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

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,...

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Published inVirulence Vol. 12; no. 1; pp. 2633 - 2647
Main 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
Format Journal Article
LanguageEnglish
Published United States Taylor & Francis 01.12.2021
Taylor & Francis Group
Subjects
Animals
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Humans
Mice
Molecular Chaperones
Parvulin-type peptidyl-prolyl isomerase
Proteomics
PrsA
Research Paper
Secretome
Streptococcal Infections
Streptococcus pyogenes
Streptococcus pyogenes - genetics
Virulence
Virulence Factors - genetics
Virulence Factors - metabolism
Streptococcus pyogenes
Parvulin-type peptidyl-prolyl isomerase
virulence
secretome
PrsA
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Summary: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.
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These authors contributed equally to this work
ISSN:2150-5594
2150-5608
DOI:10.1080/21505594.2021.1982501