformation that is required for M protein to mediate both of these interactions.

Binding of Human Immunodeficiency Virus Type 1 Gag to Membrane: Role of the Matrix Amino Terminus

“…To this end, we analyzed the distribution of Gag, using equilibrium flotation centrifugation. This approach has been used successfully to study membrane binding of the vesicular stomatitis virus M protein (3,5,6) and has also been applied to the analysis of HIV-1 MA membrane binding (42). Postnuclear supernatants from transfected HeLa cell homogenates were adjusted to 73% (wt/vol) sucrose, placed at the bottom of centrifuge tubes, overlaid with 65% (wt/vol) and 10% (wt/vol) sucrose, and centrifuged for 18 h at 100,000 ϫ g (Materials and Methods).…”

Sequence and structure relatedness of matrix protein of human respiratory syncytial virus with matrix proteins of other negative-sense RNA viruses

“…assembly and budding. They interact with envelope proteins, cell membranes and viral nucleocapsids, and also self-oligomerise [1][2][3]. Matrix proteins inhibit cellular transcription early in infection, and subsequently interact with viral nucleocapsids to inhibit viral transcriptase activity [4][5][6][7][8].…”

Monoclonal Antibody #3‐9‐16 Recognizes One of the Two Isoforms of Rabies Virus Matrix Protein That Exposes Its N‐Terminus on the Virion Surface

“…The M protein of vesicular stomatitis virus (VSV), another major member of the Rhabdoviridae, was extensively studied, and is now known to work multifunctionally in the virus replication cycle, such as the regulation of viral RNA synthesis, stabilization of viral glycoprotein and virion formation with G and RNP at the budding site (1,2,4,15,(19)(20)(21).…”