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  • 1
    Electronic Resource
    Electronic Resource
    Detection and purification of the free A subunit of heat-labile enterotoxin produced by enterotoxigenic Escherichia coli (1991)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 77 (1991), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: After removal of total B subunit and heat-labile enterotoxin (LT) from crude cell extracts of enterotoxigenic Escherichia coli (HB 101-EWD 299) by Bio-gel A 5 m column chromatography, the crude cell extract was shown to contain a free A subunit (A′ subunit) that did not bind to the coligenoid of the B subunits.The A′ subunit was found to be immunologically identical to the A subunit of holo-LT and was purified to show only one band in SDS-polyacrylamide gel electrophoresis (PAGE). The mobility of the A′ subunit was identical to that of the A subunit of holo-LT. The pI value of the A′ subunit was also the same as that of the A subunit of holo-LT.These data suggest that in enterotoxigenic E. coli there is free A subunit which may be involved in formation of holo-LT, analogously to free B subunit (coligenoid), and that the free A subunit is physicochemically and immunologically identical to the A subunit of holo-LT.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1991.tb04361.x
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  • 2
    Electronic Resource
    Electronic Resource
    Hemagglutinating activity of the B subunit(s) of the heat-labile enterotoxin isolated from chicken enterotoxigenic Escherichia coli (1989)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 57 (1989), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The hemagglutinating activity of the B subunit(s) of the heat-labile enterotoxin (LTc-B) produced by chicken enterotoxigenic Escherichia coli was studied by hemagglutination and hemagglutination inhibition. No or weak hemagglutination of intact human erythrocytes was found by the LTc-B at the highest concentration used, whereas strong hemagglutination of both neuraminidase- and pronase-treated human erythrocytes was found. Enhancement in hemagglutination of treated human erythrocytes induced by the LTc-B was over 2 to 120-fold for type A and B erythrocytes and over 8-fold for type O erythrocytes, respectively. With intact and treated sheep erythrocytes, on the other hand, no hemagglutination was found by the LTc-B at the highest concentration used. Hemagglutination of pronasetreated human type B erythrocytes by the LTc-B was inhibited by methyl-α-d-galactopyranoside, galactose, melibiose, hog A + H, asialo-bovine salivary mucin and asialo-thyroglobulin among mono-, di- and polysaccharides and glycoproteins used as inhibitors. These results suggest that the LTc-B is a galactose-specific bacterial lectin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1989.tb03229.x
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  • 3
    Electronic Resource
    Electronic Resource
    Purification and characterization of heat-labile enterotoxin isolated from chicken enterotoxigenic Escherichia coli (1988)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 52 (1988), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The heat-labile enterotoxin (LTc) isolated from chicken enterotoxigenic Escherichia coli was purified to homogeneity and its molecular and antigenic properties were compared with those of purified LTs from porcine and human enterotoxigenic Escherichia coli (LTp, LTh). The A subunit of LTc was identical to that of LTp and the B subunit of LTc was identical to that of LTh but not that of LTp, in mobility on SDS-polyacrylamide gel electrophoresis. Ouchterlony tests demonstrated that LTc is antigenically identical to LTh but not with LTp. The pI point and amino acid composition of LTc were also compared and the results suggest that chicken enterotoxigenic E. coli produced an LT similar to LTh.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1988.tb02575.x
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  • 4
    Electronic Resource
    Electronic Resource
    Evidence of common epitopes in the ganglioside binding site of Vibrio cholerae and Escherichia coli heat-labile enterotoxins (1988)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 49 (1988), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Twenty monoclonal antibodies (mAbs) reacting with cholera toxin (CT) of Vibrio cholerae strain 569B were characterized in cross-section and GM1 ganglioside inhibition assays. MAbs were characterized by reaction with CT and Escherichia coli heat-labile porcine strain (LTp) and human strain (LTh) enterotoxins, and by GM1 ganglioside inhibition of mAb binding. Eight of 10 CT-A specific and 3 of 10 CT-B-specific mAbs cross-reacted with LTh and LTp. GM1 ganglioside inhibited reactions of the CT-B cross-reacting antibodies. Results showed that these epitodes common to the B subunit of CT and LT are located in or near the GM1 ganglioside binding region, and that the GM1 ganglioside-binding region of LT differs from that of CT.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1988.tb02673.x
