Sequence and structure relatedness of matrix protein of human respiratory syncytial virus with matrix proteins of other negative-sense RNA viruses

K Latiff, J Meanger, J Mills, R Ghildyal

Research output: Contribution to journalArticle

11 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)945-948
Number of pages4
JournalClinical Microbiology and Infection
Volume10
Issue number10
DOIs
Publication statusPublished - 2004
Externally publishedYes

Fingerprint

Human respiratory syncytial virus
RNA Viruses
Proteins
Mononegavirales
Ebolavirus
Virus Assembly
Sequence Alignment
Membrane Proteins
Viruses

Cite this

@article{056efd3ed1b94ab9be19e3e5dee92f74,
title = "Sequence and structure relatedness of matrix protein of human respiratory syncytial virus with matrix proteins of other negative-sense RNA viruses",
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.",
keywords = "Amino Acid Sequence, Humans, Phylogeny, Protein Conformation, RNA Viruses, Respiratory Syncytial Viruses, Sequence Alignment, Surface Properties, Viral Matrix Proteins, Journal Article",
author = "K Latiff and J Meanger and J Mills and R Ghildyal",
year = "2004",
doi = "10.1111/j.1469-0691.2004.00980.x",
language = "English",
volume = "10",
pages = "945--948",
journal = "Clinical Microbiology and Infection",
issn = "1198-743X",
publisher = "Elsevier Limited",
number = "10",

}

TY - JOUR

T1 - Sequence and structure relatedness of matrix protein of human respiratory syncytial virus with matrix proteins of other negative-sense RNA viruses

AU - Latiff, K

AU - Meanger, J

AU - Mills, J

AU - Ghildyal, R

PY - 2004

Y1 - 2004

N2 - 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.

AB - 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.

KW - Amino Acid Sequence

KW - Humans

KW - Phylogeny

KW - Protein Conformation

KW - RNA Viruses

KW - Respiratory Syncytial Viruses

KW - Sequence Alignment

KW - Surface Properties

KW - Viral Matrix Proteins

KW - Journal Article

U2 - 10.1111/j.1469-0691.2004.00980.x

DO - 10.1111/j.1469-0691.2004.00980.x

M3 - Article

VL - 10

SP - 945

EP - 948

JO - Clinical Microbiology and Infection

JF - Clinical Microbiology and Infection

SN - 1198-743X

IS - 10

ER -