Interaction between the respiratory syncytial virus G glycoprotein cytoplasmic domain and the matrix protein.
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.
Ghildyal
Reena
R
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.
Li
Dongsheng
D
Department of Environmental Biology, RMIT University, Melbourne, Australia.
Peroulis
Irene
I
Macfarlane Burnet Institute for Medical Research and Public Health, Melbourne, Australia.
Shields
Benjamin
B
Macfarlane Burnet Institute for Medical Research and Public Health, Melbourne, Australia.
Bardin
Phillip G
PG
Department of Respiratory and Sleep Medicine, Monash Medical Centre, 246 Clayton Road, Clayton 3168, Australia.
Teng
Michael N
MN
Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, MA, USA.
Collins
Peter L
PL
Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, MA, USA.
Meanger
Jayesh
J
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.
Mills
John
J
Department of Environmental Biology, RMIT University, Melbourne, Australia.|Departments of Microbiology and Medicine, Monash University, Clayton, Australia.
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
D014759:Viral Envelope Proteins; D014763:Viral Matrix Proteins; C116204:attachment protein G