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Unique virulence role of post-translocational chaperone PrsA in shaping Streptococcus pyogenes secretome.

Authors :
Wu, Zhao-Yi
Campeau, Anaamika
Liu, Chao-Hsien
Gonzalez, David J.
Yamaguchi, Masaya
Kawabata, Shigetada
Lu, Chieh-Hsien
Lai, Chian-Yu
Chiu, Hao-Chieh
Chang, Yung-Chi
Source :
Virulence. Dec 2021, Vol. 12 Issue 1, p2633-2647. 15p.
Publication Year :
2021

Abstract

Streptococcus pyogenes (group A Streptococcus, GAS) is a strict human pathogen causing a broad spectrum of diseases and a variety of autoimmune sequelae. The pathogenesis of GAS infection mostly relies on the production of an extensive network of cell wall-associated and secreted virulence proteins, such as adhesins, toxins, and exoenzymes. PrsA, the only extracellular parvulin-type peptidyl-prolyl isomerase expressed ubiquitously in Gram-positive bacteria, has been suggested to assist the folding and maturation of newly exported proteins to acquire their native conformation and activity. Two PrsA proteins, PrsA1 and PrsA2, have been identified in GAS, but the respective contribution of each PrsA in GAS pathogenesis remains largely unknown. By combining comparative proteomic and phenotypic analysis approaches, we demonstrate that both PrsA isoforms are required to maintain GAS proteome homeostasis and virulence-associated traits in a unique and overlapping manner. The inactivation of both PrsA in GAS caused remarkable impairment in biofilm formation, host adherence, infection-induced cytotoxicity, and in vivo virulence in a murine soft tissue infection model. The concordance of proteomic and phenotypic data clearly features the essential role of PrsA in GAS full virulence. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
21505594
Volume :
12
Issue :
1
Database :
Academic Search Index
Journal :
Virulence
Publication Type :
Academic Journal
Accession number :
154362635
Full Text :
https://doi.org/10.1080/21505594.2021.1982501