4.7 Article

OmpC, a novel factor H-binding surface protein, is dispensable for the adherence and virulence of Salmonella enterica serovar Typhimurium

期刊

VETERINARY MICROBIOLOGY
卷 259, 期 -, 页码 -

出版社

ELSEVIER
DOI: 10.1016/j.vetmic.2021.109157

关键词

S; Typhimurium; Complement; OmpC; Factor H-binding proteins; Virulence

资金

  1. Natural Science Foundation of Jiangsu Province [BK20190886]
  2. National Natural Science Foundation of China [32002301, 31672516, 31172300, 30670079]
  3. China Postdoctoral Science Foundation from Jiangsu Province [2019M661953, BE2016343]
  4. State Key Laboratory of Genetically Engineered Veterinary Vaccines [AGVSKL-ZD-202004]
  5. Priority Academic Program Development of Jiangsu Higher Education Institutions (PAPD)

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Salmonella enterica serovar Typhimurium utilizes strategies to evade host immune defenses, including binding FH to circumvent complement-mediated killing. OmpC was identified as an important FHBP in enhancing survival in serum, but not a critical virulence factor. These findings provide insights into Salmonella pathogenesis and potential therapeutic targets.
Salmonella enterica serovar Typhimurium utilizes a series of strategies to evade host innate immune defenses, including the serum complement system. Many microbial pathogens have evolved the ability to bind the complement regulatory protein factor H (FH) through their surface factor H-binding proteins (FHBPs) to circumvent the complement-mediated bactericidal effect. However, the roles of FHBPs in Salmonella pathogenesis are not well understood. In this study, we demonstrated that the survival of S. Typhimurium in human serum was decreased in a time and concentration dependent manner. Pre-incubation with FH attenuated the sensitivity of S. Typhimurium strain chi 3761 to complement-mediated serum killing, suggesting FH binding enhance survival in serum. We aimed to identify novel S. Typhimurium FHBPs and characterize their biological functions. Here, six potential FHBPs were identified by two-dimensional (2D)-Far-western blot, and three of them were further confirmed to bind FH by Far-western blot and dot blot. We found that deletion of ompC (delta ompC) significantly inhibited the survival of S. Typhimurium strain chi 3761 in human serum. Our results indicated that the ompC mutation does not affect chi 3761 adhesion to HeLa cells. Furthermore, a mice infection model showed that deletion of ompC had no significant effect on the histopathological lesions or viability compared with the wild-type strain chi 3761. In summary, these results suggested that OmpC is an important FHBP, but not a critical virulence factor of S. Typhimurium.

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