Positive selection drives lactoferrin evolution in mammals.
Lactoferrin (LF) is a member of the transferrin family that is abundantly expressed and secreted by glandular epithelial cells. The biological functions of LF involve in iron homeostasis regulation of the body and antibacterial activity. Previous studies demonstrated that it had a high cationic N-terminal domain that could interact with glycosaminoglycans, lipopolysaccharides and the bacterial virulence protein. Two anti-microbial peptides, lactoferricin (LFcin) and lactoferrampin (LFampin), were also isolated and identified in N-terminal of LF. Although the antibacterial mechanism was carefully studied, little was known about the molecular evolution of LF. In this study, we estimated the nonsynonymous-to-synonymous substitution ratios ( ) per site using maximum likelihood method to analyze the LF evolution. The results of omega > 1 and five identified positive selection sites of amino acid suggested that the evolution of LF gene was characterized by positive selection. Further study found that the positive selection sites were either located in the LF-bacteria binding region or the peptides of LFcin and LFampin, indicating that the selection pressure was related to LF-bacteria interaction. The identification of these sites may contribute to the mechanism of bacteria-LF interaction.
Liang
Guo Ming
GM
Animal Science Department, Huazhong Agricultural University, Wuhan, People's Republic of China.
Jiang
Xun Ping
XP
D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry / Q000378:metabolism; D001419:Bacteria / Q000378:metabolism; D001665:Binding Sites / Q000235:genetics; D019143:Evolution, Molecular; D006801:Humans; D007781:Lactoferrin / Q000737:chemistry / Q000145:classification / Q000235:genetics* / Q000378:metabolism; D007782:Lactoglobulins / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D010802:Phylogeny; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012641:Selection, Genetic
D000900:Anti-Bacterial Agents; D007782:Lactoglobulins; D010446:Peptide Fragments; C502040:lactoferrampin; C082171:lactoferricin B; D007781:Lactoferrin
Mol Biol Evol. 2004 Jul;21(7):1264-77
15014154
Genetics. 1998 Mar;148(3):929-36
9539414
J Biol Inorg Chem. 2000 Dec;5(6):692-8
11128996
J Comput Chem. 2004 Oct;25(13):1605-12
15264254
Peptides. 2004 Feb;25(2):177-83
15062998
Mol Biol Evol. 2007 Aug;24(8):1586-91
17483113
Mol Microbiol. 1999 Apr;32(1):111-21
10216864
Acta Crystallogr D Biol Crystallogr. 1995 Sep 1;51(Pt 5):629-46
15299793
Biochimie. 2009 Jan;91(1):1-2
18957318
Genetics. 2000 May;155(1):431-49
10790415
Comp Biochem Physiol B Biochem Mol Biol. 2005 Jan;140(1):11-25
15621505
J Mol Evol. 2005 Apr;60(4):426-33
15883878
Cell Mol Life Sci. 2005 Nov;62(22):2588-98
16261252
J Mol Biol. 1999 Jun 4;289(2):303-17
10366507
Int J Antimicrob Agents. 2009 Apr;33(4):301.e1-8
18842395
Genetics. 2004 Oct;168(2):1041-51
15514074
J Mol Biol. 2001 Jun 8;309(3):751-61
11397094
Mol Biol Evol. 2001 Apr;18(4):639-47
11264416
Mar Genomics. 2008 Sep-Dec;1(3-4):95-101
21798159
Biochimie. 2009 Jan;91(1):141-54
18534196
Mol Biol Evol. 2005 Apr;22(4):1107-18
15689528
Cell Mol Life Sci. 2005 Nov;62(22):2576-87
16261253
Mol Biol Evol. 2007 Aug;24(8):1596-9
17488738
Biochimie. 2009 Jan;91(1):123-32
18573310
Biochimie. 2009 Jan;91(1):19-29
18573312
Biochim Biophys Acta. 1992 May 22;1121(1-2):130-6
1599934
Acta Crystallogr D Biol Crystallogr. 1999 Nov;55(Pt 11):1805-13
10531476
Biochimie. 2009 Jan;91(1):3-10
18541155
Comp Biochem Physiol B Biochem Mol Biol. 2005 Oct;142(2):129-41
16111909
J Mol Biol. 1997 Nov 28;274(2):222-36
9398529