Complete Genome Sequence of Streptococcus equi subsp. zooepidemicus Strain ATCC 35246

Ma, Zhe; Geng, Jianing; Zhang, Hui; Yu, Haiying; Li, Yang; Meng, Lu; Chen, Lu; Fan, Hongjie; Hu, Songnian

doi:10.1128/jb.05700-11

Cited by 38 publications

(40 citation statements)

References 9 publications

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“…S. zooepidemicus is an important pathogen of streptococcal diseases in swine [9,10] and it remains a great threat to Chinese swine breeding. In the present study, we used comparative genomic analyses between S. zooepidemicus ATCC35246 and other published S. zooepidemicus strains [11,12] to investigate the mechanisms underlying the differing pathogenicities of Streptococcus equi ssp. In particular, we tried to ascertain how S. zooepidemicus ATCC35246 is able to cause such a serious disease in pig.…”

Section: Introductionmentioning

confidence: 99%

Insight into the specific virulence related genes and toxin-antitoxin virulent pathogenicity islands in swine streptococcosis pathogen Streptococcus equi ssp. zooepidemicus strain ATCC35246

Geng

et al. 2013

BMC Genomics

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BackgroundStreptococcus equi ssp. zooepidemicus (S. zooepidemicus) is an important pathogen causing swine streptococcosis in China. Pathogenicity islands (PAIs) of S. zooepidemicus have been transferred among bacteria through horizontal gene transfer (HGT) and play important roles in the adaptation and increased virulence of S. zooepidemicus. The present study used comparative genomics to examine the different pathogenicities of S. zooepidemicus.ResultsGenome of S. zooepidemicus ATCC35246 (Sz35246) comprises 2,167,264-bp of a single circular chromosome, with a GC content of 41.65%. Comparative genome analysis of Sz35246, S. zooepidemicus MGCS10565 (Sz10565), Streptococcus equi. ssp. equi. 4047 (Se4047) and S. zooepidemicus H70 (Sz70) identified 320 Sz35246-specific genes, clustered into three toxin-antitoxin (TA) systems PAIs and one restriction modification system (RM system) PAI. These four acquired PAIs encode proteins that may contribute to the overall pathogenic capacity and fitness of this bacterium to adapt to different hosts. Analysis of the in vivo and in vitro transcriptomes of this bacterium revealed differentially expressed PAI genes and non-PAI genes, suggesting that Sz35246 possess mechanisms for infecting animals and adapting to a wide range of host environments. Analysis of the genome identified potential Sz35246 virulence genes. Genes of the Fim III operon were presumed to be involved in breaking the host-restriction of Sz35246.ConclusionGenome wide comparisons of Sz35246 with three other strains and transcriptome analysis revealed novel genes related to bacterial virulence and breaking the host-restriction. Four specific PAIs, which were judged to have been transferred into Sz35246 genome through HGT, were identified for the first time. Further analysis of the TA and RM systems in the PAIs will improve our understanding of the pathogenicity of this bacterium and could lead to the development of diagnostics and vaccines.

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Section: Introductionmentioning

confidence: 99%

Insight into the specific virulence related genes and toxin-antitoxin virulent pathogenicity islands in swine streptococcosis pathogen Streptococcus equi ssp. zooepidemicus strain ATCC35246

Geng

et al. 2013

BMC Genomics

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“…zooepidemicus expresses an SFS protein containing four FN-binding repeats (i.e. a duplication of R1R2) (20), which the present results predict would form a stable complex with two FNs.…”

Section: Discussionmentioning

confidence: 87%

Bivalent Ligation of the Collagen-binding Modules of Fibronectin by SFS, a Non-anchored Bacterial Protein of Streptococcus equi

Fogerty

et al. 2015

Journal of Biological Chemistry

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Background: Streptococcus equi expresses SFS protein that contains a disordered region, R1R2, able to inhibit the collagenfibronectin interaction. Results: The repeats of R1R2 bind to plasma fibronectin via modules 8-9 FNI in a two-step reaction involving both fibronectin subunits. Conclusion:8-9 FNI modules of compact fibronectin are arranged in a way that captures R1R2 efficiently. Significance: The same strategy may be used to engage collagen.

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“…The complete genome sequences of several S. zooepidemicus isolates have been released [2,18] and an efficient markerless gene deletion system was developed which can facilitate gene function clarification in this important microbe [22]. Recently, a homologue of hylB was cloned from a S. zooepidemicus strain.…”

Section: Introductionmentioning

confidence: 99%

Genetic and Functional Characterization of the Hyaluronate Lyase HylB and the Beta-N-Acetylglucosaminidase HylZ in Streptococcus zooepidemicus

Sun

Wang

et al. 2014

Curr Microbiol

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Hyaluronic acid (hyaluronan) is a high molecular weight glycosaminoglycan composed of repeating disaccharides of glucuronic acid and N-acetylglucosamine. The molecular weight of hyaluronan is important for its rheological property, biological function, and application. However, genes important for regulation of hyaluronan production or molecular weight remain poorly understood. Here, we address the roles of two predicated hyaluronate lyase-encoding genes, hylB and hylZ in Streptococcus zooepidemicus. Semi-quantitative RT-PCR assays showed that hylZ was constitutively expressed while the expression level of hylB was growth-phase dependent. Using recombinantly expressed 6His-HylB and -HylZ protein, enzyme assays revealed that HylB was a hyaluronate lyase, and its K(m) and V(max) were 0.57 μM and 1.43 mM min(-1), respectively. 6His-HylZ showed no activity against hyaluronan while it hydrolyzed pNp-β-GlcNAc suggesting that HylZ was a beta-N-acetylglucosaminidase. Under the optimal conditions (pH 6.0 and 50 °C), the K(m) and V(max) for 6His-HylZ to degrade pNp-β-GlcNA were 1.16 mM and 26.18 μmol min(-1) mg(-1), respectively. Characterization of ΔhylB and ΔhylZ demonstrated that loss of hylB or/and hylZ had no significant effects on cell growth, lactic acid, and hyaluronan yields. Significantly, as compared to the wild type, ΔhylB produced hyaluronan with an 18 % increase in molecular weight. Our results strongly suggest that hylB encodes a hyaluronate lyase while hylZ encodes a β-N-acetylglucosaminidase. hylB-deficient strain has the potential to produce high molecular weight hyaluronan.

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Complete Genome Sequence of Streptococcus equi subsp. zooepidemicus Strain ATCC 35246

Cited by 38 publications

References 9 publications

Insight into the specific virulence related genes and toxin-antitoxin virulent pathogenicity islands in swine streptococcosis pathogen Streptococcus equi ssp. zooepidemicus strain ATCC35246

Insight into the specific virulence related genes and toxin-antitoxin virulent pathogenicity islands in swine streptococcosis pathogen Streptococcus equi ssp. zooepidemicus strain ATCC35246

Bivalent Ligation of the Collagen-binding Modules of Fibronectin by SFS, a Non-anchored Bacterial Protein of Streptococcus equi

Genetic and Functional Characterization of the Hyaluronate Lyase HylB and the Beta-N-Acetylglucosaminidase HylZ in Streptococcus zooepidemicus

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