Abstract
Background: β2-Microglobulin (β2M) is the light chain of major histocompatibility class I (MHC I) that binds non-covalently with the a heavy chain. Both proteins attach to the antigen peptide, presenting a complex to the T cell to be destroyed via the immune mechanism. Methodology/Principal Findings: In this study, a cDNA sequence encoding β2M in the Asian seabass (Lates calcarifer) was identified and analyzed using in silico approaches to predict and characterize its functional domain. The β2M 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 β2M sequences from other species studied thus far. Alignment of the IGc1 domains of β2M 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. Conclusion/Significance: As the L. calcarifer β2M protein analyzed in this study contains a functional domain similar to that of β2M proteins in other species, it can be postulated that the β2M proteins from L. calcarifer and other organisms are derived from a common ancestor and thus have a similar immune function. Interestingly, fish β2M 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.
| Original language | English |
|---|---|
| Article number | e13159 |
| Journal | PLoS One |
| Volume | 5 |
| Issue number | 10 |
| DOIs | |
| Publication status | Published - 2010 |
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ASJC Scopus subject areas
- Agricultural and Biological Sciences(all)
- Biochemistry, Genetics and Molecular Biology(all)
- Medicine(all)
Cite this
Characterization of the functional domain of β2- microglobulin from the Asian seabass, Lates calcarifer. / Mohd-Padil, Hirzahida; Tajul-Arifin, Khairina; Mohd-Adnan, Adura.
In: PLoS One, Vol. 5, No. 10, e13159, 2010.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Characterization of the functional domain of β2- microglobulin from the Asian seabass, Lates calcarifer
AU - Mohd-Padil, Hirzahida
AU - Tajul-Arifin, Khairina
AU - Mohd-Adnan, Adura
PY - 2010
Y1 - 2010
N2 - Background: β2-Microglobulin (β2M) is the light chain of major histocompatibility class I (MHC I) that binds non-covalently with the a heavy chain. Both proteins attach to the antigen peptide, presenting a complex to the T cell to be destroyed via the immune mechanism. Methodology/Principal Findings: In this study, a cDNA sequence encoding β2M in the Asian seabass (Lates calcarifer) was identified and analyzed using in silico approaches to predict and characterize its functional domain. The β2M 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 β2M sequences from other species studied thus far. Alignment of the IGc1 domains of β2M 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. Conclusion/Significance: As the L. calcarifer β2M protein analyzed in this study contains a functional domain similar to that of β2M proteins in other species, it can be postulated that the β2M proteins from L. calcarifer and other organisms are derived from a common ancestor and thus have a similar immune function. Interestingly, fish β2M 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.
AB - Background: β2-Microglobulin (β2M) is the light chain of major histocompatibility class I (MHC I) that binds non-covalently with the a heavy chain. Both proteins attach to the antigen peptide, presenting a complex to the T cell to be destroyed via the immune mechanism. Methodology/Principal Findings: In this study, a cDNA sequence encoding β2M in the Asian seabass (Lates calcarifer) was identified and analyzed using in silico approaches to predict and characterize its functional domain. The β2M 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 β2M sequences from other species studied thus far. Alignment of the IGc1 domains of β2M 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. Conclusion/Significance: As the L. calcarifer β2M protein analyzed in this study contains a functional domain similar to that of β2M proteins in other species, it can be postulated that the β2M proteins from L. calcarifer and other organisms are derived from a common ancestor and thus have a similar immune function. Interestingly, fish β2M 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.
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U2 - 10.1371/journal.pone.0013159
DO - 10.1371/journal.pone.0013159
M3 - Article
VL - 5
JO - PLoS One
JF - PLoS One
SN - 1932-6203
IS - 10
M1 - e13159
ER -