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Haru Kato

Publications and source records attributed to Haru Kato.

20 records · Page 2Linked to original sources

Molecular epidemiological study of vertical transmission of vaginal Lactobacillus species from mothers to newborn infants in Japanese, by arbitrarily primed polymerase chain reaction.

We investigated mother-to-newborn infant transmission of Lactobacillus species in Japanese by the typing of isolates from the vagina of pregnant women and stool specimens from their newborn infants. All infants were born by uncomplicated vaginal delivery and were basically fed breast milk. Lactobacillus strains were fingerprinted by arbitrarily primed polymerase chain reaction (AP-PCR), using ERIC1R and ERIC2 primers. Of 86 pregnant women tested, 71 (82.6%) were positive for vaginal lactobacilli. At 5 days after birth, 24 (33.8%) of the 71 infants whose mothers were lactobacilli-positive had fecal lactobacilli, while only 1 (6.7%) of the 15 infants delivered from the vaginal lactobacilli-negative mothers was lactobacilli-positive ( P < 0.01). Lactobacillus crispatus was the most prevalent species of vaginal lactobacilli in mothers and of fecal lactobacilli in infants at 5 days of age, whereas Lactobacillus gasseri was the most common in infants at 1 month of age. Identification to the species level, followed by AP-PCR typing, demonstrated that 23.3% of the 86 infants were likely to be colonized in the intestine by the vaginal lactobacilli of their mothers, and that only 2 of the infants retained the same vaginal lactobacilli until 1 month of age. These results suggest that approximately one-fourth of infants acquire vaginal lactobacilli from their mothers at birth, and that the acquired lactobacilli do not last in the intestine of the infant long-term, but rather, are replaced by ones from milk or unknown sources after birth. AP-PCR with primers ERIC1R and ERIC2 is indicated as a potential tool for the typing of Lactobacillus strains.

Bacterial Typing Techniques↗

Linkage between toxin production and purine biosynthesis in Clostridium difficile.

The production of toxins A and B by Clostridium difficile was greatly enhanced under biotin-limited conditions, in which a 140-kDa protein was expressed strongly. Gene cloning revealed that this protein was a homologue of formylglycinamidine ribonucleotide synthetase (FGAM synthetase, EC 6.3.5.3), which is known as PurL in Escherichia coli and catalyses the fourth step of the de novo purine biosynthesis pathway. This enzyme consisted of a single polypeptide, although FGAM synthetases of gram-positive bacteria usually consist of two subunits. Inhibition of the enzymic activity of C. difficile PurL by O-diazoacetyl-L-serine (azaserine) resulted in enhanced toxin B production even in biotin-sufficient conditions. In contrast, blockade of the preceding step of the PurL catalysing step by sulfamethoxazole inhibited toxin B production almost completely. These results suggest that accumulation of formylglycinamide ribonucleotide (FGAR), a substrate of FGAM synthetase, enhances toxin production by C difficile and depletion of FGAR reduces toxin production.

Amino Acid Sequence↗