Feng Liu1,2,3, Jinquan Li1,4, Kang Yan1,2,3, Huan Li1,2,3, Chengfeng Sun1,2,3, Shuo Zhang5, Fangyan Yuan5, Xiangru Wang1,2,3, Chen Tan1,2,3, Huanchun Chen1,2,3, Weicheng Bei1,2,3. 1. State Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan, Hubei, China. 2. The Cooperative Innovation Center for Sustainable Pig Production, Huazhong Agricultural University, Wuhan, Hubei, China. 3. Key Laboratory of Development of Veterinary Diagnostic Products of Ministry of Agriculture, Huazhong Agricultural University, Wuhan, Hubei, China. 4. State Key Laboratory of Agricultural Microbiology, College of Food Science and Technology, Huazhong Agricultural University, Wuhan, Hubei, China. 5. Hubei Key Laboratory of Animal Embryo and Molecular Breeding, Institute of Animal Husbandry and Veterinary Sciences, Hubei Academy of Agricultural Sciences, Wuhan, China.
Abstract
Background: SsPepO is an important virulence in Streptococcus suis. Methods: In this study, we showed that SsPepO contributes to the human fibronectin-mediated adherence ability of S. suis to human brain microvascular endothelial cells. Results: The addition of an antifibronectin antibody or an arginine-glycine-aspartic acid peptide that blocks fibronectin binding to integrins significantly reduced adherence of the wild-type but not the SspepO mutant strain, indicating the importance of the SsPepO-fibronectin-integrin interaction for S. suis cellular adherence. Conclusions: By analyzing Evans blue extravasation in vivo, we showed that the interaction between SsPepO and human fibronectin significantly increased permeability of the blood-brain barrier. Furthermore, the SspepO mutant caused lower bacterial loads in the brain than wild-type S. suis in models of meningitis. These data demonstrate that SsPepO is a fibronectin-binding protein, which plays a contributing role in the development of S. suis meningitis.
Background: SsPepO is an important virulence in Streptococcus suis. Methods: In this study, we showed that SsPepO contributes to the humanfibronectin-mediated adherence ability of S. suis to human brain microvascular endothelial cells. Results: The addition of an antifibronectin antibody or an arginine-glycine-aspartic acid peptide that blocks fibronectin binding to integrins significantly reduced adherence of the wild-type but not the SspepO mutant strain, indicating the importance of the SsPepO-fibronectin-integrin interaction for S. suis cellular adherence. Conclusions: By analyzing Evans blue extravasation in vivo, we showed that the interaction between SsPepO and humanfibronectin significantly increased permeability of the blood-brain barrier. Furthermore, the SspepO mutant caused lower bacterial loads in the brain than wild-type S. suis in models of meningitis. These data demonstrate that SsPepO is a fibronectin-binding protein, which plays a contributing role in the development of S. suismeningitis.
Authors: Livia A Alves; Geovanny C Salvatierra; Victor A Freitas; José F Höfling; Débora C Bastos; Thaís L S Araujo; Renata O Mattos-Graner Journal: Front Microbiol Date: 2022-04-18 Impact factor: 5.640