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  • 1
    Electronic Resource
    Electronic Resource
    Human antibody response during sepsis against targets expressed by methicillin resistant Staphylococcus aureus (2000)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 29 (2000), S. 0 
    Details
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The identification of target structures is a prerequisite for the development of new treatment options, like antibody based therapy, against methicillin resistant Staphylococcus aureus (MRSA). In this study we identified immunodominant structures which were expressed in vivo during sepsis caused by MRSA. Using human sera we compared the immune response of humans with MRSA sepsis with the immune response of normal individuals and asymptomatically colonized individuals. We identified and characterized four staphylococcal specific antigenic structures. One target is a staphylococcal protein of 29 kDa that exhibited 29% identity to secreted protein SceA precursor of Staphylococcus carnosus. The putative function of this protein, which was designated IsaA (immunodominant staphylococcal antigen), is unknown. The second target is an immunodominant protein of 17 kDa that showed no homology to any currently known protein. This immunodominant protein was designated IsaB. The third and fourth antigens are both immunodominant proteins of 10 kDa. One of these proteins showed 100% identity to major cold shock protein CspA of S. aureus and the other protein was identified as the phosphocarrier protein Hpr of S. aureus. The identified immunodominant proteins may serve as potential targets for the development of antibody based therapy against MRSA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-695X.2000.tb01517.x
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  • 2
    Electronic Resource
    Electronic Resource
    Synthetic oligodeoxyribonucleotide probes to detect verocytotoxin-producing Escherichia coli in diseased pigs (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 Oligonucleotide probes constructed from the sequences published for Shiga-like toxin I (SLT-I) and Shiga-like toxin II (SLT-II) genes and antibody against the purified toxins were used to study the SLT (SLT-IIp) produced by porcine E. coli O138 and O139 strains. By DNA hybridization assays no homology was observed between SLT-I and SLT-IIp. By contrast the oligonucleotide probe derived from the slt-II A gene detected porcine strains of E. coli producing SLT-IIp and E. coli strains associated with human disease producing SLT-II. Homology of nucleotide sequences between SLT-IIp and SLT-II is reflected by serological cross-reactivity as demonstrated by a dot blot ELISA and neutralization of SLT-IIp with anti-SLT-II. The toxins were distinguishable in their ability to kill HeLa S-3 cells. The oligonucleotide probe and anti-SLT-II can facilitate identification of SLT-IIp producing E. coli to further clarify their role in diseased pigs.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1989.tb03308.x
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  • 3
    Electronic Resource
    Electronic Resource
    Growth of Escherichia coli in the presence of trimethoprim-sulfamethoxazole facilitates detection of Shiga-like toxin producing strains by colony blot assay (1986)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 35 (1986), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Subinhibitory concentrations of trimethoprim-sulfamethoxazole increased the total yield of Shiga-like toxin (SLT), produced by Shigella dysenteria 1 and by enterophathogenic and enterohemorrhagic strains of Escherichia coli. Stimulation of SLT synthesis by trimethoprim-sulfamethoxazole was demonstrated by an increase in cytotoxic activity for HeLa cells and the diameter of the zone formed around bacterial colonies probed with monoclonal antibodies to SLT. Thus, supplementation of culture media with trimetroprimsulfamethoxazol will facilitate SLT purification and detection of SLT-producing bacteria.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1986.tb01516.x
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  • 4
    Electronic Resource
    Electronic Resource
    Analysis of electrophoretically heterogeneous lipopolysaccharides of Escherichia coli by immunoblotting (1984)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 22 (1984), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The purified lipopolysaccharide (LPS) from each of four Escherichia coli serogroups which was separated by sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and visualized by periodic acid-silver staining, exhibited a different distribution of bands. The same serogroup-specific banding patterns were evident on immunoblots developed with homologous but not heterologous O-antisera. Thus, the electrophoretic heterogeneity of LPS was confirmed and the multiple bands seen on SDS-PAGE further shown to contain O-serogroup-specific antigenic determinants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1984.tb00724.x
