Cargando…
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...
Autores principales: | , , , , , , , |
---|---|
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 |
_version_ | 1784718630958661632 |
---|---|
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. |
format | Online Article Text |
id | pubmed-9157410 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT hirayamasatoru triosephosphateisomeraseofstreptococcuspneumoniaeisreleasedextracellularlybyautolysisandbindstohostplasminogentopromoteitsactivation AT domonhisanori triosephosphateisomeraseofstreptococcuspneumoniaeisreleasedextracellularlybyautolysisandbindstohostplasminogentopromoteitsactivation AT hiyoshitakumi triosephosphateisomeraseofstreptococcuspneumoniaeisreleasedextracellularlybyautolysisandbindstohostplasminogentopromoteitsactivation AT isonotoshihito triosephosphateisomeraseofstreptococcuspneumoniaeisreleasedextracellularlybyautolysisandbindstohostplasminogentopromoteitsactivation AT tamurahikaru triosephosphateisomeraseofstreptococcuspneumoniaeisreleasedextracellularlybyautolysisandbindstohostplasminogentopromoteitsactivation AT sasagawakarin triosephosphateisomeraseofstreptococcuspneumoniaeisreleasedextracellularlybyautolysisandbindstohostplasminogentopromoteitsactivation AT takizawafumio triosephosphateisomeraseofstreptococcuspneumoniaeisreleasedextracellularlybyautolysisandbindstohostplasminogentopromoteitsactivation AT teraoyutaka triosephosphateisomeraseofstreptococcuspneumoniaeisreleasedextracellularlybyautolysisandbindstohostplasminogentopromoteitsactivation |