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pubmed-article:6268151pubmed:abstractTextThe 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.lld:pubmed
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pubmed-article:6268151pubmed:articleTitleRole of matrix protein in assembling the membrane of vesicular stomatitis virus: reconstitution of matrix protein with negatively charged phospholipid vesicles.lld:pubmed
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