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  • 5
    Electronic Resource
    Electronic Resource
    The large-sized plasmids of enterohemorrhagic Escherichia coli O157 strains encode hemolysins which are presumably members of the E. coliα-hemolysin family (1994)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 117 (1994), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Most enterohemorrhagic Escherichia coli O157:H7 strains harbor a large-sized (90 kb) plasmid designated pO157 and show an enterohemolytic phenotype. In this study the hemolytic activity of E. coli O157:H7 strain EDL933 was investigated. Curing of strain EDL933 from pO157 resulted in loss of its hemolytic activity. By transformation with Tn801-tagged pO157 (pSK3), the hemolysin-negative E. coli K-12 strains C600 and DH5 became positive for hemolysin production. By transformation of recombinant plasmids carrying a 11.9 kb BamHI fragment and a 5.3 kb SalI fragment of pSK3 hemolytic activity is revealed when tranformed in E. coli C600 or DH5α DNA-hybridization of pO157 and subclones with the α-hemolysin specific DNA probe was only found under conditions of low stringency. No hybridization was found with enterohemolysin I (EHly1) and enterohemolysin II (EHly2) probes. Our results indicate that a hitherto not described hemolysin belonging to the α-hemolysin family is encoded by the 90 kb plasmid of E. coli O157 strains.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1994.tb06763.x
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  • 6
    Electronic Resource
    Electronic Resource
    A gene cluster closely related to type II secretion pathway operons of Gram-negative bacteria is located on the large plasmid of enterohemorrhagic Escherichia coli O157 strains (1997)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 148 (1997), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Analysis of 14.162 kb of DNA derived from plasmid pO157 of enterohemorrhagic Escherichia coli (EHEC) O157:H7 strain EDL933, extending in the 5′ direction of the recently described EHEC-hly operon, revealed 13 open reading frames (ORF) which showed great similarities to genes of members of the type II pathway secretion systems of Gram-negative bacteria. We named the ORFs etpC to etpO for 〈inlineGraphic alt="inline image" href="urn:x-wiley:03781097:FML265:FML_265_mu1" location="equation/FML_265_mu1.gif"/〉 HEC 〈inlineGraphic alt="inline image" href="urn:x-wiley:03781097:FML265:FML_265_mu2" location="equation/FML_265_mu2.gif"/〉 ype II secretion 〈inlineGraphic alt="inline image" href="urn:x-wiley:03781097:FML265:FML_265_mu3" location="equation/FML_265_mu3.gif"/〉 athway. In addition, an IS911-like insertion element was found to separate the etp genes from the EHEC-hlyC gene. Hybridization experiments with a specific etp probe and various categories of enteric E. coli pathotypes revealed that the etp gene cluster occurred in all 30 EHEC strains of serogroup O157 (100%) tested and is distributed sporadically among other EHEC serogroups (60%). In addition, the etp genes were rarely detected in STEC isolated from bovine feces (10%). Moreover, it was found not to occur in enteropathogenic E. coli, enteroaggregative E. coli, enterotoxigenic E. coli and enteroinvasive E. coli. The results obtained with the etp probe were confirmed by a PCR approach to specifically detect an internal fragment of the etpD gene.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1997.tb10299.x
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  • 7
    Electronic Resource
    Electronic Resource
    EspP, a novel extracellular serine protease of enterohaemorrhagic Escherichia coli O157:H7 cleaves human coagulation factor V (1997)
    Oxford UK : Blackwell Science Ltd
