Triosephosphate isomerase of Streptococcus pneumoniae is released extracellularly by autolysis and binds to host plasminogen to promote its activation.
Streptococcus pneumoniae
autolysin
plasmin
plasminogen
triosephosphate isomerase
virulence strategy
Journal
FEBS open bio
ISSN: 2211-5463
Titre abrégé: FEBS Open Bio
Pays: England
ID NLM: 101580716
Informations de publication
Date de publication:
06 2022
06 2022
Historique:
revised:
04
03
2022
received:
17
09
2021
accepted:
15
03
2022
pubmed:
18
3
2022
medline:
3
6
2022
entrez:
17
3
2022
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 35298875
doi: 10.1002/2211-5463.13396
pmc: PMC9157410
doi:
Substances chimiques
Plasminogen
9001-91-6
Fibrinolysin
EC 3.4.21.7
Triose-Phosphate Isomerase
EC 5.3.1.1
Banques de données
RefSeq
['ABJ53817.1', 'ABJ54917.1', 'WP_000022815.1', 'ABJ54738.1', 'Q04MM8.1', 'WP_001040724.1', '5IBX_E', 'WP_001019003.1', 'Q04HT9.1', 'WP_001061169.1', 'ABJ53925.1', 'WP_000114489.1', 'ABJ55261.1', 'ABJ55165.1', 'WP_001109677.1']
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1206-1219Informations de copyright
© 2022 The Authors. FEBS Open Bio published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.
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