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Systematic study of genes influencing cellular chain length in Streptococcus sanguinis

Evans, Karra, Stone, Victoria, Chen, Lei, Ge, Xiuchun, Xu, Ping·2014·Microbiology
DOI 10.1099/mic.0.071688-0PMC PMC3919539
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Abstract

Streptococcus sanguinis is a Gram-positive bacterium that is indigenous to the oral cavity. S. sanguinis, a primary colonizer of the oral cavity, serves as a tether for the attachment of other oral pathogens. The colonization of microbes on the tooth surface forms dental plaque, which can lead to the onset of periodontal disease. We examined a comprehensive mutant library to identify genes related to cellular chain length and morphology using phase-contrast microscopy. A number of hypothetical genes related to the cellular chain length were identified in this study. Genes related to the cellular chain length were analysed along with clusters of orthologous groups (COG) for gene functions. It was discovered that the highest proportion of COG functions related to cellular chain length was ‘cell division and chromosome separation’. However, different COG functions were also found to be related with altered cellular chain length. This suggested that different genes related with multiple mechanisms contribute to the cellular chain length in S. sanguinis SK36.

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Figures

Fig. 1. Chain morphologies of mutants. (a) SK36, the wild-type strain. (b) A longer chain mutant with deletion of SSA_0933 gene for acetyltransferase. (c) A shorter chain mutant with deletion of SSA_0422 gene for phosphoglycerate mutase family protein. (d) A chain clustered mutant with deletion of SSA_0285 gene for formate acetyltransferase 3.
Fig. 1. Chain morphologies of mutants. (a) SK36, the wild-type strain. (b) A longer chain mutant with deletion of SSA_0933 gene for acetyltransferase. (c) A shorter chain mutant with deletion of SSA_0422 gene for phosphoglycerate mutase family protein. (d) A chain clustered mutant with deletion of SSA_0285 gene for formate acetyltransferase 3.CC BY · PubMed Central
Fig. 2. Cellular chain length and auto-aggregation of selected mutants and their complementation. Upper panel, the cellular chain lengths of mutants and their complemented strains were examined and compared with the wild-type (WT) as described in Methods. Lower panel, their auto-aggregations were determined by OD600 and the aggregation percentage was calculated as described in Methods. * P<0.05. Error bars indicate ±sd.
Fig. 2. Cellular chain length and auto-aggregation of selected mutants and their complementation. Upper panel, the cellular chain lengths of mutants and their complemented strains were examined and compared with the wild-type (WT) as described in Methods. Lower panel, their auto-aggregations were determined by OD600 and the aggregation percentage was calculated as described in Methods. * P<0.05. Error bars indicate ±sd.CC BY · PubMed Central
Fig. 3. Cellular chain length related gene distribution by COG functions. The ratio between the number of longer chain or shorter chain mutants and the total number of annotated genes in the genome (gene percentage) was calculated for every COG function. COG function abbreviations: Q, secondary metabolites biosynthesis, transport and catabolism; P, inorganic ion transport and metabolism; D, cell division and chromosome partitioning; T, signal transduction mechanisms; E, amino acid transport and metabolism; H, coenzyme metabolism; M, cell envelope biogenesis, outer membrane; G, carbohydrate transport and metabolism; L, DNA replication, recombination and repair; K, transcription; O, post-translational modification, protein turnover, chaperones; C, energy production and conversion; R, general function prediction only; S, function unknown; N, cell motility and secretion; F, nucleotide transport and metabolism; I, lipid metabolism; J, translation, ribosomal structure and biogenesis.
Fig. 3. Cellular chain length related gene distribution by COG functions. The ratio between the number of longer chain or shorter chain mutants and the total number of annotated genes in the genome (gene percentage) was calculated for every COG function. COG function abbreviations: Q, secondary metabolites biosynthesis, transport and catabolism; P, inorganic ion transport and metabolism; D, cell division and chromosome partitioning; T, signal transduction mechanisms; E, amino acid transport and metabolism; H, coenzyme metabolism; M, cell envelope biogenesis, outer membrane; G, carbohydrate transport and metabolism; L, DNA replication, recombination and repair; K, transcription; O, post-translational modification, protein turnover, chaperones; C, energy production and conversion; R, general function prediction only; S, function unknown; N, cell motility and secretion; F, nucleotide transport and metabolism; I, lipid metabolism; J, translation, ribosomal structure and biogenesis.CC BY · PubMed Central
Fig. 4. Cell morphological comparisons by SEM. (a) The wild-type strain SK36. (b) Ssx_0655, a cell division protein FtsA mutant, shows wider and longer cells. (c) Ssx_2223, a capsular polysaccharide biosynthesis protein Wzd (chain length regulator) mutant, shows clear capsule surrounding the cells. Septum (S), Z-ring (Z) and polysaccharide (P) are indicated. Bars, 1 μm.
Fig. 4. Cell morphological comparisons by SEM. (a) The wild-type strain SK36. (b) Ssx_0655, a cell division protein FtsA mutant, shows wider and longer cells. (c) Ssx_2223, a capsular polysaccharide biosynthesis protein Wzd (chain length regulator) mutant, shows clear capsule surrounding the cells. Septum (S), Z-ring (Z) and polysaccharide (P) are indicated. Bars, 1 μm.CC BY · PubMed Central

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Metadata

Authors
Evans, K., Stone, V., Chen, L., Ge, X., & Xu, P.
Venue
Microbiology
Publisher
Microbiology Society
Published
2014-02-01
Volume
160
Issue
2
Pages
307-315
ISSN
  • 1350-0872
  • 1465-2080
DOI
10.1099/mic.0.071688-0
PMC
PMC3919539
Cited by
14
References
1
Language
en
Funders
  • Incentive Program (144602-3)
  • Virginia Commonwealth University Presidential Research
  • National Institutes of Health (R01DE018138, R01DE023078)

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