Sequence and structure relatedness of matrix protein of human respiratory syncytial virus with matrix proteins of other negative-sense RNA viruses.
Matrix proteins of viruses within the order Mononegavirales have similar functions and play important roles in virus assembly. Protein sequence alignment, phylogenetic tree derivation, hydropathy profiles and secondary structure prediction were performed on selected matrix protein sequences, using human respiratory syncytial virus matrix protein as the reference. No general conservation of primary, secondary or tertiary structure was found, except for a broad similarity in the hydropathy pattern correlating with the fact that all the proteins studied are membrane-associated. Interestingly, the matrix proteins of Ebola virus and human respiratory syncytial virus shared secondary structure homology.
Latiff
K
K
Children's Virology Research Unit, Macfarlane Burnet Institute of Medical Research and Public Health, Monash University, Melbourne, Australia.
Meanger
J
J
Mills
J
J
Ghildyal
R
R
D000595:Amino Acid Sequence / Q000235:genetics; D006801:Humans; D010802:Phylogeny; D011487:Protein Conformation; D012328:RNA Viruses / Q000235:genetics* / Q000378:metabolism; D012136:Respiratory Syncytial Viruses / Q000235:genetics* / Q000378:metabolism / Q000502:physiology; D016415:Sequence Alignment; D013499:Surface Properties; D014763:Viral Matrix Proteins / Q000235:genetics* / Q000502:physiology
D014763:Viral Matrix Proteins