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Respiratory syncytial virus matrix protein associates with nucleocapsids in infected cells.

Ghildyal R, Mills J, Murray M, Vardaxis N, Meanger J

  • Journal The Journal of general virology

  • Published 02 May 2002

  • Volume 83

  • ISSUE Pt 4

  • Pagination 753-757

  • DOI 10.1099/0022-1317-83-4-753


Little is known about the functions of the matrix (M) protein of respiratory syncytial virus (RSV). By analogy with other negative-strand RNA viruses, the M protein should inhibit the viral polymerase prior to packaging and facilitate virion assembly. In this study, localization of the RSV M protein in infected cells and its association with the RSV nucleocapsid complex was investigated. RSV-infected cells were shown to contain characteristic cytoplasmic inclusions. Further analysis showed that these inclusions were localization sites of the M protein as well as the N, P, L and M2-1 proteins described previously. The M protein co-purified with viral ribonucleoproteins (RNPs) from RSV-infected cells. The transcriptase activity of purified RNPs was enhanced by treatment with antibodies to the M protein in a dose-dependent manner. These data suggest that the M protein is associated with RSV nucleocapsids and, like the matrix proteins of other negative-strand RNA viruses, can inhibit virus transcription.