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Functional and Structural Characterization of the Antiphagocytic Properties of a Novel Transglutaminase from Streptococcus suis*

Jie Yu,Yaya Pian,Jingpeng Ge,Jie Guo,Yuling Zheng,Hua Jiang,Huai-jie Hao,Yuan Yuan,Yongqiang Jiang,Maojun Yang

Published 2015 in Journal of Biological Chemistry

ABSTRACT

Background: SsTGase was a newly identified secreted immunogenic protein of S. suis 2. Results: Anti-phagocytic ability of SsTGase-N was dependent on its TGase activity, and its crystal structure revealed that dimerization was crucial for maintaining functional activities. Conclusion: SsTGase was a novel virulence factor of Ss2 by acting as a TGase in dimer form. Significance: The presented research suggested that SsTGase could serve as a new therapeutic target. Streptococcus suis serotype 2 (Ss2) is an important swine and human zoonotic pathogen. In the present study, we identified a novel secreted immunogenic protein, SsTGase, containing a highly conserved eukaryotic-like transglutaminase (TGase) domain at the N terminus. We found that inactivation of SsTGase significantly reduced the virulence of Ss2 in a pig infection model and impaired its antiphagocytosis in human blood. We further solved the crystal structure of the N-terminal portion of the protein in homodimer form at 2.1 Å. Structure-based mutagenesis and biochemical studies suggested that disruption of the homodimer directly resulted in the loss of its TGase activity and antiphagocytic ability. Characterization of SsTGase as a novel virulence factor of Ss2 by acting as a TGase would be beneficial for developing new therapeutic agents against Ss2 infections.

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