Sequence analysis of the gtfC gene from Streptococcus mutans GS-5

Ueda, Shunsaku; Shiroza, Teruaki; Kuramitsu, Howard K.

doi:10.1016/0378-1119(88)90382-4

Cited by 146 publications

(156 citation statements)

References 16 publications

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“…In addition, an inverted repeat sequence characteristic of rho-independent termination sequences was found 200 bp downstream from the gtfa stop codon (results not shown). In addition, an analysis of codon usage for the gtfD gene revealed generally similar utilisation to that of the previously sequenced gtfB and gtfC genes (Shiroza et al, 1987;Ueda et al, 1988). Bg, BglII; H, HindIII; K, KpnI; P, PstI; S, SalI; X, XbaI.…”

Section: Nucleotide Sequence Of the Gtfd Genesupporting

confidence: 54%

Nucleotide sequence of the Streptococcus mutans gtfD gene encoding the glucosyltransferase-S enzyme

Honda

Kato

Kuramitsu

1990

Journal of General Microbiology

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The nucleotide sequene of the Strepfucuccus mufuns GS-5 g f p gene coding for the glucosyltransferase which synthesizes water-soluble glucan (GTF-S) has been determined. The complete gene contains 4293 base pairs and the unprocessed protein is composed of 1430 amino acids with a molecular mass of 159 814 Da. The amino terminus of the unprocessed protein resembles the signal sequences of other extracellular proteins secreted by S. mufans and that of the GTF-I secreted by Sfreptococcus downei. In addition, the GTF-S protein exhibits high amino acid similarity with the strain GS-5 enzymes responsible for insoluble glucan synthesis (GTF-I, GTF-SI) previously isolated and sequenced in this laboratory. These results indicate that all three gtfgenes evolved from a common ancestral gene.

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Section: Nucleotide Sequence Of the Gtfd Genesupporting

confidence: 54%

Nucleotide sequence of the Streptococcus mutans gtfD gene encoding the glucosyltransferase-S enzyme

Honda

Kato

Kuramitsu

1990

Journal of General Microbiology

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“…As mentioned in the Introduction, these repeated domains have also been found in toxin A (Dove et al, 1990;Wren et al, 1990) and toxin B (Barroso et al, 1990;von Eichel-Streiber et al, 1990) of Clostridia spp. and the glucan-binding proteins and glucosyltransferases of other streptococci (Ferretti et al, 1987;Shiroza et al, 1987;Ueda et al, 1988;Banas et al, 1990;Gilmore et al, 1990). In contrast, the N-termini of LytA and PspA are distinct and thereby confer different biological activities on each individual protein.…”

Section: Discussionmentioning

confidence: 99%

“…Two surface proteins have been described that non-covalently bind to the phosphorylcholine by repeated choline-binding domains (Garcia et al, 1986;. This motif has also been identified within the surface proteins of other bacteria [for two excellent reviews see Wren (1991) and Giffard and Jacques (1994)], including a secreted glycoprotein from Clostridium acetobutylicum (Sanchez-Beato et al, 1995), toxins A (Dove et al, 1990;Wren et al, 1990) and B (Barroso et al, 1990;von EichelStreiber et al, 1990) from Clostridium difficile, a glucanbinding protein from Streptococcus mutans (Banas et al, 1990) and several glucosyltransferases from S. downei and S. mutans (Ferretti et al, 1987;Shiroza et al, 1987;Ueda et al, 1988;Gilmore et al, 1990). It has been proposed and supported by experimental data that these repeated domains present in the glucosyltransferases and the toxins from Clostridia (Barroso et al, 1990;Dove et al, 1990;Wren et al, 1990) are responsible for binding to several classes of sugars (Ferretti et al, 1987;Abo et al, 1991;Vickerman et al, 1996).…”

Section: Introductionmentioning

confidence: 99%

Contribution of novel choline‐binding proteins to adherence, colonization and immunogenicity of Streptococcus pneumoniae

