Allelic functional variation of FimH among Salmonella enterica subspecies  

作　　者：Xiamei Kang Jiaqi Chen Xiao Zhou Abdelaziz Ed-Dra Min Yue 

机构地区：[1]Instituteof Preventive Veterinary Sciences&Department of Veterinary Medicine,Zhejiang University College of Animal Sciences,Hangzhou 310058,China [2]Laboratory of Engineering and Applied Technologies,Higher School of Technology,Sultan Moulay Slimane University,PB:591,Mghila University Campus,23000Beni Mellal,Morocco [3]Hainan Institute of Zhejiang University,Sanya,China [4]Zhejiang Provincial Key Laboratory of Preventive Veterinary Medicine,Hangzhou 310058,China

出　　处：《Animal Diseases》2023年第4期265-274,共10页动物疾病（英文）

基　　金：supported by the National Program on Key Research Project of China(2022YFC2604201);well as the European Union's Horizon 2020 Research and Innovation Programme under Grant Agreement No.861917-SAFFl,Zhejiang Provincial Key R&D Program of China(2023C03045);Hainan Provincial Joint Project of Sanya Yazhou Bay Science and Technology City(2021JJLH0083);Key Research and Development Program of Hangzhou(202203A08);District-level project for high-level innovative and entrepreneurial talents of"Zijinshan Talents Gaochun Plan"(202100677).

摘　　要：Salmonella enterica has a wide diversity,with numerous serovars belonging to six different subspecies with dynamic animal-host tropism.The FimH protein is the adhesin mediating binding to various cells,and slight amino acid discrepancy significantly affects the adherence capacities.To date,the general function of FimH variability across dif-ferent subspecies of Salmonella enterica has not been addressed.To investigate the biological functions of FimH among the six Salmonella enterica subspecies,the present study performed several assays to determine biofilm for-mation,Caenorhabditis elegans killing,and intestinal porcine enterocyte cell IPEC-J2 adhesion by using various FimH allele mutants.In general,allelic mutations in both the lectin and pilin domains of FimH could cause changes in bind-ing affnity,such as the N79S mutation.We also observed that the N79S variation in Salmonella Dublin increased the adhesive ability of IPEC-J2 cells.Moreover,a new amino acid substitution,T260M,within the pilin domain in one subspecies llb strain beneficial to binding to cells was highlighted in this study,even though the biofilm-forming and Caenorhabditis elegans-killing abilities exhibited no significant differences in variants.Combined with point muta-tions being a natural tendency due to positive selection in harsh environments,we speculate that allelic variation T26oM probably contributes to pathoadaptive evolution in Salmonella enterica subspecies llb.

关 键 词：Salmonella subspecies FimH Amino acid substitution BINDING Allelic variation 

分 类 号：Q95[生物学—动物学]