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Three goose-type lysozymes in the gastropod Oncomelania hupensis: cDNA sequences and lytic activity of recombinant proteins
Zhang, Shu H.1; Zhu, Dan D.1; Chang, Ming X.1; Zhao, Qin P.2; Jiao, Ran1; Huang, Bei1; Fu, Jian P.1; Liu, Zhi X.1; Nie, P.1; Nie, P (reprint author), Chinese Acad Sci, Inst Hydrobiol, State Key Lab Freshwater Ecol & Biotechnol, Wuhan 430072, Hubei Province, Peoples R China
2012
Source PublicationDEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY
ISSN0145-305X
Volume36Issue:1Pages:241-246
AbstractThree goose-type (g-type) lysozymes, designated as OHLysG1, OHLysG2 and OHLysG3 were identified from expressed sequence tags (ESTs) of a gastropod Oncomelania hupensis, the intermediate host of Schistosoma japonicum. The full cDNA sequences of OHLysG1, OHLysG2 and OHLysG3 consisted of 735, 909 and 808 nucleotides, with an open reading frame of 198, 214 and 249 codons containing a 21, 7 and 8 amino acid (aa) signal peptide at the N-terminus, respectively. The three g-type lysozymes shared conserved features with other g-type lysozymes, such as the substrate binding sites, the catalytic residues critical for the fundamental structure and function of g-type lysozymes. It seems possible that g-type lysozymes in molluscs shared one conserved cysteine with those in birds and mammals, and six conserved cysteines were observed for mollusc g-type lysozymes, with two unique cysteines present in the g-type lysozymes of O. hupensis. The three lysozyme genes were expressed mainly in hepatopancreas, with relatively low expression level observed in head-foot muscle and intestine. When comparing S. japonicum-infected and uninfected snails, significant increase (P < 0.05) was observed for all the three lysozymes in infected snails, with the highest increase detected in hepatopancreas, and lowest in intestine, implying their defensive role in the host-parasite, i.e. snail-trematode system. The three recombinant lysozymes expressed in Escherichia coil strain M15 showed lytic activity against Aeromonas hydrophila, Vibrio fluvialis, Aeromonas sobria and Micrococcus lysodeikticus. In conclusion, the finding of three g-type lysozymes in O. hupensis provides structural and functional evidence of multiple g-type lysozymes in gastropod, which may have evolutional implication in the snail-trematode system. (C) 2011 Elsevier Ltd. All rights reserved.; Three goose-type (g-type) lysozymes, designated as OHLysG1, OHLysG2 and OHLysG3 were identified from expressed sequence tags (ESTs) of a gastropod Oncomelania hupensis, the intermediate host of Schistosoma japonicum. The full cDNA sequences of OHLysG1, OHLysG2 and OHLysG3 consisted of 735, 909 and 808 nucleotides, with an open reading frame of 198, 214 and 249 codons containing a 21, 7 and 8 amino acid (aa) signal peptide at the N-terminus, respectively. The three g-type lysozymes shared conserved features with other g-type lysozymes, such as the substrate binding sites, the catalytic residues critical for the fundamental structure and function of g-type lysozymes. It seems possible that g-type lysozymes in molluscs shared one conserved cysteine with those in birds and mammals, and six conserved cysteines were observed for mollusc g-type lysozymes, with two unique cysteines present in the g-type lysozymes of O. hupensis. The three lysozyme genes were expressed mainly in hepatopancreas, with relatively low expression level observed in head-foot muscle and intestine. When comparing S. japonicum-infected and uninfected snails, significant increase (P < 0.05) was observed for all the three lysozymes in infected snails, with the highest increase detected in hepatopancreas, and lowest in intestine, implying their defensive role in the host-parasite, i.e. snail-trematode system. The three recombinant lysozymes expressed in Escherichia coli strain M15 showed lytic activity against Aeromonas hydrophila, Vibrio fluvialis, Aeromonas sobria and Micrococcus lysodeikticus. In conclusion, the finding of three g-type lysozymes in O. hupensis provides structural and functional evidence of multiple g-type lysozymes in gastropod, which may have evolutional implication in the snail-trematode system. (C) 2011 Elsevier Ltd. All rights reserved.
