Role of group A Streptococcus HtrA in the maturation of SpeB protease

Cole, Jason N., Aquilina, John A., Hains, Peter G., Henningham, Anna, Sriprakash, Kadaba S., Caparon, Michael G., Nizet, Victor, Kotb, Malak, Cordwell, Stuart J., Djordjevic, Steven P. and Walker, Mark J. (2007) Role of group A Streptococcus HtrA in the maturation of SpeB protease. Proteomics, 7 24: 4488-4498. doi:10.1002/pmic.200700626


Author Cole, Jason N.
Aquilina, John A.
Hains, Peter G.
Henningham, Anna
Sriprakash, Kadaba S.
Caparon, Michael G.
Nizet, Victor
Kotb, Malak
Cordwell, Stuart J.
Djordjevic, Steven P.
Walker, Mark J.
Title Role of group A Streptococcus HtrA in the maturation of SpeB protease
Formatted title
Role of group A Streptococcus HtrA in the maturation of SpeB protease
Journal name Proteomics   Check publisher's open access policy
ISSN 1615-9853
1615-9861
Publication date 2007-12-01
Year available 2007
Sub-type Article (original research)
DOI 10.1002/pmic.200700626
Open Access Status
Volume 7
Issue 24
Start page 4488
End page 4498
Total pages 11
Place of publication Weinheim, Germany
Publisher Wiley - VCH Verlag
Language eng
Formatted abstract
The serine protease high-temperature requirement A (HtrA) (DegP) of the human pathogen Streptococcus pyogenes (group A Streptococcus; GAS) is localized to the ExPortal secretory microdomain and is reportedly essential for the maturation of cysteine protease streptococcal pyrogenic exotoxin B (SpeB). Here, we utilize HSC5 (M5 serotype) and the in-frame isogenic mutant HSC5ΔhtrA to determine whether HtrA contributes to the maturation of other GAS virulence determinants. Mutanolysin cell wall extracts and secreted proteins were arrayed by 2-DE and identified by MALDI-TOF PMF analysis. HSC5ΔhtrA had elevated levels of cell wall-associated M protein, whilst the supernatant had higher concentrations of M protein fragments and a reduced amount of mature SpeB protease, compared to wild-type (WT). Western blot analysis and protease assays revealed a delay in the maturation of SpeB in the HSC5ΔhtrA supernatant. HtrA was unable to directly process SpeB zymogen (proSpeB) to the active form in vitro. We therefore conclude that HtrA plays an indirect role in the maturation of cysteine protease SpeB.
Keyword HtrA
SpeB
Streptococcus pyogenes
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: ERA 2012 Admin Only
School of Chemistry and Molecular Biosciences
 
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