The serotype-specific glucose side chain of rhamnoseâglucose polysaccharides is essential for adsorption of bacteriophage M102 to<i>Streptococcus mutans</i>

Shibata, Yukie; Yamashita, Yoshihisa; Ploeg, Jan R. van der

doi:10.1111/j.1574-6968.2009.01546.x

Cited by 28 publications

(29 citation statements)

References 19 publications

(36 reference statements)

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“…S. mutans strain OMZ 381 is one of a few strains which support propagation of bacteriophage M102 (Delisle & Rostkowski, 1993;Shibata et al, 2009). OMZ 381 was therefore chosen for isolation of phage-resistant mutants.…”

Section: Methodsmentioning

confidence: 99%

“…Several mechanisms that render lactic acid bacteria resistant to phage infection have been described: inhibition of phage adsorption, inhibition of DNA injection, restriction modification of phage DNA, and abortive infection (Forde & Fitzgerald, 1999). In the case of S. mutans, nothing is known about the last three mechanisms, but it has been shown that M102 does adsorb also to S. mutans serotype c strains that do not support propagation (Shibata et al, 2009). This suggests that factors different from phage adsorption must determine resistance of S. mutans serotype c strains to infection by M102.…”

Section: Introductionmentioning

confidence: 99%

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Analysis of CRISPR in Streptococcus mutans suggests frequent occurrence of acquired immunity against infection by M102-like bacteriophages

Ploeg

2009

Microbiology

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102

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Clustered regularly interspaced short palindromic repeats (CRISPR) consist of highly conserved direct repeats interspersed with variable spacer sequences. They can protect bacteria against invasion by foreign DNA elements. The genome sequence of Streptococcus mutans strain UA159 contains two CRISPR loci, designated CRISPR1 and CRISPR2. The aims of this study were to analyse the organization of CRISPR in further S. mutans strains and to investigate the importance of CRISPR in acquired immunity to M102-like phages. The sequences of CRISPR1 and CRISPR2 arrays were determined for 29 S. mutans strains from different persons. More than half of the CRISPR1 spacers and about 35 % of the CRISPR2 spacers showed sequence similarity with the genome sequence of M102, a virulent siphophage specific for S. mutans. Although only a few spacers matched the phage sequence completely, most of the mismatches had no effect on the amino acid sequences of the phage-encoded proteins. The results suggest that S. mutans is often attacked by M102-like bacteriophages, and that its acquisition of novel phage-derived CRISPR sequences goes along with the presence of S. mutans phages in the environment. Analysis of CRISPR1 of M102-resistant mutants of S. mutans OMZ 381 showed that some of them had acquired novel spacers, and the sequences of all but one of these matched the phage M102 genome sequence. This suggests that the acquisition of the spacers contributed to the resistance against phage infection. However, since not all resistant mutants had new spacers, and since the removal of the CRISPR1 array in one of the mutants and in wild-type strains did not lead to loss of resistance to infection by M102, the acquisition of resistance must be based on further elements as well.

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Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Analysis of CRISPR in Streptococcus mutans suggests frequent occurrence of acquired immunity against infection by M102-like bacteriophages

Ploeg

2009

Microbiology

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102

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“…The analysis of CRISPR cassettes in 29 S. mutans strains revealed that CRISPR spacers had high sequence similarity with M102, a virulent siphophage specific for S. mutans, suggesting that phage-derived spacers present in these strains likely resulted from M102-like phage attacks (45). Subsequently, it was shown that M102 adheres to phage-sensitive and phage-resistant S. mutans serotype c strains, indicating that factors besides phage adsorption determine resistance of S. mutans serotype c strains to infection by M102 phage (49). Despite these studies that explored the role of CRISPR-Cas systems in S. mutans in conferring phage immunity, recent transcriptome studies suggest other functions that CRISPR-Cas systems might have in S. mutans are poorly understood (50)(51)(52)(53)(54)(55).…”

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confidence: 99%

Role of the Streptococcus mutans CRISPR-Cas Systems in Immunity and Cell Physiology