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  • 5
    Electronic Resource
    Electronic Resource
    Amino acid sequence of heat-labile enterotoxin from chicken enterotoxigenic Escherichia coli is identical to that of human strain H 10407 (1993)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 108 (1993), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The DNA sequence of heat-labile enterotoxin from the chicken enterotoxigenic Escherichia coli 21d strain was determined by direct dideoxy sequencing of polymerase chain reaction (PCR)-amplified DNA and was compared with those of heat-labile enterotoxins from porcine and human enterotoxigenic E. coli strains EWD 299 and H 10407. The structural genes of the A and B subunits of chicken heat-labile enterotoxin were identical to those of human heat-labile enterotoxin from the human H 10407 strain. Moreover, 67 base pairs of the upstream and 60 base pairs of the downstream region of the chicken heat-labile enterotoxin gene were also identical to those of the human heat-labile enterotoxin from strain H 10407. However, the patterns of plasmids from the 21d and H 10407 strains were different. The 21d strain had no band corresponding to the 42-MDa plasmid of the H10407 strain encoding the heat-labile enterotoxin gene but it had a smaller plasmid. These data suggest that although the DNA sequence of chicken heat-labile enterotoxin is identical to that of human heat-labile enterotoxin, the plasmid encoding the chicken heat-labile enterotoxin gene in the chicken might be different from that encoding the human heat-labile enterotoxin gene in the H10407 strain.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1993.tb06092.x
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  • 6
    Electronic Resource
    Electronic Resource
    A heat-labile enterotoxin (LT) purified from chicken enterotoxigenic Excherichia coli is identical to porcine LT (1990)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 67 (1990), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract We have previously reported that the heat-labile enterotoxin (LTc) isolated from a chicken enterotoxigenic Escherichia coli (ETEC) was identical to LTh produced by human ETEC (Tsuji et al. (1988) FEMS Microbiol Lett. 52, 79–84). In this study, we purified an LTc-like toxin (LTc′) from another strain isolated from a chicken that developed diarrhea at a different place and time to the previously reported chicken. ts molecular weight and antigenicity were compared with those of purified LTs from porcine and human ETEC (LTp and LTh). The A subunit of Ltc′ was identical to those of the purified LTs in mobility on SDS-polyacrylamide gel electrophoresis. The Ouchterlony test demonstrated that LTc′ was antigenically identical to LTp. The isoelectric point and amino acid composition of LTc′ were also identical to those of LTp. These data suggest that chicken ETEC can be grouped with both the porcine and human types on the basis of the LTs produced.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1990.tb04042.x
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  • 7
    Electronic Resource
    Electronic Resource
    Comparison of coligenoid formation by B subunits of porcine and human Escherichia coli heat-labile enterotoxins (1990)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 69 (1990), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract A hybrid B subunit (coligenoid) of heat-labile enterotoxin could not be made from human heat-labile enterotoxin B subunit(LTh-B) and porcine LTp-B subunit(LTp-B). LTp-B monomer was able to form coligenoid by reassociation with homologous LTp-B monomer, but not with heterogeneous LTh-B monomer and vice versa. The dissociation of both coligenoids into monomers by SDS treatment occurred in a time-dependent manner, but the dissociation of LTh-B colligenoid was faster than that of LTp-B coligenoid. The association of LTp-B monomer is tighter than that of LTh-B monomer. The pI values of LTp-B coligenoid, LTp-B monomer and denatured LTp-B monomer were similar at 9.6–9.8, while the pI values of LTh-B coligenoid, LTh-B monomer and denatured LTh-B monomer were determined as 5.6–5.8, 9.2–9.6 and 9.2–9.6, respectively. All the ionic amino acids of LTp-B exist on the coligenoid surface. The difference in pI values between LTh-B coligenoid and LTh-B monomer suggests that some basic amino acids are located within the LTh-B coligenoid complex, but are exposed in the LTh-B monomer. These data suggest that the 4 amino acid substitutions between LTh-B and LTp-B result in a three dimensional structure difference and a less stable formation of LTh-B coligenoid compared to LTp-B coligenoid.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1990.tb04248.x
