Interaction between the respiratory syncytial virus G glycoprotein cytoplasmic domain and the matrix protein

Reena Ghildyal, Li Dongsheng, Irene Peroulis, Benjamin Sheilds, Philip Bardin, Michael Teng, Peter Collins, Jayesh Meanger, John Mills

    Research output: Contribution to journalArticle

    52 Citations (Scopus)

    Abstract

    Paramyxovirus assembly at the cell membrane requires the movement of viral components to budding sites and envelopment of nucleocapsids by cellular membranes containing viral glycoproteins, facilitated by interactions with the matrix protein. The specific protein interactions during assembly of respiratory syncytial virus (RSV) are unknown. Here, the postulated interaction between the RSV matrix protein (M) and G glycoprotein (G) was investigated. Partial co-localization of M with G was demonstrated, but not with a truncated variant lacking the cytoplasmic domain and one-third of the transmembrane domain, in cells infected with recombinant RSV or transfected to express G and M. A series of G mutants was constructed with progressively truncated or modified cytoplasmic domains. Data from co-expression in cells and a cell-free binding assay showed that the N-terminal aa 2–6 of G play a key role in G–M interaction, with serine at position 2 and aspartate at position 6 playing key roles.
    Original languageEnglish
    Pages (from-to)1879-1884
    Number of pages6
    JournalJournal of General Virology
    Volume86
    Issue number7
    DOIs
    Publication statusPublished - 2005

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