Role of matrix protein in assembling the membrane of vesicular stomatitis virus: reconstitution of matrix protein with negatively charged phospholipid vesicles

• Published in: Biochemistry (Easton) Vol. 20; no. 13; pp. 3902 - 3907
• Main Authors: Zakowski, Jack J, Petri, William A, Wagner, Robert R
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 23.06.1981
• Subjects: Acetic Anhydrides - pharmacology; Phosphatidylcholines - metabolism; Phosphatidylserines - metabolism; Phospholipids - metabolism; Succinic Anhydrides - pharmacology; Transcription, Genetic - drug effects; Vesicular stomatitis Indiana virus - metabolism; Viral Matrix Proteins; Viral Proteins - metabolism
• ISSN: 0006-2960; 1520-4995
• DOI: 10.1021/bi00516a037

The matrix (M) protein of vesicular stomatitis virus (VSV) was reconstituted into phospholipid vesicles by detergent dialysis. Reconstitution of the positively charged M protein occurred only in the presence of negatively charged phospholipids such as phosphatidylserine, phosphatidic acid, or phosphatidylinositol. Preformed vesicles containing negatively charged phospholipids also bound free M protein. Derivatization of the positively charged lysines in M protein with acetic anhydride or succinic anhydride prevented M protein reconstitution but did not affect the biological property of M protein to inhibit in vitro VSV transcription. An additional indication of the electrostatic nature of the M protein binding to the vesicles was that M protein could not be reconstituted in the presence of 0.5 M NaCl. Nonelectrostatic forces also appear to be involved in the association of the M protein with vesicles, since previously reconstituted M protein remained associated with the vesicles upon subsequent exposure to 0.5 M NaCl.