Rosenow

Ryan

Weiser

et al. 1997

Molecular Microbiology

438

465

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SummaryThe surface of Streptococcus pneumoniae is decorated with a family of choline-binding proteins (CBPs) that are non-covalently bound to the phosphorylcholine of the teichoic acid. Two examples (PspA, a protective antigen, and LytA, the major autolysin) have been well characterized. We identified additional CPBs and characterized a new CBP, CbpA, as an adhesin and a determinant of virulence. Using choline immobilized on a solid matrix, a mixture of proteins from a pspA-deficient strain of pneumococcus was eluted in a choline-dependent fashion. Antisera to these proteins passively protected mice challenged in the peritoneum with a lethal dose of pneumococci. The predominant component of this mixture, CbpA, is a 75-kDa surface-exposed protein that reacts with human convalescent antisera. The deduced sequence from the corresponding gene showed a chimeric architecture with a unique N-terminal region and a C-terminal domain consisting of 10 repeated choline-binding domains nearly identical to PspA. A cbpA-deficient mutant showed a >50% reduction in adherence to cytokine-activated human cells and failed to bind to immobilized sialic acid or lacto-N-neotetraose, known pneumococcal ligands on eukaryotic cells. Carriage of this mutant in an animal model of nasopharyngeal colonization was reduced 100-fold. There was no difference between the parent strain and this mutant in an intraperitoneal model of sepsis. These data for CbpA extend the important functions of the CBP family to bacterial adherence and identify a pneumococcal vaccine candidate.

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“…Recently, a number of genes encoding GTF enzymes have been isolated. Of these the gtfI and gtfS genes of S. downei MFe28 and the gtfB, gtfC and gtfD genes of S. mutans strain GS5 (which encode a GTF-I and two GTF-S activities respectively) have been sequenced (Ferretti et al, 1987;Shiroza et al, 1987;Ueda et al, 1988 ;Gilmore et al 1990 ;Honda et al, 1990) and it has been found that all these genes are closely related to each other. In the case of S. mutans GS5 the gtfB and gtfC genes, but not the gtfD gene, lie in close proximity to one another (Perry & Kuramitsu, 1990).…”

Section: Introductionmentioning

confidence: 99%

Molecular characterization of a cluster of at least two glucosyltransferase genes in Streptococcus salivarius ATCC 25975

Giffard¹,

Simpson²,

Milward³

et al. 1991

Journal of General Microbiology

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~~~The oral micro-organism Streptococcus safivarius ATCC 25975 synthesizes extracellular glucosyltransferases (GTFs) which polymerize the glucose moiety of sucrose into glucan polymers. Two separate genes encoding the activities of a GTF-I (a GTF that synthesizes an insoluble product) and a GTF-S (a GTF that synthesizes soluble product) were cloned into bacteriophage IIA7.1. The inserts in the I-clones were characterized by restriction mapping and Southern hybridization and were found to overlap, implying that the two genes lay very close to one another on the S. safiuarius chromosome. Both genes were subcloned into phagemid vector pIBI30 where they were expressed at a high level. The GTF-I-encoding gene was named gtfJ and the GTF-S-encoding gene, gtfK. Nucleotide sequencing showed that gtfJ and most probably gtfK were closely related to thegtf genes of the mutans streptococci. Sequence alignment also indicated that gtfK lay very close to and downstream from gtfJ, and that both were transcribed in the same direction.

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Sequence analysis of the gtfC gene from Streptococcus mutans GS-5

Cited by 146 publications

References 16 publications

Nucleotide sequence of the Streptococcus mutans gtfD gene encoding the glucosyltransferase-S enzyme

Nucleotide sequence of the Streptococcus mutans gtfD gene encoding the glucosyltransferase-S enzyme

Contribution of novel choline‐binding proteins to adherence, colonization and immunogenicity of Streptococcus pneumoniae

Molecular characterization of a cluster of at least two glucosyltransferase genes in Streptococcus salivarius ATCC 25975

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