- The type II histidine triad protein HtpsC facilitates invasion of epithelial cells by highly virulent Streptococcus suis serotype 2
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Yunjun Lu , Shu Li , Xiaodong Shen , Yan Zhao , Dongming Zhou , Dan Hu , Xushen Cai , Lixia Lu , Xiaohui Xiong , Ming Li , Min Cao
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J. Microbiol. 2021;59(10):949-957. Published online September 7, 2021
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DOI: https://doi.org/10.1007/s12275-021-1129-1
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Streptococcus suis serotype 2 (S. suis 2) is an important zoonotic
pathogen that presents a significant threat both to pigs
and to workers in the pork industry. The initial steps of S. suis
2 pathogenesis are unclear. In this study, we found that the
type II histidine triad protein HtpsC from the highly virulent
Chinese isolate 05ZYH33 is structurally similar to internalin
A (InlA) from Listeria monocytogenes, which plays an important
role in mediating listerial invasion of epithelial cells. To
determine if HtpsC and InlA function similarly, an isogenic
htpsC mutant (ΔhtpsC) was generated in S. suis by homologous
recombination. The htpsC deletion strain exhibited a
diminished ability to adhere to and invade epithelial cells from
different sources. Double immunofluorescence microscopy
also revealed reduced survival of the ΔhtpsC mutant after cocultivation
with epithelium. Adhesion to epithelium and invasion
by the wild type strain was inhibited by a monoclonal
antibody against E-cadherin. In contrast, the htpsC-deficient
mutant was unaffected by the same treatment, suggesting that
E-cadherin is the host-cell receptor that interacts with HtpsC
and facilitates bacterial internalization. Based on these results,
we propose that HtpsC is involved in the process by which
S. suis 2 penetrates host epithelial cells, and that this protein
is an important virulence factor associated with cell adhesion
and invasion.
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Citations
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- Rapid and specific detection of Streptococcus suis serotype 2 using a RPA–PfAgo system coupled with fluorescence and lateral flow dipstick
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- Functional Definition of LuxS, an Autoinducer-2 (AI-2) Synthase and Its Role in Full Virulence of Streptococcus suis Serotype 2
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Min Cao , Youjun Feng , Changjun Wang , Feng Zheng , Ming Li , Hui Liao , Yinghua Mao , Xiuzhen Pan , Jing Wang , Dan Hu , Fuquan Hu , Jiaqi Tang
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J. Microbiol. 2011;49(6):1000-1011. Published online December 28, 2011
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DOI: https://doi.org/10.1007/s12275-011-1523-1
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Quorum sensing is a widespread chemical communication in response to fluctuation of bacterial population density, and has been implicated into bacterial biofilm formation and regulation of expression of virulence factors. The luxS gene product, S-ribosylhomocysteinase, catalizes the last committed step in biosynthetic pathway of autoinducer 2 (AI-2), a signaling molecule for inter-species quorum sensing. We found a luxS homologue in 05ZYH33, an epidemic strain of Streptococcus suis serotype 2 (SS2) in China. A luxS null mutant (ΔluxS) of 05ZYH33 strain was obtained using an approach of homologous recombination. LuxS was determined to be required for AI-2 production in 05ZYH33 strain of S. suis 2. Inactivation of luxS gene led to a wide range of phenotypic changes including thinner capsular walls, increased tolerance to H2O2, reduced adherence capacity to epithelial cells, etc. In particular, loss of LuxS impaired dramatically its full virulence of SS2 in experimental model of piglets, and functional complementation restored it nearly to the level of parent strain. Genome-wide transcriptome analyses suggested that some known virulence factors such as CPS are down-regulated in the ΔluxS mutant, which might in part explain virulence attenuation by luxS deletion. Similarly, 29 of 71 genes with different expression level were proposed to be targets candidate regulated by LuxS/AI-2-dependent quorum sensing.
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