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      Vibrio parahaemolyticus, enterotoxigenic Escherichia coli, enterohemorrhagic Escherichia coli and Vibrio cholerae

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          Abstract

          This review highlighted the following: (i) pathogenic mechanism of the thermostable direct hemolysin produced by Vibrio parahaemolyticus, especially on its cardiotoxicity, (ii) heat-labile and heat-stable enterotoxins produced by enterotoxigenic Escherichia coli, especially structure–activity relationship of heat-stable enterotoxin, (iii) RNA N-glycosidase activity of Vero toxins (VT1 and VT2) produced by enterohemorrhagic Escherichia coli O157:H7, (iv) discovery of Vibrio cholerae O139, (v) isolation of new variant of Vibrio cholerae O1 El Tor that carries classical ctxB, and production of high concentration of cholera toxin by these strains, and (vi) conversion of viable but nonculturable (VBNC) Vibrio cholerae to culturable state by co-culture with eukaryotic cells.

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          The mechanism of action of ricin and related toxic lectins on eukaryotic ribosomes. The site and the characteristics of the modification in 28 S ribosomal RNA caused by the toxins.

          K Mitsui, Masako Y Endo, M Motizuki … (1987)
          Ricin is a potent cytotoxic protein derived from the higher plant Ricinus communis that inactivates eukaryotic ribosomes. In this paper we have studied the mechanism of action of ricin A-chain on rat liver ribosomes in vitro. Our findings indicate that the toxin inactivates the ribosomes by modifying both or either of two nucleoside residues, G4323 and A4324, in 28 S rRNA. These nucleotides are located close to the alpha-sarcin cleavage site and become resistant to all ribonucleases tested. The examination of the lability of phosphodiester bonds of these nucleotides to both mild alkaline digestion and aniline treatment at acidic pH suggests that the base of A4324 is removed by the toxin. This unique activity of ricin A-chain was also observed when naked 28 S rRNA is used as a substrate, indicating that the toxin directly acts on the RNA. Similar activity on 28 S rRNA is also exhibited by abrin and modeccin, ricin-related toxins, suggesting a general mechanistic pathway for ribosome inactivation by lectin toxins.
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            RNA N-glycosidase activity of ricin A-chain. Mechanism of action of the toxic lectin ricin on eukaryotic ribosomes.

            Masako Y Endo, K Tsurugi (1987)
            The modification reaction of 28 S rRNA in eukaryotic ribosomes by ricin A-chain was characterized. To examine whether ricin A-chain release any bases from 28 S rRNA, rat liver ribosomes were incubated with a catalytic amount of the toxin, and a fraction containing free bases and nucleosides was prepared from the postribosomal fraction of the reaction mixture by means of ion-exchange column chromatography. Thin-layer chromatographic analysis of this fraction revealed a release of 1 mol of adenine from 1 mol of ribosome. When the ribosomes or naked total RNAs were treated with ricin A-chain in the presence of [32P] phosphate, little incorporation of the radioactivity into 28 S rRNA was observed, indicating that the release is not mediated by phosphorolysis. Thus, considering together with the previous result (Endo, Y., Mitsui, K., Motizuki, M., and Tsurugi, K. (1987) J. Biol. Chem. 262, 5908-5912), the results in the present experiments demonstrated that ricin A-chain inactivates the ribosomes by cleaving the N-glycosidic bond of A4324 of 28 S rRNA in a hydrolytic fashion.
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              Vero response to a cytotoxin of Escherichia coli.

              J Konowalchuk, J Speirs, S. Genadieva-Stavric (1977)
              A cytotoxin was found in culture filtrates of a number of Escherichia coli strains that differed from the known heat-stable and heat-labile enterotoxins of E. coli. It was cytotoxic for Vero but not for Y-1 or CHO cells, and its effect on Vero was distinctly different from that of heat-labile enterotoxin. It was labile to heat and antigenically different from heat-labile enterotoxin, and membrane filtration indicated a molecular weight of 10,000 to 30,000.
              Article 0 comments Cited 82 times – based on 0 reviews     Review now
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                Author and article information

                Journal
                Journal ID (nlm-ta): Proc Jpn Acad Ser B Phys Biol Sci
                Journal ID (publisher-id): PJAB
                Title: Proceedings of the Japan Academy. Series B, Physical and Biological Sciences
                Publisher: The Japan Academy (Tokyo, Japan )
                ISSN (Print): 0386-2208
                ISSN (Electronic): 1349-2896
                Publication date (Print): 11 January 2011
                Volume: 87
                Issue: 1
                Pages: 1-12
                Affiliations
                [*1 ]Collaborative Research Center of Okayama University for Infectious Diseases in India, Kolkata, India.
                Author notes
                [† ]Corespondence should be addressed: Y. Takeda, Collaborative Research Center of Okayama University for Infectious Diseases in India, 57 Dr. S. C. Banerjee Road, ID Hospital Campus, Beliaghata, Kolkata 700010, India (e-mail: takeda.yoshi@ 123456pharm.okayama-u.ac.jp ).

                (Communicated by Kumao TOYOSHIMA, M.J.A.)

                Article
                Publisher ID: pjab-87-001
                DOI: 10.2183/pjab.87.1
                PMC ID: 3035056
                PubMed ID: 21233598
                SO-VID: f198ea16-8d95-484e-8072-d089834864b3
                Copyright © © 2011 The Japan Academy
                License:

                This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                Date received : 4 November 2010
                Date accepted : 7 December 2010
                Categories
                Subject: Review

                ScienceOpen disciplines: Life sciences
                Keywords: thermostable direct hemolysin,heat-labile and heat-stable enterotoxins,rna n-glycosidase activity of vero toxins,vibriocholerae o139,viable but nonculturable (vbnc) vibriocholerae
                Data availability:
                ScienceOpen disciplines: Life sciences
                Keywords: thermostable direct hemolysin, heat-labile and heat-stable enterotoxins, rna n-glycosidase activity of vero toxins, vibriocholerae o139, viable but nonculturable (vbnc) vibriocholerae

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