Search

Your search keyword '"Abe, Akio"' showing total 11 results
Start Over Author "Abe, Akio" Publisher wiley
11 results on '"Abe, Akio"'

2. Tandem tyrosine phosphosites in the Enteropathogenic Escherichia coli chaperone CesT are required for differential type III effector translocation and virulence

Author

Runte, Cameron S., primary, Jain, Umang, additional, Getz, Landon J., additional, Secord, Sabrina, additional, Kuwae, Asaomi, additional, Abe, Akio, additional, LeBlanc, Jason J., additional, Stadnyk, Andrew W., additional, Kaper, James B., additional, Hansen, Anne-Marie, additional, and Thomas, Nikhil A., additional

Published
2018
Full Text
View/download PDF

6. ChemInform Abstract: Guadinomines, Type III Secretion System Inhibitors, Produced by Streptomyces sp. K01-0509. Part 1. Taxonomy, Fermentation, Isolation and Biological Properties.

Author

Iwatsuki, Masato, primary, Uchida, Ryuji, additional, Yoshijima, Hitomi, additional, Ui, Hideaki, additional, Shiomi, Kazuro, additional, Matsumoto, Atsuko, additional, Takahashi, Yoko, additional, Abe, Akio, additional, Tomoda, Hiroshi, additional, and Omura, Satoshi, additional

Published
2008
Full Text
View/download PDF

11. BopB is a type III secreted protein in Bordetella bronchiseptica and is required for cytotoxicity against cultured mammalian cells.

Author

Kuwae A, Ohishi M, Watanabe M, Nagai M, and Abe A

Subjects
Amino Acid Sequence, Animals, Bacterial Proteins genetics, Bordetella bronchiseptica genetics, Carrier Proteins genetics, Cell Line, Culture Media, Digitonin pharmacology, Gene Deletion, Genes, Bacterial, Hemolysis, Humans, Molecular Sequence Data, Molecular Weight, Protein Transport drug effects, Rats, Virulence Factors, Bordetella chemistry, Virulence Factors, Bordetella genetics, Virulence Factors, Bordetella isolation & purification, Bordetella bronchiseptica metabolism, Bordetella bronchiseptica pathogenicity, Virulence Factors, Bordetella metabolism
Abstract

The cytotoxicity of Bordetella bronchiseptica to infected cells is known to be dependent on a B. bronchiseptica type III secretion system. Although the precise mechanism of the type III secretion system is unknown, BopN, BopD and Bsp22 have been identified as type III secreted proteins. In order to identify other proteins secreted via the type III secretion machinery in Bordetella, a type III mutant was generated, and its secretion profile was compared with that of the wild-type strain. The results showed that the wild-type strain, but not the type III mutant, secreted a 40-kDa protein into the culture supernatant. This protein was identified as BopB by the analysis of its N-terminal amino acid sequence. Severe cytotoxicity such as necrosis was induced in L2 cells by infection with the wild-type B. bronchiseptica. In contrast, this effect was not observed by the BopB mutant infection. The haemolytic activity of the BopB mutant was greatly impaired compared with that of the wild-type strain. The results of a digitonin assay strongly suggested that BopB was translocated into HeLa cells infected with the wild-type strain. Taken together, our results demonstrate that Bordetella secretes BopB via a type III secretion system during infection. BopB may play a role in the formation of pores in the host plasma membrane which serve as a conduit for the translocation of effector proteins into host cells.

Published
2003
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results