Hisae Baba
Health Sciences University of Hokkaido
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Featured researches published by Hisae Baba.
Current Microbiology | 2003
Arihide Kamaguchi; Koji Nakayama; Satoshi Ichiyama; Reiko Nakamura; Toshihiro Watanabe; Michio Ohta; Hisae Baba; Tohru Ohyama
Vesicles from the outer membrane of Porphyromonas gingivalis have the ability to aggregate a wide range of Streptococcus spp., Fusobacterium nucleatum, Actinomyces naeslundii, and Actinomyces viscosus. We found that in the presence of P. gingivalis vesicles, Staphylococcus aureus coaggregated with Streptococcus spp., and the mycelium-type Candida albicans, but not the yeast type. Autoaggregation of S. aureus in the presence of P. gingivalis vesicles is inhibited by L-arginine, L-lysine, and L-cysteine. Both the methicillin-sensitive (MSSA) and -resistant (MRSA) strains of S. aureus were able to coaggregate with Streptococcus spp., A. naeslundii, and A. viscosus when they were treated with P. gingivalis vesicles. P. gingivalis vesicle-treated mycelium-type C. albicans coaggregated with S. aureus, but the yeast-type did not. These results indicate that strains of S. aureus, including MRSA, could adhere to oral biofilms in dental plaque on the tooth surface or in the gingival crevice when P. gingivalis is present.
Microbiology and Immunology | 2001
Arihide Kamaguchi; Koji Nakayama; Tohru Ohyama; Toshihiro Watanabe; Masaaki Okamoto; Hisae Baba
Porphyromonas gingivalis cells coaggregated with Prevotella intermedia cells. The coaggregation was inhibited with L‐arginine, L‐lysine, Nα‐p‐tosyl‐L‐lysine chloromethyl ketone, trypsin inhibitor, and leupeptin. Heat‐ and proteinase K‐treated P. gingivalis cells showed no coaggregation with P. intermedia cells, whereas heat and proteinase K treatments of P. intermedia cells did not affect the coaggregation. The vesicles from P. gingivalis culture supernatant aggregated with P. intermedia cells, and this aggregation was also inhibited by addition of L‐arginine or L‐lysine and by heat treatment of the vesicles. The rgpA rgpB, rgpA kgp, rgpA rgpB kgp, and rgpA kgp hagA mutants of P. gingivalis did not coaggregate with P. intermedia. On the other hand, the fimA mutant lacking the FimA fimbriae showed coaggregation with P. intermedia as well as the wild type parent. These results strongly imply that a heat‐labile and proteinous factor on the cell surface of P. gingivalis, most likely the gingipain‐adhesin complex, is involved in coaggregation of P. gingivalis and P. intermedia.
Microbiology and Immunology | 1994
Arihide Kamaguchi; Hisae Baba; Masaaki Hoshi; Koshiro Inomata
Coaggregation occurred between Porphyromonas gingivalis and mutans streptococci. The coaggregation was completely inhibited by l‐arginine, Nα‐p‐tosyl‐l‐lysine chloromethyl ketone (TLCK), and a trypsin inhibitor, and weakly inhibited by l‐lysine, N‐ethylmaleimide, lysozyme, and human whole saliva. The results of heat and proteinase K treatment suggested that a heat‐labile proteinaceous substance of P. gingivalis and a heat‐stable substance of mutans streptococci may play a role in the coaggregation. Mutans streptococci also aggregated in the presence of the heat‐labile factor in the supernatant of P. gingivalis. The aggregation was also inhibited by l‐arginine, TLCK, and a trypsin inhibitor.
Microbiology and Immunology | 1995
Arihide Kamaguchi; Hisae Baba; Masaaki Hoshi; Koshiro Inomata
The vesicles of Porphyromonas gingivalis ATCC 33277 strongly aggregated Streptococcus cricetus, S. rattus, and S. mutans, but poorly aggregated S. sobrinus. The adherence of S. mutans OMZ 70 to hydroxyapatite (HA) coated with whole saliva was increased in parallel with the quantity of the vesicles. The significant increase of adherence of S. mutans OMZ 70 by the vesicles was also observed on the HA coated with parotid saliva, submandibular saliva, serum, and type I collagen. These findings suggest that the vesicles may act as a bridge between mutans streptococcus and the tooth surface.
Microbiology and Immunology | 1986
Hirofumi Danbara; Hiroshi Arita; Hisae Baba; Masanosuke Yoshikawa
In spite of the ability of the genetic determinants for enterotoxin production to be conjugally transferred, mobilized or transposed, enterotoxigenic Escherichia coli (ETEC) isolated from diarrheal patients is restricted to certain serotypes. Four conjugative enterotoxigenic plasmids (Ent plasmids) encoding either a heat‐labile enterotoxin or a heat‐stable enterotoxin or both and belonging to one of three incompatibility groups IncFI, IncHl, or IncX, were examined for their transferability to and stability in 157 nonenterotoxigenic Escherichia coli strains belonging to various serotypes and 89 clinical isolates nonenterotoxigenic but belonging to those serotypes in which ETEC from diarrheal patients are usually found. The serotypes of the strains to which Ent plasmids were efficiently transferred and in which they were maintained stably were not always the serotypes in which ETEC had usually been found and vice versa. The frequencies of transfer of four Ent and two R plasmids to each of the 157 recipients were correlated with each other, indicating that the frequency of transfer of the plasmid is not determined by a resident plasmid, if there is one, but by a recipient factor which commonly affects transferability to all donors. These results have led to the conclusion that the reason why only certain serotypes are found among ETEC isolated from diarrheal patients is not the ability of these strains specifically and preferentially to acquire and maintain the Ent plasmids.
Microbiology | 2003
Arihide Kamaguchi; Tohru Ohyama; Eiko Sakai; Reiko Nakamura; Toshihiro Watanabe; Hisae Baba; Koji Nakayama
Japanese Journal of Oral Biology | 1995
Arihide Kamaguchi; Hisae Baba
Japanese Journal of Oral Biology | 1983
Hisae Baba; Arihide Kamaguchi; Kaede Tanaka; Kazuo Takano
Japanese Journal of Medical Mycology | 1984
Taisuke Akisada; Kaoru Harada; Hisae Baba; Arihide Kamaguchi; Kaoru Eto
東日本歯学雑誌 | 2002
有秀 鎌口; 麗子 中村; 俊弘 渡部; 徹 大山; 久衛 馬場; アリヒデ カマグチ; レイコ ナカムラ; トシヒロ ワタナベ; トオル オオヤマ; ヒサエ ババ; Arihide Kamaguchi; Reiko Nakamura; Toshihiro Watanabe; Tohru Ohyama; Hisae Baba