The outer membrane protein, OMP71, of Riemerella anatipestifer, mediates adhesion and virulence by binding to CD46 in ducks.

IF 3.7 1区 农林科学 Q1 VETERINARY SCIENCES Veterinary Research Pub Date : 2024-10-15 DOI:10.1186/s13567-024-01393-9
Yanhua Wang, Sen Li, Congran Ning, Rongkun Yang, Yaxin Wu, Xu Cheng, Jike Xu, Yi Wang, Fei Liu, Yang Zhang, Sishun Hu, Yuncai Xiao, Zili Li, Zutao Zhou
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Abstract

The Riemerella anatipestifer bacterium is known to cause infectious serositis in ducklings. Moreover, its adherence to the host's respiratory mucosa is a critical step in pathogenesis. Membrane cofactor protein (MCP; CD46) is a complement regulatory factor on the surface of eukaryotic cell membranes. Bacteria have been found to bind to this protein on host cells. Outer membrane proteins (OMPs) are necessary for adhesion, colonisation, and pathogenicity of Gram-negative bacteria; however, the mechanism by which R. anatipestifer adheres to duck cells remains unclear. In this study, pull-down assays and LC-MS/MS identified eleven OMPs interacting with duck CD46 (dCD46), with OMP71 exhibiting the strongest binding. The ability of an omp71 gene deletion strain to bind dCD46 is weaker than that of the wild-type strain, suggesting that this interaction is important. Further evidence of this interaction was obtained by synthesising OMP71 using an Escherichia coli recombinant protein expression system. Adhesion and invasion assays and protein and antibody blocking assays confirmed that OMP71 promoted the R. anatipestifer YM strain (RA-YM) adhesion to duck embryo fibroblasts (DEFs) by binding to CD46. Tests of the pathogenicity of a Δomp71 mutant strain of RA-YM on ducks compared to the wild-type parent supported the hypothesis that OMP71 was a key virulence factor of RA-YM. In summary, the finding that R. anatipestifer exploits CD46 to bind to host cells via OMP71 increases our understanding of the molecular mechanism of R. anatipestifer invasion. The finding suggests potential targets for preventing and treating diseases related to R. anatipestifer infection.

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鸭疫酵母菌的外膜蛋白 OMP71 通过与鸭体内的 CD46 结合,介导粘附和毒力。
已知锐孢霉菌(Riemerella anatipestifer)可导致雏鸭感染性血清炎。此外,它对宿主呼吸道粘膜的粘附是致病的关键一步。膜辅助因子蛋白(MCP;CD46)是真核细胞膜表面的一种补体调节因子。已发现细菌与宿主细胞上的这种蛋白结合。外膜蛋白(OMPs)是革兰氏阴性细菌粘附、定植和致病所必需的;然而,锐尖镰刀菌粘附鸭细胞的机制仍不清楚。在这项研究中,通过牵引试验和 LC-MS/MS 鉴定出 11 种与鸭 CD46(dCD46)相互作用的 OMPs,其中 OMP71 的结合力最强。OMP71基因缺失株与dCD46的结合能力弱于野生型株,表明这种相互作用非常重要。通过使用大肠杆菌重组蛋白表达系统合成 OMP71,进一步证明了这种相互作用。粘附和侵袭试验以及蛋白质和抗体阻断试验证实,OMP71通过与CD46结合,促进了锐蝽YM株(RA-YM)与鸭胚成纤维细胞(DEFs)的粘附。与野生型亲本相比,Δomp71突变株RA-YM对鸭的致病性试验支持了OMP71是RA-YM的关键致病因子的假设。总之,锐毒蜥利用CD46通过OMP71与宿主细胞结合的发现增加了我们对锐毒蜥入侵分子机制的了解。这一发现为预防和治疗与锐蝽感染有关的疾病提供了潜在靶点。
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来源期刊
Veterinary Research
Veterinary Research 农林科学-兽医学
CiteScore
7.00
自引率
4.50%
发文量
92
审稿时长
3 months
期刊介绍: Veterinary Research is an open access journal that publishes high quality and novel research and review articles focusing on all aspects of infectious diseases and host-pathogen interaction in animals.
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