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Articles

A Conserved UDP-Glucose Dehydrogenase Encoded outside the hasABC Operon Contributes to Capsule Biogenesis in Group A Streptococcus

Jason N. Cole, Ramy K. Aziz, Kirsten Kuipers, Anjuli M. Timmer, Victor Nizet, Nina M. van Sorge
Jason N. Cole
aDepartment of Pediatrics, University of California San Diego, La Jolla, California, USA
bThe School of Chemistry and Molecular Biosciences and the Australian Infectious Diseases Research Centre, The University of Queensland, St. Lucia, Brisbane, Queensland, Australia
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Ramy K. Aziz
cSystems Biology Research Group, University of California San Diego, La Jolla, California, USA
dDepartment of Microbiology and Immunology, Faculty of Pharmacy, Cairo University, Cairo, Egypt
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Kirsten Kuipers
aDepartment of Pediatrics, University of California San Diego, La Jolla, California, USA
gUniversity Medical Center Utrecht, Utrecht, The Netherlands
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Anjuli M. Timmer
aDepartment of Pediatrics, University of California San Diego, La Jolla, California, USA
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Victor Nizet
aDepartment of Pediatrics, University of California San Diego, La Jolla, California, USA
eSkaggs School of Pharmacy and Pharmaceutical Sciences, University of California San Diego, La Jolla, California, USA
fRady Children's Hospital, San Diego, California, USA
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Nina M. van Sorge
aDepartment of Pediatrics, University of California San Diego, La Jolla, California, USA
gUniversity Medical Center Utrecht, Utrecht, The Netherlands
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DOI: 10.1128/JB.01317-12
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ABSTRACT

Group A Streptococcus (GAS) is a human-specific bacterial pathogen responsible for serious morbidity and mortality worldwide. The hyaluronic acid (HA) capsule of GAS is a major virulence factor, contributing to bloodstream survival through resistance to neutrophil and antimicrobial peptide killing and to in vivo pathogenicity. Capsule biosynthesis has been exclusively attributed to the ubiquitous hasABC hyaluronan synthase operon, which is highly conserved across GAS serotypes. Previous reports indicate that hasA, encoding hyaluronan synthase, and hasB, encoding UDP-glucose 6-dehydrogenase, are essential for capsule production in GAS. Here, we report that precise allelic exchange mutagenesis of hasB in GAS strain 5448, a representative of the globally disseminated M1T1 serotype, did not abolish HA capsule synthesis. In silico whole-genome screening identified a putative HasB paralog, designated HasB2, with 45% amino acid identity to HasB at a distant location in the GAS chromosome. In vitro enzymatic assays demonstrated that recombinant HasB2 is a functional UDP-glucose 6-dehydrogenase enzyme. Mutagenesis of hasB2 alone slightly decreased capsule abundance; however, a ΔhasB ΔhasB2 double mutant became completely acapsular. We conclude that HasB is not essential for M1T1 GAS capsule biogenesis due to the presence of a newly identified HasB paralog, HasB2, which most likely resulted from gene duplication. The identification of redundant UDP-glucose 6-dehydrogenases underscores the importance of HA capsule expression for M1T1 GAS pathogenicity and survival in the human host.

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A Conserved UDP-Glucose Dehydrogenase Encoded outside the hasABC Operon Contributes to Capsule Biogenesis in Group A Streptococcus
Jason N. Cole, Ramy K. Aziz, Kirsten Kuipers, Anjuli M. Timmer, Victor Nizet, Nina M. van Sorge
Journal of Bacteriology Oct 2012, 194 (22) 6154-6161; DOI: 10.1128/JB.01317-12

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A Conserved UDP-Glucose Dehydrogenase Encoded outside the hasABC Operon Contributes to Capsule Biogenesis in Group A Streptococcus
Jason N. Cole, Ramy K. Aziz, Kirsten Kuipers, Anjuli M. Timmer, Victor Nizet, Nina M. van Sorge
Journal of Bacteriology Oct 2012, 194 (22) 6154-6161; DOI: 10.1128/JB.01317-12
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