Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2007-1-29
pubmed:abstractText
We analysed 72 clinical isolates of enterohaemorrhagic Escherichia coli (EHEC) O111 from patients with diarrhoea or haemolytic uraemic syndrome (HUS) isolated during the period from 1955 to 2005 and identified six motile strains (flagellar antigens 8, 10 and 11); the remaining 66 (92%) were nonmotile (NM) and could not be typed by conventional H serotyping. To improve subtyping methodologies, we determined genotypes of the flagellin-encoding fliC. Three fliC genotypes were found which were identical to those of motile EHEC O111 with H antigens 8, 10 and 11 and designated fliC(H8), fliC(H10) and fliC(H11). The IS629 insertion element was present, identically located, in six epidemiologically unrelated isolates with fliC(H8). The prevalence of the fliC genotypes in the 72 EHEC O111 strains were fliC(H8) (89%), fliC(H10) (7%) and fliC(H11) (4%). Within these fliC genotypes, a high degree of homogeneity for the presence of disease-associated genes was found. The adhesins-encoding genes eae and efa-1 were present in all strains with fliC(H8) and fliC(H11), but absent from strains with fliC(H10). The latter strains have not been reported previously. Strains with fliC(H10) and fliC(H11), but not those with fliC(H8), retained intact cadA and cadC loci and decarboxylated lysine. Three different stx genotypes including stx(1), stx(2) and stx(1)/stx(2) were determined among the 72 EHEC O111. We observed a significant increase over time in the frequency of strains harbouring both stx(1) and stx(2). The presence of stx(2) both alone and in combination with stx(1) was significantly (chi(2)=23.16, P<0.00001, CI(95) [2.29; 9.76]) associated with HUS. Therefore, the emergence of EHEC O111 should be monitored carefully. We conclude that EHEC O111 strains can be differentiated using specific loci required for motility, adherence, Stx production, and lysine decarboxylation. The divergence within EHEC O111 makes it possible to subtype these emerging pathogens in the laboratory thereby providing a basis for further investigations into their ecological niches and survival capabilities.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adhesins, Bacterial, http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Bacterial, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Toxins, http://linkedlifedata.com/resource/pubmed/chemical/CadC protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/Carboxy-Lyases, http://linkedlifedata.com/resource/pubmed/chemical/DNA, Bacterial, http://linkedlifedata.com/resource/pubmed/chemical/DNA Transposable Elements, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Efa1 protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins, http://linkedlifedata.com/resource/pubmed/chemical/FliC protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/H antigen, http://linkedlifedata.com/resource/pubmed/chemical/Lysine, http://linkedlifedata.com/resource/pubmed/chemical/O Antigens, http://linkedlifedata.com/resource/pubmed/chemical/Shiga Toxin, http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators, http://linkedlifedata.com/resource/pubmed/chemical/Virulence Factors, http://linkedlifedata.com/resource/pubmed/chemical/eaeA protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/lysine decarboxylase
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1438-4221
pubmed:author
pubmed:issnType
Print
pubmed:volume
297
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
17-26
pubmed:meshHeading
pubmed-meshheading:17157559-Adhesins, Bacterial, pubmed-meshheading:17157559-Antigens, Bacterial, pubmed-meshheading:17157559-Bacterial Toxins, pubmed-meshheading:17157559-Carboxy-Lyases, pubmed-meshheading:17157559-DNA, Bacterial, pubmed-meshheading:17157559-DNA Transposable Elements, pubmed-meshheading:17157559-DNA-Binding Proteins, pubmed-meshheading:17157559-Decarboxylation, pubmed-meshheading:17157559-Diarrhea, pubmed-meshheading:17157559-Escherichia coli, pubmed-meshheading:17157559-Escherichia coli Infections, pubmed-meshheading:17157559-Escherichia coli Proteins, pubmed-meshheading:17157559-Genes, Bacterial, pubmed-meshheading:17157559-Genotype, pubmed-meshheading:17157559-Hemolytic-Uremic Syndrome, pubmed-meshheading:17157559-Humans, pubmed-meshheading:17157559-Lysine, pubmed-meshheading:17157559-O Antigens, pubmed-meshheading:17157559-Polymerase Chain Reaction, pubmed-meshheading:17157559-Polymorphism, Restriction Fragment Length, pubmed-meshheading:17157559-Sequence Analysis, DNA, pubmed-meshheading:17157559-Serotyping, pubmed-meshheading:17157559-Shiga Toxin, pubmed-meshheading:17157559-Trans-Activators, pubmed-meshheading:17157559-Virulence Factors
pubmed:year
2007
pubmed:articleTitle
Structural and functional differences between disease-associated genes of enterohaemorrhagic Escherichia coli O111.
pubmed:affiliation
Institute for Hygiene, and the National Consulting Laboratory on Haemolytic Uraemic Syndrome, University Hospital Münster, Robert Koch Strasse 41, D-48149 Münster, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't