論文

査読有り 国際誌
2022年3月17日

Triosephosphate isomerase of Streptococcus pneumoniae is released extracellularly by autolysis and binds to host plasminogen to promote its activation.

FEBS open bio
  • Satoru Hirayama
  • ,
  • Hisanori Domon
  • ,
  • Takumi Hiyoshi
  • ,
  • Toshihito Isono
  • ,
  • Hikaru Tamura
  • ,
  • Karin Sasagawa
  • ,
  • Fumio Takizawa
  • ,
  • Yutaka Terao

記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1002/2211-5463.13396

Recruitment of plasminogen is an important infection strategy of the human pathogen Streptococcus pneumoniae to invade host tissues. In Streptococcus aureus, triosephosphate isomerase (TPI) has been reported to bind plasminogen. In this study, the TPI of S. pneumoniae (TpiA) was identified through proteomic analysis of bronchoalveolar lavage fluid from a murine pneumococcal pneumonia model. The binding kinetics of recombinant pneumococcal TpiA with plasminogen were characterized using surface plasmon resonance (SPR, Biacore), ligand blot analyses, and enzyme-linked immunosorbent assay. Enhanced plasminogen activation and subsequent degradation by plasmin were also shown. Release of TpiA into the culture medium was observed to be dependent on autolysin. These findings suggest that S. pneumoniae releases TpiA via autolysis, which then binds to plasminogen and promotes its activation, thereby contributing to tissue invasion via degradation of the extracellular matrix.

リンク情報
DOI
https://doi.org/10.1002/2211-5463.13396
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/35298875
ID情報
  • DOI : 10.1002/2211-5463.13396
  • PubMed ID : 35298875

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