Two Goose-Type Lysozymes in Mytilus galloprovincialis: Possible Function Diversification and Adaptive Evolution

	Two Goose-Type Lysozymes in Mytilus galloprovincialis: Possible Function Diversification and Adaptive Evolution
	Wang, Qing; Zhang, Linbao; Zhao, Jianmin; You, Liping; Wu, Huifeng
发表期刊	PLOS ONE
ISSN	1932-6203
	2012-09-21
卷号	7 期号:9 页码:e45148
关键词	Oyster Crassostrea-virginica I-type Lysozymes Lytic Activity Molecular Adaptation Recombinant Protein Positive Selection Stomach Lysozymes Eastern Oyster Egg-white Phylogenetic Analysis
产权排序	[Wang, Qing; Zhang, Linbao; Zhao, Jianmin; You, Liping; Wu, Huifeng] Chinese Acad Sci, Yantai Inst Coastal Zone Res, Key Lab Coastal Zone Environm Proc, CAS,Shandong Prov Key Lab Coastal Zone Environm, Yantai, Peoples R China
通讯作者	Zhao, JM (reprint author), Chinese Acad Sci, Yantai Inst Coastal Zone Res, Key Lab Coastal Zone Environm Proc, CAS,Shandong Prov Key Lab Coastal Zone Environm, Yantai, Peoples R China.
作者部门	中科院海岸带环境过程与生态修复重点实验室
英文摘要	Two goose-type lysozymes (designated as MGgLYZ1 and MGgLYZ2) were identified from the mussel Mytilus galloprovincialis. MGgLYZ1 mRNA was widely expressed in the examined tissues and responded sensitively to bacterial challenge in hemocytes, while MGgLYZ2 mRNA was predominately expressed and performed its functions in hepatopancreas. However, immunolocalization analysis showed that both these lysozymes were expressed in all examined tissues with the exception of adductor muscle. Recombinant MGgLYZ1 and MGgLYZ2 could inhibit the growth of several Gram-positive and Gram-negative bacteria, and they both showed the highest activity against Pseudomonas putida with the minimum inhibitory concentration (MIC) of 0.95-1.91 mu M and 1.20-2.40 mu M, respectively. Protein sequences analysis revealed that MGgLYZ2 had lower isoelectric point and less protease cutting sites than MGgLYZ1. Recombinant MGgLYZ2 exhibited relative high activity at acidic pH of 4-5, while MGgLYZ1 have an optimum pH of 6. These results indicated MGgLYZ2 adapted to acidic environment and perhaps play an important role in digestion. Genomic structure analysis suggested that both MGgLYZ1 and MGgLYZ2 genes are composed of six exons with same length and five introns, indicating these genes were conserved and might originate from gene duplication during the evolution. Selection pressure analysis showed that MGgLYZ1 was under nearly neutral selection while MGgLYZ2 evolved under positive selection pressure with three positively selected amino acid residues (Y-102, L-200 and S-202) detected in the mature peptide. All these findings suggested MGgLYZ2 perhaps served as a digestive lysozyme under positive selection pressure during the evolution while MGgLYZ1 was mainly involved in innate immune responses.; Two goose-type lysozymes (designated as MGgLYZ1 and MGgLYZ2) were identified from the mussel Mytilus galloprovincialis. MGgLYZ1 mRNA was widely expressed in the examined tissues and responded sensitively to bacterial challenge in hemocytes, while MGgLYZ2 mRNA was predominately expressed and performed its functions in hepatopancreas. However, immunolocalization analysis showed that both these lysozymes were expressed in all examined tissues with the exception of adductor muscle. Recombinant MGgLYZ1 and MGgLYZ2 could inhibit the growth of several Gram-positive and Gram-negative bacteria, and they both showed the highest activity against Pseudomonas putida with the minimum inhibitory concentration (MIC) of 0.95-1.91 mu M and 1.20-2.40 mu M, respectively. Protein sequences analysis revealed that MGgLYZ2 had lower isoelectric point and less protease cutting sites than MGgLYZ1. Recombinant MGgLYZ2 exhibited relative high activity at acidic pH of 4-5, while MGgLYZ1 have an optimum pH of 6. These results indicated MGgLYZ2 adapted to acidic environment and perhaps play an important role in digestion. Genomic structure analysis suggested that both MGgLYZ1 and MGgLYZ2 genes are composed of six exons with same length and five introns, indicating these genes were conserved and might originate from gene duplication during the evolution. Selection pressure analysis showed that MGgLYZ1 was under nearly neutral selection while MGgLYZ2 evolved under positive selection pressure with three positively selected amino acid residues (Y-102, L-200 and S-202) detected in the mature peptide. All these findings suggested MGgLYZ2 perhaps served as a digestive lysozyme under positive selection pressure during the evolution while MGgLYZ1 was mainly involved in innate immune responses.
文章类型	Article
资助机构	NSFC [30901115, 31172388]; Chinese Academy of Sciences; Open Project Program of the Key Laboratory of Marine Bio-resources Sustainable Utilization; SCSIO; CAS; Department of Science and Technology of Yantai City of China [2011067]
收录类别	SCI
语种	英语
关键词[WOS]	OYSTER CRASSOSTREA-VIRGINICA ; I-TYPE LYSOZYMES ; LYTIC ACTIVITY ; MOLECULAR ADAPTATION ; RECOMBINANT PROTEIN ; POSITIVE SELECTION ; STOMACH LYSOZYMES ; EASTERN OYSTER ; EGG-WHITE ; PHYLOGENETIC ANALYSIS
研究领域[WOS]	Science & Technology - Other Topics
WOS记录号	WOS:000309392800028
引用统计	被引频次：32[WOS] [WOS记录] [WOS相关记录]
文献类型	期刊论文
条目标识符	http://ir.yic.ac.cn/handle/133337/6074
专题	中国科学院海岸带环境过程与生态修复重点实验室
作者单位	Chinese Acad Sci, Yantai Inst Coastal Zone Res, Key Lab Coastal Zone Environm Proc, CAS,Shandong Prov Key Lab Coastal Zone Environm, Yantai, Peoples R China
推荐引用方式 GB/T 7714	Wang, Qing,Zhang, Linbao,Zhao, Jianmin,et al. Two Goose-Type Lysozymes in Mytilus galloprovincialis: Possible Function Diversification and Adaptive Evolution[J]. PLOS ONE,2012,7(9):e45148.
APA	Wang, Qing,Zhang, Linbao,Zhao, Jianmin,You, Liping,&Wu, Huifeng.(2012).Two Goose-Type Lysozymes in Mytilus galloprovincialis: Possible Function Diversification and Adaptive Evolution.PLOS ONE,7(9),e45148.
MLA	Wang, Qing,et al."Two Goose-Type Lysozymes in Mytilus galloprovincialis: Possible Function Diversification and Adaptive Evolution".PLOS ONE 7.9(2012):e45148.

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