Publications by authors named "E Asaga"

In order to clarify the role that sortase (SrtA) plays in anchoring dextranase (Dex) to the cell wall of Streptococcus mutans, both Dex- and SrtA- mutants were constructed by insertional inactivation of the respective genes. Western blot analysis with a Dex antiserum showed that in the srtA mutant the Dex was not bound to the cell wall but was secreted into the culture supernatant. In contrast, in the wild type, Dex remained cell-wall-associated.

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Aims: To establish a rapid method to differentiate Streptococcus downei and S. sobrinus by multiplex PCR.

Methods And Results: A PCR primer pair specific to S.

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A sortase-deficient mutant of Streptococcus mutans was prepared by insertional inactivation of a sortase gene (srtA). The srtA mutant was defective in cell wall-anchoring of two surface proteins 200 and 75 kDa in size. A previous study has shown that the 200 kDa protein is a surface protein antigen PAc and that the sortase catalyzes cell wall-anchoring of PAc in S.

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Sortase has been shown to be a protease that catalyzes the cell wall anchoring of surface proteins containing an LPXTG motif in gram-positive bacteria. In this study, we determined the complete nucleotide sequence of the sortase gene (srtA) of Streptococcus mutans and found a surface protein that was linked to the cell wall by the sortase. The results show that srtA gene of S.

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An oral parasite Trichomonas tenax ATCC 30207 synthesizes and secretes various proteinases. By gelatin-SDS-PAGE, we found five proteinases bands (30, 37, 46, 51 and 60 kDa) in cell lysate and four bands (37, 45, 52 and 60 kDa) in culture filtrate. The proteinases hydrolyzed acid soluble type I collagen as well as gelatin.

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