Characterization of the functional domain of β2-microglobulin from the Asian seabass, Lates calcarifer.

<h4>Background</h4>β2-Microglobulin (β(2)M) is the light chain of major histocompatibility class I (MHC I) that binds non-covalently with the α heavy chain. Both proteins attach to the antigen peptide, presenting a complex to the T cell to be destroyed via the immune mechanism.<h4>...

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Autores principales:	Hirzahida Mohd-Padil, Khairina Tajul-Arifin, Adura Mohd-Adnan
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2010
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/ce4c586758724f69a1812ca4a748c5ae
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spelling	oai:doaj.org-article:ce4c586758724f69a1812ca4a748c5ae2021-11-18T07:03:39ZCharacterization of the functional domain of β2-microglobulin from the Asian seabass, Lates calcarifer.1932-620310.1371/journal.pone.0013159https://doaj.org/article/ce4c586758724f69a1812ca4a748c5ae2010-10-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/20949082/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203<h4>Background</h4>β2-Microglobulin (β(2)M) is the light chain of major histocompatibility class I (MHC I) that binds non-covalently with the α heavy chain. Both proteins attach to the antigen peptide, presenting a complex to the T cell to be destroyed via the immune mechanism.<h4>Methodology/principal findings</h4>In this study, a cDNA sequence encoding β(2)M in the Asian seabass (Lates calcarifer) was identified and analyzed using in silico approaches to predict and characterize its functional domain. The β(2)M cDNA contains an open reading frame (ORF) of 351 bases with a coding capacity of 116 amino acids. A large portion of the protein consists of the IG constant domain (IGc1), similar to β(2)M sequences from other species studied thus far. Alignment of the IGc1 domains of β(2)M from L. calcarifer and other species shows a high degree of overall conservation. Seven amino acids were found to be conserved across taxa whereas conservation between L. calcarifer and other fish species was restricted to 14 amino acids at identical conserved positions.<h4>Conclusion/significance</h4>As the L. calcarifer β(2)M protein analyzed in this study contains a functional domain similar to that of β(2)M proteins in other species, it can be postulated that the β(2)M proteins from L. calcarifer and other organisms are derived from a common ancestor and thus have a similar immune function. Interestingly, fish β(2)M genes could also be classified according to the ecological habitat of the species, i.e. whether it is from a freshwater, marine or euryhaline environment.Hirzahida Mohd-PadilKhairina Tajul-ArifinAdura Mohd-AdnanPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 5, Iss 10, p e13159 (2010)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Hirzahida Mohd-Padil Khairina Tajul-Arifin Adura Mohd-Adnan Characterization of the functional domain of β2-microglobulin from the Asian seabass, Lates calcarifer.
description	<h4>Background</h4>β2-Microglobulin (β(2)M) is the light chain of major histocompatibility class I (MHC I) that binds non-covalently with the α heavy chain. Both proteins attach to the antigen peptide, presenting a complex to the T cell to be destroyed via the immune mechanism.<h4>Methodology/principal findings</h4>In this study, a cDNA sequence encoding β(2)M in the Asian seabass (Lates calcarifer) was identified and analyzed using in silico approaches to predict and characterize its functional domain. The β(2)M cDNA contains an open reading frame (ORF) of 351 bases with a coding capacity of 116 amino acids. A large portion of the protein consists of the IG constant domain (IGc1), similar to β(2)M sequences from other species studied thus far. Alignment of the IGc1 domains of β(2)M from L. calcarifer and other species shows a high degree of overall conservation. Seven amino acids were found to be conserved across taxa whereas conservation between L. calcarifer and other fish species was restricted to 14 amino acids at identical conserved positions.<h4>Conclusion/significance</h4>As the L. calcarifer β(2)M protein analyzed in this study contains a functional domain similar to that of β(2)M proteins in other species, it can be postulated that the β(2)M proteins from L. calcarifer and other organisms are derived from a common ancestor and thus have a similar immune function. Interestingly, fish β(2)M genes could also be classified according to the ecological habitat of the species, i.e. whether it is from a freshwater, marine or euryhaline environment.
format	article
author	Hirzahida Mohd-Padil Khairina Tajul-Arifin Adura Mohd-Adnan
author_facet	Hirzahida Mohd-Padil Khairina Tajul-Arifin Adura Mohd-Adnan
author_sort	Hirzahida Mohd-Padil
title	Characterization of the functional domain of β2-microglobulin from the Asian seabass, Lates calcarifer.
title_short	Characterization of the functional domain of β2-microglobulin from the Asian seabass, Lates calcarifer.
title_full	Characterization of the functional domain of β2-microglobulin from the Asian seabass, Lates calcarifer.
title_fullStr	Characterization of the functional domain of β2-microglobulin from the Asian seabass, Lates calcarifer.
title_full_unstemmed	Characterization of the functional domain of β2-microglobulin from the Asian seabass, Lates calcarifer.
title_sort	characterization of the functional domain of β2-microglobulin from the asian seabass, lates calcarifer.
publisher	Public Library of Science (PLoS)
publishDate	2010
url	https://doaj.org/article/ce4c586758724f69a1812ca4a748c5ae
work_keys_str_mv	AT hirzahidamohdpadil characterizationofthefunctionaldomainofb2microglobulinfromtheasianseabasslatescalcarifer AT khairinatajularifin characterizationofthefunctionaldomainofb2microglobulinfromtheasianseabasslatescalcarifer AT aduramohdadnan characterizationofthefunctionaldomainofb2microglobulinfromtheasianseabasslatescalcarifer
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Characterization of the functional domain of β2-microglobulin from the Asian seabass, Lates calcarifer.

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