中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Three clip domain serine proteases (cSPs) and one clip domain serine protease homologue (cSPH) identified from haemocytes and eyestalk cDNA libraries of swimming crab Portunus trituberculatus

文献类型:期刊论文

作者Li, Qianqian1,2; Cui, Zhaoxia1; Liu, Yuan1; Wang, Shuangyan1,2; Song, Chengwen1,2
刊名FISH & SHELLFISH IMMUNOLOGY
出版日期2012-04-01
卷号32期号:4页码:565-571
关键词Portunus trituberculatus Clip domain Serine protease Serine protease homologue mRNA expression profile
ISSN号1050-4648
通讯作者Cui, ZX (reprint author), Chinese Acad Sci, Inst Oceanol, EMBL, 7 Nanhai Rd, Qingdao 266071, Peoples R China.
英文摘要Four genes including three clip domain serine proteases (PtcSP1, PtcSP2 and PtcSP3) and one clip domain serine protease homologue (PtcSPH) of the swimming crab Portunus trituberculatus (Decapoda: Brachyura: Portunidae) were characterized based on analysis of expressed sequence tags from haemocytes and eyestalk cDNA libraries. The relative four peptidases, which share high structural similarity to the clip-SPs of other arthropod species, appeared to possess a clip domain at the N-terminus and an enzymatically active serine protease domain at the C-terminus except PtcSPH for its second catalytic residue Asp. (D) replaced by Ala (A). Alignment among the four full-sequences showed that PtcSP2 and PtcSP3 had the highest identical score (58%) while the similarity of other sequences was lower than 24%. The mRNA transcripts of PtcSPs and PtcSPH could be detected widely in all the examined tissues with remarkable different expression levels. The temporal expressions of PtcSPs and PtcSPH demonstrated different time-dependent expression pattern post Vibrio alginolyticus, Micrococcus luteus. and Pichia pastoris challenge. Especially, the expression of PtcSPH transcripts showed greater change against V. alginolyticus compared with the other two microorganisms. These findings suggest that PtcSPs and PtcSPH play different roles in the antibacterial defence mechanism of P. trituberculatus crab. (C) 2012 Elsevier Ltd. All rights reserved.
学科主题Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences
收录类别SCI
原文出处10.1016/j.fsi.2012.01.006
语种英语
WOS记录号WOS:000301827100007
公开日期2013-09-24
源URL[http://ir.qdio.ac.cn/handle/337002/12401]  
专题海洋研究所_海洋生物技术研发中心
海洋研究所_实验海洋生物学重点实验室
作者单位1.Chinese Acad Sci, Inst Oceanol, EMBL, Qingdao 266071, Peoples R China
2.Chinese Acad Sci, Grad Univ, Beijing 100039, Peoples R China
推荐引用方式
GB/T 7714
Li, Qianqian,Cui, Zhaoxia,Liu, Yuan,et al. Three clip domain serine proteases (cSPs) and one clip domain serine protease homologue (cSPH) identified from haemocytes and eyestalk cDNA libraries of swimming crab Portunus trituberculatus[J]. FISH & SHELLFISH IMMUNOLOGY,2012,32(4):565-571.
APA Li, Qianqian,Cui, Zhaoxia,Liu, Yuan,Wang, Shuangyan,&Song, Chengwen.(2012).Three clip domain serine proteases (cSPs) and one clip domain serine protease homologue (cSPH) identified from haemocytes and eyestalk cDNA libraries of swimming crab Portunus trituberculatus.FISH & SHELLFISH IMMUNOLOGY,32(4),565-571.
MLA Li, Qianqian,et al."Three clip domain serine proteases (cSPs) and one clip domain serine protease homologue (cSPH) identified from haemocytes and eyestalk cDNA libraries of swimming crab Portunus trituberculatus".FISH & SHELLFISH IMMUNOLOGY 32.4(2012):565-571.

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来源:海洋研究所

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