    Molecular microbiology 24 (1997), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: In this study, we identified and characterized a novel secreted protein, the extracellular serine protease EspP, which is encoded by the large plasmid of enterohaemorrhagic Escherichia coli (EHEC) O157:H7. The corresponding espP gene consists of a 3900 bp open reading frame that is able to encode a 1300-amino-acid protein. EspP is synthesized as a large precursor which is then processed at the N- and C-termini during secretion. It can be grouped into the autotransporter protein family. The deduced amino acid sequence of EspP showed homology to several secreted or surface-exposed proteins of pathogenic bacteria, in particular EspC of enteropathogenic E. coli and IgA1 proteases from Neisseria spp. and Haemophilus influenzae. Hybridization experiments and immunoblot analysis of clinical EHEC isolates showed that EspP is widespread among EHEC of the serogroup O157 and that it also exists in serogroup O26. A specific immune response against EspP was detected in sera from patients suffering from EHEC infections. Functional analysis showed that EspP is a protease capable of cleaving pepsin A and human coagulation factor V. Degradation of factor V could contribute to the mucosal haemorrhage observed in patients with haemorrhagic colitis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1997.3871751.x
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  • 8
    Electronic Resource
    Electronic Resource
    Genes coding for Shiga-like toxin and heat-stabile enterotoxin in porcine strains of Escherichia coli (1989)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 58 (1989), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Besides diarrheagenic enterotoxigenic Escherichia coli (ETEC) that produce classical heat stable and/or heat labile enterotoxins (STs, LTs) and the class of Shiga-like toxin-producing enterohemorrhagic E. coli (EHEC), a new category of E. coli is defined sharing similarities with ETEC and EHEC. DNA hybridization studies indicate that some E. coli serovars from porcine origin harbor genes encoding cytotonic ST and cytotoxic Shiga-like toxin. The presence of two potent toxins might contribute to the virulence of such strains and should be taken into consideration when bioassays are performed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1989.tb03029.x
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  • 9
    Electronic Resource
    Electronic Resource
    A new method for induction of specific polyclonal antibodies using immunostained proteins on nitrocellulose membrane, and HIV 1 core antigen and Escherichia coli verotoxin as examples (1988)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 47 (1988), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Two polyclonal antibodies against verotoxin 1 and the core protein p24 of HIV 1 were raised in mice by a new immunization procedure. Both proteins were transferred to nitrocellulose, reacted with polyspecific antisera and the antigen-antibody complexes were then visualized by immunostaining. For preparation of antisera the stained protein bands were cut from the nitrocellulose sheets and implanted subcutaneously into the backs of BALB/c mice, without any adjuvant. A single booster was given 4 weeks later by implanting a second strip. All mice produced high titers of antibody directed against the antigen used for immunization. Thus, antibodies of high specificity can be elicited against protein bands in stained immunoblots.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1988.tb02499.x
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  • 10
    Electronic Resource
    Electronic Resource
    Highly conserved B-subunit genes of Shiga-like toxin II variants found in Escherichia coli O157 strains (1994)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 118 (1994), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract To determine the degree of heterogeneity among Shiga-like toxin-II (SLT-II)-related toxins present in enterohemorrhagic Escherichia coli O157 strains, slt-IIB-related genes of 15 strains were amplified and sequenced. Of these 15 isolates, six contained only the slt-II-related genes, seven strains harbored slt-II-related genes together with slt-II, and two strains had slt-II-related genes plus slt-I. In strains carruing slt-II-related genes alone or in combination with slt-I, the PCR fragments were directly subjected to Taq cycle sequence analysis. Direct sequencing was not possible with the seven strains possessing both slt-II and slt-II-related genes, since the PCR products contained both genes. In order to allow sequence analysis of these slt-II-related genes, the PCR products were first subjected to restriction enzyme digestion with FokI, which selectively digested slt-IIB. This resulted in an undigested 270-bp fragment consisting of pure slt-II-related genes. Interestingly, comparison of the nucleotide sequences revealed 100% homology of all analyzed 15 slt-IIB-related toxin genes. In addition, the nucleotide sequence of slt-IIB-related toxin genes were identical to slt-IIcB. Our findings indicate that SLT-IIc is a major variant form of SLT-II present in E. coli O517 strains.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1994.tb06849.x
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