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A Choroid Plexus Epithelial Cell-based Model of the Human Blood-Cerebrospinal Fluid Barrier to Study Bacterial Infection from the Basolateral Side
Published on: May 6, 2016
HtpsB, a type II histidine triad protein of Streptococcus suis, contributes to bacterial virulence and blood-brain
Jingyan Fan1, Jinpeng Zhang1, Baiyi Chen1
1Key Laboratory of Applied Biotechnology on Animal Science & Veterinary Medicine of Zhejiang Province, Zhejiang Engineering Research Center for Veterinary Diagnostics & Advanced Technology, Zhejiang International Science and Technology Cooperation Base for Veterinary Medicine and Health Management, Belt and Road International Joint Laboratory for One Health and Food Safety, China-Australia Joint Laboratory for Animal Health Big Data Analytics, College of Veterinary Medicine of Zhejiang A&F University, Hangzhou, Zhejiang 311300, China.
Abstract:
Streptococcus suis (S. suis) is an important zoonotic pathogen that leads to serious diseases in pigs and humans, marked by conditions such as meningitis and septicemia. The histidine triad protein (HtP) family plays a significant role in the pathogenicity of S. suis. However, the specific function of HtpsB in the pathogenicity of S. suis remains unclear to date. In this study, we demonstrated that the gene deletion mutant ∆htpsB exhibited significantly reduced pathogenicity compared with SC19, both in vivo and in vitro. This attenuation was particularly evident in its reduced virulence and its impaired ability to disrupt and invade the blood-brain barrier (BBB). Furthermore, the adhesion, invasion, and toxicity of ∆htpsB to human brain microvascular endothelial cells (HBMECs) were diminished. HSPA8 was identified as an interacting partner of HtpsB in HBMECs, suggesting that it mediates the interaction between SS2 and HBMECs. These findings provide an important theoretical basis for a comprehensive analysis of the molecular mechanisms by which S. suis traverses the BBB to cause meningitis.
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