Triosephosphate isomerase of <i>Streptococcus pneumoniae</i> is released extracellularly by autolysis and binds to host plasminogen to promote its activation-Reference-Cited by-同舟云学术

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

Published:2022-03-29 Issue:6 Volume:12 Page:1206-1219
ISSN:2211-5463
Container-title:FEBS Open Bio
language:en
Short-container-title:FEBS Open Bio

Author:

Hirayama Satoru¹^ORCID,Domon Hisanori¹²,Hiyoshi Takumi¹²³,Isono Toshihito¹,Tamura Hikaru¹³,Sasagawa Karin¹³,Takizawa Fumio¹³,Terao Yutaka¹²^ORCID

Affiliation:

1. Division of Microbiology and Infectious Diseases Niigata University Graduate School of Medical and Dental Sciences Japan

2. Center for Advanced Oral Science Niigata University Graduate School of Medical and Dental Sciences Japan

3. Division of Periodontology Niigata University Graduate School of Medical and Dental Sciences Japan

Funder

Japan Society for the Promotion of Science

Publisher

Wiley

Subject

General Biochemistry, Genetics and Molecular Biology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/2211-5463.13396

Reference51 articles.

1. Pneumonia and Invasive Pneumococcal Diseases: The Role of Pneumococcal Conjugate Vaccine in the Era of Multi-Drug Resistance

2. Surface bound plasmin promotes migration ofStreptococcus pneumoniaethrough reconstituted basement membranes

3. Tissue-type plasminogen activator-mediated activation of plasminogen on the surface of group A, C, and G streptococci

4. alpha-Enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface

5. Purification of native α-enolase from Streptococcus pneumoniae that binds plasminogen and is immunogenic

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