title: Interaction between the respiratory syncytial virus G glycoprotein cytoplasmic domain and the matrix protein.
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.
authors.affiliation: Macfarlane Burnet Institute for Medical Research and Public Health, Melbourne, Australia.|Departments of Microbiology and Medicine, Monash University, Clayton, Australia.|Department of Respiratory and Sleep Medicine, Monash Medical Centre, 246 Clayton Road, Clayton 3168, Australia.
authors.forename: Reena
authors.initials: R
authors.lastname: Ghildyal
authors.affiliation: Department of Environmental Biology, RMIT University, Melbourne, Australia.
authors.forename: Dongsheng
authors.initials: D
authors.lastname: Li
authors.affiliation: Macfarlane Burnet Institute for Medical Research and Public Health, Melbourne, Australia.
authors.forename: Irene
authors.initials: I
authors.lastname: Peroulis
authors.affiliation: Macfarlane Burnet Institute for Medical Research and Public Health, Melbourne, Australia.
authors.forename: Benjamin
authors.initials: B
authors.lastname: Shields
authors.affiliation: Department of Respiratory and Sleep Medicine, Monash Medical Centre, 246 Clayton Road, Clayton 3168, Australia.
authors.forename: Phillip G
authors.initials: PG
authors.lastname: Bardin
authors.affiliation: Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, MA, USA.
authors.forename: Michael N
authors.initials: MN
authors.lastname: Teng
authors.affiliation: Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, MA, USA.
authors.forename: Peter L
authors.initials: PL
authors.lastname: Collins
authors.affiliation: Macfarlane Burnet Institute for Medical Research and Public Health, Melbourne, Australia.|Department of Respiratory and Sleep Medicine, Monash Medical Centre, 246 Clayton Road, Clayton 3168, Australia.
authors.forename: Jayesh
authors.initials: J
authors.lastname: Meanger
authors.affiliation: Department of Environmental Biology, RMIT University, Melbourne, Australia.|Departments of Microbiology and Medicine, Monash University, Clayton, Australia.
authors.forename: John
authors.initials: J
authors.lastname: Mills
mesh_terms: D000595:Amino Acid Sequence; D002460:Cell Line; D006801:Humans; D008969:Molecular Sequence Data; D009154:Mutation; D018113:Respiratory Syncytial Virus, Human / Q000235:genetics / Q000378:metabolism*; D014759:Viral Envelope Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D014763:Viral Matrix Proteins / Q000235:genetics / Q000378:metabolism*; D019065:Virus Assembly
chemical_list: D014759:Viral Envelope Proteins; D014763:Viral Matrix Proteins; C116204:attachment protein G