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Histo-blood group antigens in Crassostrea gigas and binding profiles with GⅡ.4 Norovirus

Histo-blood group antigens in Crassostrea gigas and binding profiles with GⅡ.4 Norovirus

作     者:MA Liping LIU Hui SU Laij in ZHAO Feng ZHOU Deqing DUAN Delin 马丽萍;刘慧;苏来金;赵峰;周德庆;段德麟

作者机构:Key Laboratory of Experimental Marine BiologyInstitute of OceanologyChinese Academy of SciencesQingdao 266071China Key Laboratory for Sustainable Utilization of Marine Fisheries ResourcesMinistry of AgricultureYellow Sea Fisheries Research InstituteChinese Academy of Fishery SciencesQingdao 266071China Laboratory for Marine Biology and BiotechnologyQingdao National Laboratory for Marine Science and TechnologyQingdao 266071China 

出 版 物:《Journal of Oceanology and Limnology》 (海洋湖沼学报(英文))

年 卷 期:2018年第36卷第4期

页      面:1383-1391页

核心收录:

学科分类:090603[农学-临床兽医学] 12[管理学] 1204[管理学-公共管理] 120402[管理学-社会医学与卫生事业管理(可授管理学、医学学位)] 1004[医学-公共卫生与预防医学(可授医学、理学学位)] 09[农学] 0906[农学-兽医学] 10[医学] 

基  金:Supported by the National Natural Science Foundation of China(No.31471663) the Qingdao Postdoctoral Application Research Project 

主  题:Crassostrea gigas norovirus histo-blood group antigen binding 

摘      要:Noroviruses(NoVs) are the main cause of viral gastroenteritis outbreaks worldwide, and oysters are the most common carriers of NoV contamination and transmission. NoVs bind specifically to oyster tissues through histo-blood group antigens(HBGAs), and this facilitates virus accumulation and increases virus persistence in oysters. To investigate the interaction of HBGAs in Pacific oysters with GⅡ.4 NoV, we examined HBGAs with ELISAs and investigated binding patterns with oligosaccharide-binding assays using P particles as a model of five GⅡ.4 NoV capsids. The HBGAs in the gut and gills exhibited polymorphisms. In the gut, type A was detected(100%), whereas type Leb(91.67%) and type A(61.11%) were both observed in the gills. Moreover, we found that seasonal NoV gastroenteritis outbreaks were not significantly associated with the specific HBGAs detected in the oyster gut and gills. In the gut, we found that strain-2006 b and strain-96/96 US bound to type A and H1 but only weakly bound to type Leb; in contrast, the Camberwell and Hunter strains exhibited weak binding to types H1 and Ley, and strain-Sakai exhibited no binding to any HBGA type. In the gills, strain-96/96 US and strain-2006 b bound to type Leb but only weakly bound to type H1; strains Camberwell, Hunter, and Sakai did not bind to oyster HBGAs. Assays for oligosaccharide binding to GⅡ.4 NoV P particles showed that strain-95/96 US and strain-2006 b strongly bound to type A, B, H1, Leb, and Ley oligosaccharides, while strains Camberwell and Hunter showed weak binding ability to type H1 and Ley oligosaccharides and strain-Sakai showed weak binding ability to type Leb and Ley oligosaccharides. Our study presents new information and enhances understanding about the mechanism for NoV accumulation in oysters. Further studies of multiple NoV-tissue interactions might assist in identifying new or improved strategies for minimizing contamination, including HBGA-based attachment inhibition or depuration.

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