title: Role of matrix protein in assembling the membrane of vesicular stomatitis virus: reconstitution of matrix protein with negatively charged phospholipid vesicles.
abstract: 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.
mesh_terms: D000089:Acetic Anhydrides / Q000494:pharmacology; D010713:Phosphatidylcholines / Q000378:metabolism; D010718:Phosphatidylserines / Q000378:metabolism; D010743:Phospholipids / Q000378:metabolism*; D013387:Succinic Anhydrides / Q000494:pharmacology; D014158:Transcription, Genetic / Q000187:drug effects; D014721:Vesicular stomatitis Indiana virus / Q000378:metabolism*; D014763:Viral Matrix Proteins; D014764:Viral Proteins / Q000378:metabolism*
chemical_list: D000089:Acetic Anhydrides; D010713:Phosphatidylcholines; D010718:Phosphatidylserines; D010743:Phospholipids; D013387:Succinic Anhydrides; D014763:Viral Matrix Proteins; D014764:Viral Proteins; C031800:acetic anhydride; C031801:succinic anhydride