Functional Analysis of a Fibronectin Binding Protein of Streptococcus parasanguinis FW213
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Functional Analysis of a Fibronectin Binding Protein of Streptococcus parasanguinis FW213 Yi‑Ywan M. Chen1,2,3 · Pei‑Shan Lu2 · Pei‑Hua Tsai2 · Cheng‑Hsun Chiu3 Received: 1 March 2020 / Accepted: 28 July 2020 © Springer Science+Business Media, LLC, part of Springer Nature 2020
Abstract Streptococcus parasanguinis is a primary colonizer of dental plaque and an opportunistic pathogen for subacute endocarditis. A putative fibronectin binding protein (Spaf_1409) that lacks both an N-terminal signal peptide and a C-terminal cell wall-anchoring motif was identified from the S. parasanguinis FW213 genome. Spaf_1409 was abundantly present in the cytoplasm and also was found in the cell wall preparation and culture supernatant. By using an isogenic mutant strain, MPH4, Spaf_1409 was found to mediate the binding of S. parasanguinis FW213 to fibronectin. Inactivation of Spaf_1409 did not significantly alter the mass of static biofilm, but reduced the resistance of S. parasanguinis against the shearing force in a flow cell biofilm system, resulting in scattered biofilm. The mortality in Galleria mellonella larvae infected with MPH4 was higher than in those infected with wild-type S. parasanguinis. However, fewer viable bacterial cells were recovered from larvae infected with MPH4, compared to those infected with wild-type S. parasanguinis, up to 42 h post infection, suggesting that the infection by MPH4, but not the growth, was responsible for the elevated mortality. The phagocytic analysis using flow cytometry indicated that Spaf_1409 participates in the recognition of S. parasanguinis FW213 by RAW264.7 macrophages, suggesting that inactivation of Spaf_1409 intensified the immune responses in larvae, leading to larval death. Taken together, the data indicate that Spaf_1409 plays different roles in the development of dental biofilm and in systemic infections.
Introduction Fibronectin, a high molecular weight adhesive glycoprotein, exists widely on host tissues and in the bloodstream. Pathogenic bacteria such as Streptococcus spp. and Staphylococcus spp. are known to possess multiple fibronectin binding proteins (FBPs) which can facilitate bacterial interaction with hosts and establish infections [1]. Similar to other members of the microbial surface component-recognizing adhesive matrix molecules (MSCRAMMs), the structural Electronic supplementary material The online version of this article (https://doi.org/10.1007/s00284-020-02152-7) contains supplementary material, which is available to authorized users. * Yi‑Ywan M. Chen [email protected] 1
Department of Microbiology and Immunology, College of Medicine, Chang Gung University, 259 Wen‑Hwa 1st Road, Guishan Dist., Taoyuan City 333, Taiwan
2
Graduate Institute of Biomedical Sciences, College of Medicine, Chang Gung University, Taoyuan, Taiwan
3
Molecular Infectious Disease Research Center, Chang Gung Memorial Hospital, Linkou, Taiwan
organization and adhesion mechanism of FBPs generally are similar among species [2]. Thus far, two types of FBPs have
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