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  • 8
    Electronic Resource
    Electronic Resource
    Hemagglutinating activity of the B subunit(s) of the heat-labile enterotoxin isolated from human enterotoxigenic Escherichia coli (1988)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 49 (1988), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The hemagglutinating activity of the B subunit(s) of the heat-labile toxin (LTh - B) produced by human enterotoxigenic Escherichia coli was studied by hemagglutination and hemagglutination inhibition. Very strong hemagglutination of both neuraminidase- and pronase-treated human erythrocytes was induced by the LTh - B whereas that of intact ones was induced weakly or not at all by the LTh - B at the highest concentration used. Enhancement in hemagglitination of these human erythrocytes by the LTh - B was about 8- to 512-fold for type A and B erythrocytes and 16-fold for type O erthrocytes, respectively. On the other hand, no hemagglutination of intact and treated sheep erythrocytes was found by the LTh - B at the highest concentration used. Hemagglutination of pronase-treated human type B erythrocytes by the LTh - B was inhibited by galactose and melibiose among mono-, di- and polysaccharides used as inhibitors. These findings suggest that the LTh - B is a bacterial lectin specific for galactose-linked residues.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1988.tb02777.x
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  • 9
    Electronic Resource
    Electronic Resource
    Hemagglutinating activity of the heat-labile enterotoxin isolated from porcine enterotoxigenic Escherichia coli (1988)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 49 (1988), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The hemagglutinating activity of the heat-labile enterotoxin (LTp) isolated from porcine enterotoxigenic Escherichia coli was studied by hemagglutination inhibition. The hemagglutinating activity of LTp was enhanced 64–512-fold with pronase- and neuraminidase-treated human erythrocytes although both intact human and sheep erythrocytes were not agglutinated by LTp at the highest concentration used. No enhancement was found in hemagglutination of neuraminidase-treated sheep erythrocytes by LTp. Hemagglutination of pronase-treated human type A erythrocytes induced by LTp was inhibited by melibiose and galactose among mono-, di-, and polysaccharides used as inhibitors. Galactose was a slightly better inhibitor than melibiose. These findings suggest that LTp is a bacterial lectin specific for galactose.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1988.tb02712.x
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  • 10
    Electronic Resource
    Electronic Resource
    The amino acid sequence of the β-subunit: Of porcine enterotoxigenic Escherichia coli enterotoxin — Analysis and comparison with literature data (1984)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 25 (1984), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The amino acid composition and sequence of the β-subunit of heat-labile enterotoxin (LT) purified from a porcine (LTp) strain, WT-1, of enterotoxigenic Escherichia coli was analysed, and the result was compared with that reported by Dallas and Falkow [Nature 288 (1980) 499-501] who deduced the amino acid sequence of LTp from data on the DNA sequence of a porcine strain, EWD299. The purified β-subunit of the LTp of WT-1 was carboxymethylated, succinylated, digested with chymotrypsin and subjected to high performance liquid chromatography (HPLC). The amino acid composition of the peptide peaks from the column were analysed and compared with the data reported by Dallas and Falkow. Only one fraction differed in amino acid composition from that reported, containing lysine instead of methionine. This fraction was found to consist of two peptides with the sequences Lys-Ser-Gly-Glu-Thr-Phe and Arg-Ile-Thr-Tyr. The former peptide is reported to have the sequence Met-Ser-Gly-Glu-Thr-Phe. Thus, the amino acid at position 43 from the N terminus of the β-subunit of LTp is lysine, not methionine as reported. This is the first report which studied the amino acid sequence of LTp analysed by protein toxin itself, not by DNA sequence analysis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1984.tb01465.x
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