Please use this identifier to cite or link to this item: https://repository.monashhealth.org/monashhealthjspui/handle/1/32525
Title: Sequence and structure relatedness of matrix protein of human respiratory syncytial virus with matrix proteins of other negative-sense RNA viruses.
Authors: Mills J.;Latiff K.;Meanger J.;Ghildyal R.
Institution: (Latiff, Meanger, Mills, Ghildyal) Children's Virology Research Unit, Macfarlane Burnet Inst. of Med. Res., Monash University, Melbourne, Vic., Australia (Latiff, Meanger, Ghildyal) Department of Microbiology, Monash University, Monash Medical Centre, Melbourne, Vic., Australia (Latiff, Ghildyal) Monash University, Department of Medicine, Monash Medical Centre, Melbourne, Vic., Australia
Issue Date: 19-Oct-2012
Copyright year: 2004
Publisher: Blackwell Publishing Ltd (9600 Garsington Road, Oxford OX4 2XG, United Kingdom)
Place of publication: United Kingdom
Publication information: Clinical Microbiology and Infection. 10 (10) (pp 945-948), 2004. Date of Publication: October 2004.
Abstract: 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. © 2004 Copyright by the European Society of Clinical Microbiology and Infectious Diseases.
DOI: http://monash.idm.oclc.org/login?url=http://dx.doi.org/10.1111/j.1469-0691.2004.00980.x
PubMed URL: 15373896 [http://www.ncbi.nlm.nih.gov/pubmed/?term=15373896]
ISSN: 1198-743X
URI: https://repository.monashhealth.org/monashhealthjspui/handle/1/32525
Type: Article
Subjects: protein structure
*Respiratory syncytial pneumovirus
RNA virus
Sendai virus
sequence alignment
sequence homology
Vesicular stomatitis virus
virus assembly
*matrix protein/ec [Endogenous Compound]
Canine distemper morbillivirus
amino acid sequence
article
avian pneumovirus
Borna disease virus
controlled study
Ebola virus
genetic conservation
Influenza virus A
Measles virus
Mumps virus
Newcastle disease paramyxovirus
nonhuman
Parainfluenza virus 1
phylogeny
priority journal
protein secondary structure
Mumps virus
Newcastle disease paramyxovirus
nonhuman
Parainfluenza virus 1
phylogeny
priority journal
protein secondary structure
protein structure
*Respiratory syncytial pneumovirus
RNA virus
article
sequence alignment
sequence homology
Vesicular stomatitis virus
virus assembly
amino acid sequence
Sendai virus
Avian pneumovirus
Borna disease virus
Canine distemper morbillivirus
controlled study
Ebola virus
genetic conservation
Influenza virus A
Measles virus
Appears in Collections:Articles

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