et al. 2015

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b CRISPR-Cas systems provide adaptive microbial immunity against invading viruses and plasmids. The cariogenic bacterium Streptococcus mutans UA159 has two CRISPR-Cas systems: CRISPR1 (type II-A) and CRISPR2 (type I-C) with several spacers from both CRISPR cassettes matching sequences of phage M102 or genomic sequences of other S. mutans. The deletion of the cas genes of CRISPR1 (⌬C1S), CRISPR2 (⌬C2E), or both CRISPR1؉2 (⌬C1SC2E) or the removal of spacers 2 and 3 (⌬CR1SP13E) in S. mutans UA159 did not affect phage sensitivity when challenged with virulent phage M102. Using plasmid transformation experiments, we demonstrated that the CRISPR1-Cas system inhibits transformation of S. mutans by the plasmids matching the spacers 2 and 3. Functional analysis of the cas deletion mutants revealed that in addition to a role in plasmid targeting, both CRISPR systems also contribute to the regulation of bacterial physiology in S. mutans. Compared to wild-type cells, the ⌬C1S strain displayed diminished growth under cell membrane and oxidative stress, enhanced growth under low pH, and had reduced survival under heat shock and DNA-damaging conditions, whereas the ⌬C2E strain exhibited increased sensitivity to heat shock. Transcriptional analysis revealed that the two-component signal transduction system VicR/K differentially modulates expression of cas genes within CRISPR-Cas systems, suggesting that VicR/K might coordinate the expression of two CRISPR-Cas systems. Collectively, we provide in vivo evidence that the type II-A CRISPR-Cas system of S. mutans may be targeted to manipulate its stress response and to influence the host to control the uptake and dissemination of antibiotic resistance genes.

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“…Each serotype RGP has unique linkages of its glucose side chains (35). It has been shown recently that the glucose side chain of RGP is indispensable for adsorption and infection of S. mutans phage M102 (41).…”

mentioning

confidence: 99%

“…All serotypes of S. mutans produce cell wall rhamnose-glucose polysaccharides (RGPs) consisting of a backbone structure of ␣1,2-and ␣1,3-linked rhamnosyl units with glucose side chains linked to alternate molecules on the cell wall (35,41). Each serotype RGP has unique linkages of its glucose side chains (35).…”

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confidence: 99%

Biology and Genome Sequence of Streptococcus mutans Phage M102AD

Delisle

Guo

Chalmers

et al. 2012

Appl Environ Microbiol

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ABSTRACTM102AD is the new designation for aStreptococcus mutansphage described in 1993 as phage M102. This change was necessitated by the genome analysis of anotherS. mutansphage named M102, which revealed differences from the genome sequence reported here. Additional host range analyses confirmed thatS. mutansphage M102AD infects only a few serotype c strains. Phage M102AD adsorbed very slowly to its host, and it cannot adsorb to serotype e and f strains ofS. mutans. M102AD adsorption was blocked by c-specific antiserum. Phage M102AD also adsorbed equally well to heat-treated and trypsin-treated cells, suggesting carbohydrate receptors. Saliva and polysaccharide production did not inhibit plaque formation. The genome of this siphophage consisted of a linear, double-stranded, 30,664-bp DNA molecule, with a GC content of 39.6%. Analysis of the genome extremities indicated the presence of a 3′-overhangcossite that was 11 nucleotides long. Bioinformatic analyses identified 40 open reading frames, all in the same orientation. No lysogeny-related genes were found, indicating that phage M102AD is strictly virulent. No obvious virulence factor gene candidates were found. Twelve proteins were identified in the virion structure by mass spectrometry. Comparative genomic analysis revealed a close relationship betweenS. mutansphages M102AD and M102 as well as withStreptococcus thermophilusphages. This study also highlights the importance of conducting research with biological materials obtained from recognized microbial collections.

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The serotype-specific glucose side chain of rhamnoseâglucose polysaccharides is essential for adsorption of bacteriophage M102 toStreptococcus mutans

Cited by 28 publications

References 19 publications

Analysis of CRISPR in Streptococcus mutans suggests frequent occurrence of acquired immunity against infection by M102-like bacteriophages

Analysis of CRISPR in Streptococcus mutans suggests frequent occurrence of acquired immunity against infection by M102-like bacteriophages

Role of the Streptococcus mutans CRISPR-Cas Systems in Immunity and Cell Physiology

Biology and Genome Sequence of Streptococcus mutans Phage M102AD

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The serotype-specific glucose side chain of rhamnoseâglucose polysaccharides is essential for adsorption of bacteriophage M102 toStreptococcus mutans

Cited by 28 publications

References 19 publications

Analysis of CRISPR in Streptococcus mutans suggests frequent occurrence of acquired immunity against infection by M102-like bacteriophages

Analysis of CRISPR in Streptococcus mutans suggests frequent occurrence of acquired immunity against infection by M102-like bacteriophages

Role of the Streptococcus mutans CRISPR-Cas Systems in Immunity and Cell Physiology

Biology and Genome Sequence of Streptococcus mutans Phage M102AD

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The serotype-specific glucose side chain of rhamnoseâglucose polysaccharides is essential for adsorption of bacteriophage M102 toStreptococcus mutans