Genome of Streptococcus oralis Strain Uo5

Reichmann, Peter; Nuhn, Michael; Denapaite, Dalia; Brückner, Reinhold; Henrich, Bernhard; Maurer, Patrick; Rieger, Martin; Klages, Sven; Reinhard, Richard; Hakenbeck, Regine

doi:10.1128/jb.00321-11

Cited by 32 publications

(32 citation statements)

References 14 publications

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“…mitis strains from different parts of the world (22); S. oralis Uo5 (26) was used as a reference for this species. Concatenated sequences of six genes were analyzed by the MEGA6 program, including those from 23 atypical strains of this study.…”

Section: Resultsmentioning

confidence: 99%

Insight into the Diversity of Penicillin-Binding Protein 2x Alleles and Mutations in Viridans Streptococci

Linden

Otten

Bergmann

et al. 2017

Antimicrob Agents Chemother

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The identification of commensal streptococci species is an everlasting problem due to their ability to genetically transform. A new challenge in this respect is the recent description of Streptococcus pseudopneumoniae as a new species, which was distinguished from closely related pathogenic S. pneumoniae and commensal S. mitis by a variety of physiological and molecular biological tests. Forty-one atypical S. pneumoniae isolates have been collected at the German National Reference Center for Streptococci (GNRCS). Multilocus sequence typing (MLST) confirmed 35 isolates as the species S. pseudopneumoniae. A comparison with the pbp2x sequences from 120 commensal streptococci isolated from different continents revealed that pbp2x is distinct among penicillin-susceptible S. pseudopneumoniae isolates. Four penicillin-binding protein x (PBPx) alleles of penicillin-sensitive S. mitis account for most of the diverse sequence blocks in resistant S. pseudopneumoniae, S. pneumoniae, and S. mitis, and S. infantis and S. oralis sequences were found in S. pneumoniae from Japan. PBP2x genes of the family of mosaic genes related to pbp2x in the S. pneumoniae clone Spain23F-1 were observed in S. oralis and S. infantis as well, confirming its global distribution. Thirty-eight sites were altered within the PBP2x transpeptidase domains of penicillin-resistant strains, excluding another 37 sites present in the reference genes of sensitive strains. Specific mutational patterns were detected depending on the parental sequence blocks, in agreement with distinct mutational pathways during the development of beta-lactam resistance. The majority of the mutations clustered around the active site, whereas others are likely to affect stability or interactions with the C-terminal domain or partner proteins.

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Section: Resultsmentioning

confidence: 99%

Insight into the Diversity of Penicillin-Binding Protein 2x Alleles and Mutations in Viridans Streptococci

Linden

Otten

Bergmann

et al. 2017

Antimicrob Agents Chemother

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“…A . The schematic maps of the nanAB operon of S. pneumoniae G54 and the orthologous locus in its close relatives, including S. gordonii V288 (NC_009785.1), S. sanguinis SK36 (NC_009009.1) [46], S. mitis B6 (NC_013853.1) [47] and S. oralis Uo5 (NC_015291.1) [48] are shown. In S. pneumoniae the complete locus includes 18 ORFs, some of them conserved in the other species [23].…”

Section: Resultsmentioning

confidence: 99%

Regulation of neuraminidase expression in Streptococcus pneumoniae

et al. 2012

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BackgroundSialic acid (N-acetylneuraminic acid; NeuNAc) is one of the most important carbohydrates for Streptococcus pneumoniae due of its role as a carbon and energy source, receptor for adhesion and invasion and molecular signal for promotion of biofilm formation, nasopharyngeal carriage and invasion of the lung.ResultsIn this work, NeuNAc and its metabolic derivative N-acetyl mannosamine (ManNAc) were used to analyze regulatory mechanisms of the neuraminidase locus expression. Genomic and metabolic comparison to Streptococcus mitis, Streptococcus oralis, Streptococcus gordonii and Streptococcus sanguinis elucidates the metabolic association of the two amino sugars to different parts of the locus coding for the two main pneumococcal neuraminidases and confirms the substrate specificity of the respective ABC transporters. Quantitative gene expression analysis shows repression of the locus by glucose and induction of all predicted transcriptional units by ManNAc and NeuNAc, each inducing with higher efficiency the operon encoding for the transporter with higher specificity for the respective amino sugar. Cytofluorimetric analysis demonstrated enhanced surface exposure of NanA on pneumococci grown in NeuNAc and ManNAc and an activity assay allowed to quantify approximately twelve times as much neuraminidase activity on induced cells as opposed to glucose grown cells.ConclusionsThe present data increase the understanding of metabolic regulation of the nanAB locus and indicate that experiments aimed at the elucidation of the relevance of neuraminidases in pneumococcal virulence should possibly not be carried out on bacteria grown in glucose containing media.

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“…This is likely because the purified neuraminidase used is more effective than that produced by S. oralis at revealing ␤-1,4-linked galactose. S. oralis neuraminidase activity is predicted to be encoded by nanA and surface associated in an SrtA-dependent manner (28,32). Our genome sequence of ATCC 10557 contains a gene predicted to encode a neuraminidase.…”

Section: Resultsmentioning

confidence: 99%

Streptococcus oralis Neuraminidase Modulates Adherence to Multiple Carbohydrates on Platelets

et al. 2017

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Adherence to host surfaces is often mediated by bacterial binding to surface carbohydrates. Although it is widely appreciated that some bacterial species express glycosidases, previous studies have not considered whether bacteria bind to multiple carbohydrates within host glycans as they are modified by bacterial glycosidases. Streptococcus oralis is a leading cause of subacute infective endocarditis. Binding to platelets is a critical step in disease; however, the mechanisms utilized by S. oralis remain largely undefined. Studies revealed that S. oralis, like Streptococcus gordonii and Streptococcus sanguinis, binds platelets via terminal sialic acid. However, unlike those organisms, S. oralis produces a neuraminidase, NanA, which cleaves terminal sialic acid. Further studies revealed that following NanA-dependent removal of terminal sialic acid, S. oralis bound exposed ␤-1,4-linked galactose. Adherence to both these carbohydrates required Fap1, the S. oralis member of the serine-rich repeat protein (SRRP) family of adhesins. Mutation of a conserved residue required for sialic acid binding by other SRRPs significantly reduced platelet binding, supporting the hypothesis that Fap1 binds this carbohydrate. The mechanism by which Fap1 contributes to ␤-1,4-linked galactose binding remains to be defined; however, binding may occur via additional domains of unknown function within the nonrepeat region, one of which shares some similarity with a carbohydrate binding module. This study is the first demonstration that an SRRP is required to bind ␤-1,4-linked galactose and the first time that one of these adhesins has been shown to be required for binding of multiple glycan receptors.

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Genome of Streptococcus oralis Strain Uo5

Cited by 32 publications

References 14 publications

Insight into the Diversity of Penicillin-Binding Protein 2x Alleles and Mutations in Viridans Streptococci

Insight into the Diversity of Penicillin-Binding Protein 2x Alleles and Mutations in Viridans Streptococci

Regulation of neuraminidase expression in Streptococcus pneumoniae

Streptococcus oralis Neuraminidase Modulates Adherence to Multiple Carbohydrates on Platelets

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