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Respiratory syncytial virus matrix protein associates with nucleocapsids in infected cells

Children’s Virology Research Unit, Macfarlane Burnet Institute for Medical Research and Public Health, PO Box 254, Yarra Bend Road, Fairfield, Victoria 3078, Australia¹
Department of Medical Laboratory Science, School of Medical Sciences, RMIT University, Bundoora, Victoria 3083, Australia²

Author for correspondence: J. Meanger. Fax +613 9282 2100. e-mail jayesh{at}burnet.edu.au

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.