Mutual exclusivity of hyaluronan and hyaluronidase in invasive group a Streptococcus

Henningham, Anna, Yamaguchi, Masaya, Aziz, Ramy K., Kuipers, Kirsten, Buffalo,Cosmo Z., Dahesh, Samira, Choudhury, Biswa, Van Vleet, Jeremy, Yamaguchi, Yuka, Seymour, Lisa M., Ben Zakour, Nouri L., He, Lingjun, Smith, Helen V., Grimwood, Keith, Beatson, Scott A., Ghosh, Partho, Walker, Mark J., Nizet, Victor and Cole, Jason N. (2014) Mutual exclusivity of hyaluronan and hyaluronidase in invasive group a Streptococcus. Journal of Biological Chemistry, 289 46: 32303-32315. doi:10.1074/jbc.M114.602847

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Author Henningham, Anna
Yamaguchi, Masaya
Aziz, Ramy K.
Kuipers, Kirsten
Buffalo,Cosmo Z.
Dahesh, Samira
Choudhury, Biswa
Van Vleet, Jeremy
Yamaguchi, Yuka
Seymour, Lisa M.
Ben Zakour, Nouri L.
He, Lingjun
Smith, Helen V.
Grimwood, Keith
Beatson, Scott A.
Ghosh, Partho
Walker, Mark J.
Nizet, Victor
Cole, Jason N.
Title Mutual exclusivity of hyaluronan and hyaluronidase in invasive group a Streptococcus
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
1083-351X
Publication date 2014-11-14
Year available 2014
Sub-type Article (original research)
DOI 10.1074/jbc.M114.602847
Open Access Status File (Publisher version)
Volume 289
Issue 46
Start page 32303
End page 32315
Total pages 13
Place of publication Bethesda, MD United States
Publisher American Society for Biochemistry and Molecular Biology
Collection year 2015
Language eng
Formatted abstract
A recent analysis of group A Streptococcus (GAS) invasive infections in Australia has shown a predominance of M4 GAS, a serotype recently reported to lack the antiphagocytic hyaluronic acid (HA) capsule. Here, we use molecular genetics and bioinformatics techniques to characterize 17 clinical M4 isolates associated with invasive disease in children during this recent epidemiology. All M4 isolates lacked HA capsule, and whole genome sequence analysis of two isolates revealed the complete absence of the hasABC capsule biosynthesis operon. Conversely, M4 isolates possess a functional HA-degrading hyaluronate lyase (HylA) enzyme that is rendered nonfunctional in other GAS through a point mutation. Transformation with a plasmid expressing hasABC restored partial encapsulation in wild-type (WT) M4 GAS, and full encapsulation in an isogenic M4 mutant lacking HylA. However, partial encapsulation reduced binding to human complement regulatory protein C4BP, did not enhance survival in whole human blood, and did not increase virulence of WT M4 GAS in a mouse model of systemic infection. Bioinformatics analysis found no hasABC homologs in closely related species, suggesting that this operon was a recent acquisition. These data showcase a mutually exclusive interaction of HA capsule and active HylA among strains of this leading human pathogen.
Keyword Bacterial Pathogenesis
Hyaluronan
Hyaluronate
Infectious Disease
Invasive Disease
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2015 Collection
School of Chemistry and Molecular Biosciences
Institute for Molecular Bioscience - Publications
 
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