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

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 p...

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Autores principales: Hirayama, Satoru, Domon, Hisanori, Hiyoshi, Takumi, Isono, Toshihito, Tamura, Hikaru, Sasagawa, Karin, Takizawa, Fumio, Terao, Yutaka
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9157410/
https://www.ncbi.nlm.nih.gov/pubmed/35298875
http://dx.doi.org/10.1002/2211-5463.13396
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author Hirayama, Satoru
Domon, Hisanori
Hiyoshi, Takumi
Isono, Toshihito
Tamura, Hikaru
Sasagawa, Karin
Takizawa, Fumio
Terao, Yutaka
author_facet Hirayama, Satoru
Domon, Hisanori
Hiyoshi, Takumi
Isono, Toshihito
Tamura, Hikaru
Sasagawa, Karin
Takizawa, Fumio
Terao, Yutaka
author_sort Hirayama, Satoru
collection PubMed
description 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.
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spelling pubmed-91574102022-06-04 Triosephosphate isomerase of Streptococcus pneumoniae is released extracellularly by autolysis and binds to host plasminogen to promote its activation Hirayama, Satoru Domon, Hisanori Hiyoshi, Takumi Isono, Toshihito Tamura, Hikaru Sasagawa, Karin Takizawa, Fumio Terao, Yutaka FEBS Open Bio Research Articles 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. John Wiley and Sons Inc. 2022-03-29 /pmc/articles/PMC9157410/ /pubmed/35298875 http://dx.doi.org/10.1002/2211-5463.13396 Text en © 2022 The Authors. FEBS Open Bio published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Articles
Hirayama, Satoru
Domon, Hisanori
Hiyoshi, Takumi
Isono, Toshihito
Tamura, Hikaru
Sasagawa, Karin
Takizawa, Fumio
Terao, Yutaka
Triosephosphate isomerase of Streptococcus pneumoniae is released extracellularly by autolysis and binds to host plasminogen to promote its activation
title Triosephosphate isomerase of Streptococcus pneumoniae is released extracellularly by autolysis and binds to host plasminogen to promote its activation
title_full Triosephosphate isomerase of Streptococcus pneumoniae is released extracellularly by autolysis and binds to host plasminogen to promote its activation
title_fullStr Triosephosphate isomerase of Streptococcus pneumoniae is released extracellularly by autolysis and binds to host plasminogen to promote its activation
title_full_unstemmed Triosephosphate isomerase of Streptococcus pneumoniae is released extracellularly by autolysis and binds to host plasminogen to promote its activation
title_short Triosephosphate isomerase of Streptococcus pneumoniae is released extracellularly by autolysis and binds to host plasminogen to promote its activation
title_sort triosephosphate isomerase of streptococcus pneumoniae is released extracellularly by autolysis and binds to host plasminogen to promote its activation
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9157410/
https://www.ncbi.nlm.nih.gov/pubmed/35298875
http://dx.doi.org/10.1002/2211-5463.13396
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