SubtypeArticle
KeywordGoose-type Lysozyme Lytic Activity Recombinant Protein Oncomelania Hupensis Mollusc
Department[Zhang, Shu H.; Zhu, Dan D.; Chang, Ming X.; Jiao, Ran; Huang, Bei; Fu, Jian P.; Liu, Zhi X.; Nie, P.] Chinese Acad Sci, Inst Hydrobiol, State Key Lab Freshwater Ecol & Biotechnol, Wuhan 430072, Hubei Province, Peoples R China; [Zhao, Qin P.] Wuhan Univ, Sch Basic Med Sci, Dept Parasitol, Wuhan 430071, Hubei Province, Peoples R China
DOI10.1016/j.dci.2011.06.014
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine
Funding OrganizationChinese Academy of Sciences[KSCX2-YW-N-055]; National Natural Science Foundation of China[30770353] ; Chinese Academy of Sciences[KSCX2-YW-N-055]; National Natural Science Foundation of China[30770353] ; Chinese Academy of Sciences[KSCX2-YW-N-055]; National Natural Science Foundation of China[30770353] ; Chinese Academy of Sciences[KSCX2-YW-N-055]; National Natural Science Foundation of China[30770353]
Indexed BySCI
Language英语
WOS Research AreaImmunology ; Zoology
WOS SubjectImmunology ; Zoology
WOS IDWOS:000299390300028
WOS KeywordMOLECULAR-CLONING ; CHLAMYS-FARRERI ; CHICKEN-TYPE ; EGG-WHITE ; C-TYPE ; GENE ; EXPRESSION ; EVOLUTION ; ORGANIZATION ; MOLLUSKS
Funding OrganizationChinese Academy of Sciences[KSCX2-YW-N-055]; National Natural Science Foundation of China[30770353] ; Chinese Academy of Sciences[KSCX2-YW-N-055]; National Natural Science Foundation of China[30770353] ; Chinese Academy of Sciences[KSCX2-YW-N-055]; National Natural Science Foundation of China[30770353] ; Chinese Academy of Sciences[KSCX2-YW-N-055]; National Natural Science Foundation of China[30770353]
Citation statistics
Cited Times:17[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.ihb.ac.cn/handle/342005/16737
Collection鱼类生物学及渔业生物技术研究中心_期刊论文
Corresponding AuthorNie, P (reprint author), Chinese Acad Sci, Inst Hydrobiol, State Key Lab Freshwater Ecol & Biotechnol, Wuhan 430072, Hubei Province, Peoples R China
Affiliation1.Chinese Acad Sci, Inst Hydrobiol, State Key Lab Freshwater Ecol & Biotechnol, Wuhan 430072, Hubei Province, Peoples R China
2.Wuhan Univ, Sch Basic Med Sci, Dept Parasitol, Wuhan 430071, Hubei Province, Peoples R China
Recommended Citation
GB/T 7714
Zhang, Shu H.,Zhu, Dan D.,Chang, Ming X.,et al. Three goose-type lysozymes in the gastropod Oncomelania hupensis: cDNA sequences and lytic activity of recombinant proteins[J]. DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,2012,36(1):241-246.
APA Zhang, Shu H..,Zhu, Dan D..,Chang, Ming X..,Zhao, Qin P..,Jiao, Ran.,...&Nie, P .(2012).Three goose-type lysozymes in the gastropod Oncomelania hupensis: cDNA sequences and lytic activity of recombinant proteins.DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,36(1),241-246.
MLA Zhang, Shu H.,et al."Three goose-type lysozymes in the gastropod Oncomelania hupensis: cDNA sequences and lytic activity of recombinant proteins".DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY 36.1(2012):241-246.
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