Study on phylogenetic relationships, variability, and correlated mutations in M2 proteins of influenza virus A.

M2 channel, an influenza virus transmembrane protein, serves as an important target for antiviral drug design. There are still discordances concerning the role of some residues involved in proton transfer as well as the mechanism of inhibition by commercial drugs. The viral M2 proteins show high con...

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Autores principales:	Ly Le, Jacek Leluk
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/16068c5d30314edc95c8b2c3e9a54d36
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spelling	oai:doaj.org-article:16068c5d30314edc95c8b2c3e9a54d362021-11-18T06:48:51ZStudy on phylogenetic relationships, variability, and correlated mutations in M2 proteins of influenza virus A.1932-620310.1371/journal.pone.0022970https://doaj.org/article/16068c5d30314edc95c8b2c3e9a54d362011-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21829678/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203M2 channel, an influenza virus transmembrane protein, serves as an important target for antiviral drug design. There are still discordances concerning the role of some residues involved in proton transfer as well as the mechanism of inhibition by commercial drugs. The viral M2 proteins show high conservativity; about 3/4 of the positions are occupied by one residue in over 95%. Nine M2 proteins from the H3N2 strain and possibly two proteins from H2N2 strains make a phylogenic cluster closely related to 2RLF. The variability range is limited to 4 residues/position with one exception. The 2RLF protein stands out by the presence of 2 serines at the positions 19 and 50, which are in most other M2 proteins occupied by cysteines. The study of correlated mutations shows that there are several positions with significant mutational correlation that have not been described so far as functionally important. That there are 5 more residues potentially involved in the M2 mechanism of action. The original software used in this work (Consensus Constructor, SSSSg, Corm, Talana) is freely accessible as stand-alone offline applications upon request to the authors. The other software used in this work is freely available online for noncommercial purposes at public services on bioinformatics such as ExPASy or NCBI. The study on mutational variability, evolutionary relationship, and correlated mutation presented in this paper is a potential way to explain more completely the role of significant factors in proton channel action and to clarify the inhibition mechanism by specific drugs.Ly LeJacek LelukPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 8, p e22970 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Ly Le Jacek Leluk Study on phylogenetic relationships, variability, and correlated mutations in M2 proteins of influenza virus A.
description	M2 channel, an influenza virus transmembrane protein, serves as an important target for antiviral drug design. There are still discordances concerning the role of some residues involved in proton transfer as well as the mechanism of inhibition by commercial drugs. The viral M2 proteins show high conservativity; about 3/4 of the positions are occupied by one residue in over 95%. Nine M2 proteins from the H3N2 strain and possibly two proteins from H2N2 strains make a phylogenic cluster closely related to 2RLF. The variability range is limited to 4 residues/position with one exception. The 2RLF protein stands out by the presence of 2 serines at the positions 19 and 50, which are in most other M2 proteins occupied by cysteines. The study of correlated mutations shows that there are several positions with significant mutational correlation that have not been described so far as functionally important. That there are 5 more residues potentially involved in the M2 mechanism of action. The original software used in this work (Consensus Constructor, SSSSg, Corm, Talana) is freely accessible as stand-alone offline applications upon request to the authors. The other software used in this work is freely available online for noncommercial purposes at public services on bioinformatics such as ExPASy or NCBI. The study on mutational variability, evolutionary relationship, and correlated mutation presented in this paper is a potential way to explain more completely the role of significant factors in proton channel action and to clarify the inhibition mechanism by specific drugs.
format	article
author	Ly Le Jacek Leluk
author_facet	Ly Le Jacek Leluk
author_sort	Ly Le
title	Study on phylogenetic relationships, variability, and correlated mutations in M2 proteins of influenza virus A.
title_short	Study on phylogenetic relationships, variability, and correlated mutations in M2 proteins of influenza virus A.
title_full	Study on phylogenetic relationships, variability, and correlated mutations in M2 proteins of influenza virus A.
title_fullStr	Study on phylogenetic relationships, variability, and correlated mutations in M2 proteins of influenza virus A.
title_full_unstemmed	Study on phylogenetic relationships, variability, and correlated mutations in M2 proteins of influenza virus A.
title_sort	study on phylogenetic relationships, variability, and correlated mutations in m2 proteins of influenza virus a.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/16068c5d30314edc95c8b2c3e9a54d36
work_keys_str_mv	AT lyle studyonphylogeneticrelationshipsvariabilityandcorrelatedmutationsinm2proteinsofinfluenzavirusa AT jacekleluk studyonphylogeneticrelationshipsvariabilityandcorrelatedmutationsinm2proteinsofinfluenzavirusa
_version_	1718424335036710912

Study on phylogenetic relationships, variability, and correlated mutations in M2 proteins of influenza virus A.

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