β-Lactamase expression in Yersinia enterocolitica biovars 1A, 1B and 3

Stock, Ingo; Heisig, Peter; Wiedemann, B.

doi:10.1099/0022-1317-49-5-403

Cited by 25 publications

(31 citation statements)

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“…The resistance profile obtained is in agreement with previous studies, in which resistance to AMP and many cephalosporins is frequently observed Tzelepi et al, 1999;White et al, 2002;Stock & Wiedemann, 2003). In fact, the expression of b-lactamase enzymes A and B has already been associated with Y. enterocolitica, Yersinia intermedia and Yersinia frederiksenii (Stock et al, , 2000Tzelepi et al, 1999). …”

supporting

confidence: 91%

Molecular typing and virulence markers of Yersinia enterocolitica strains from human, animal and food origins isolated between 1968 and 2000 in Brazil

Falcão

Pitondo-Silva³

et al. 2006

Journal of Medical Microbiology

102

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Molecular typing and virulence markers were used to evaluate the genetic profiles and virulence potential of 106 Yersinia enterocolitica strains. Of these strains, 71 were bio-serotype 4/O : 3, isolated from human and animal clinical material, and 35 were of biotype 1A or 2 and of diverse serotypes, isolated from food in Brazil between 1968 and 2000. Drug resistance was also investigated. All the strains were resistant to three or more drugs. The isolates showed a virulence-related phenotype in the aesculin, pyrazinamidase and salicin tests, except for the food isolates, only two of which were positive for these tests. For the other phenotypic virulence determinants (autoagglutination, Ca ++ dependence and Congo red absorption), the strains showed a diverse behaviour. The inv, ail and ystA genes were detected in all human and animal strains, while all the food isolates were positive for inv, and 3 % of them positive for ail and ystA. The presence of virF was variable in the three groups of strains. The strains were better discriminated by PFGE than by enterobacterial repetitive intergenic consensus PCR (ERIC-PCR). A higher genomic similarity was observed among the 4/O : 3 strains, isolated from human and animal isolates, than among the food strains, with the exception of two food strains possessing the virulence genes and grouped close to the 4/O : 3 strains by ERIC-PCR. Unusually, the results revealed the virulence potential of a bio-serotype 1A/O : 10 strain, suggesting that food contaminated with Y. enterocolitica biotype 1A may cause infection. This also suggests that ERIC-PCR may be used as a tool to reveal clues about the virulence potential of Y. enterocolitica strains. Furthermore, the results also support the hypothesis that animals may act as reservoirs of Y. enterocolitica for human infections in Brazil, an epidemiological aspect that has not been investigated in this country, confirming data from other parts of the world. INTRODUCTIONYersinia enterocolitica is the most prevalent Yersinia species connected to disease in humans (Bottone, 1999; RobinsBrowne, 2001). It has also frequently been isolated from animals, food and the environment (Fredriksson-Ahomaa et al., 1999;Thoerner et al., 2003; Falcão et al., 2004).Y. enterocolitica is responsible for gastroenteritis and other syndromes in humans and animals (Bottone, 1999 biochemical and serological tests that enable the differentiation of the strains into diverse bio-serotypes (Aleksic & Bockemühl, 1999). Also, pathogenic strains are related to some phenotypic characteristics, such as pyrazinamidase production, aesculin hydrolysis, salicin fermentation, calcium dependence, autoagglutination and Congo red absorption (Bottone, 1999). Molecular genetic studies have emphasized the importance of a virulence plasmid (pYV) that encodes various virulence genes, among them virF, which is an important transcriptional regulator of other plasmid genes, as well as the role of chromosomal virulence genes that mediate cell invasion (inv and ail) and produce a therm...

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supporting

confidence: 91%

Molecular typing and virulence markers of Yersinia enterocolitica strains from human, animal and food origins isolated between 1968 and 2000 in Brazil

Falcão

Pitondo-Silva³

et al. 2006

Journal of Medical Microbiology

102

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“…This leads to the assumption that BlaA is an enzyme primarily acting on penicillins, whereas BlaB is more specific to cephalosporins (2,11,14,15). These observations are supported by a limited number of experiments that examined the effects of specific inhibitors on the ␤-lactamase activities of cellular lysates derived from various Y. enterocolitica clinical isolates (11,18,19). The goal of this study was to test this hypothesis for the well-defined and -studied strain Y. enterocolitica 8081.…”

mentioning

confidence: 72%

“…This collection of antibiotics overlaps with those that were previously tested in other studies (11,18,19). The ⌬blaA strain had a significantly lower MIC than either the wild-type strain or the ⌬blaB strain, both of which had the same MIC in each case.…”

mentioning

confidence: 96%

“…Previous studies have documented the distribution of these ␤-lactamases in a wide variety of clinical and environmental Y. enterocolitica isolates and have determined the overall resistance or susceptibility of these strains to various ␤-lactam antibiotics (9-11, 13, 16, 18, 19). It appears that strains within a given biovar tend to display similar phenotypes (18).…”

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confidence: 99%

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Contribution of BlaA and BlaB β-Lactamases to Antibiotic Susceptibility of Yersinia enterocolitica Biovar 1B

Bent

Young

2010

Antimicrob Agents Chemother

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Highly pathogenic Yersinia enterocolitica biovar 1B produces two distinct ␤-lactamases, BlaA and BlaB. Mutants of a representative biovar 1B isolate were constructed and evaluated to determine the extent of limitation of susceptibility to broad-spectrum ␤-lactam antibiotics by BlaA and BlaB. The results demonstrated that BlaA, a class A enzyme, plays a significant role in limiting susceptibility to penicillins and cephalosporins. The contribution of BlaB, a class C enzyme, was less profound and was limited primarily to cephalosporin susceptibility.

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“…Resistance of Y. enterocolitica to numerous â-lactams is predominantly attributed to the expression of two different chromosomally encoded â-lactamases called BlaA (a class A enzyme) and BlaB (a class C â-lactamase) [31]. Recently it was shown that although all Y. enterocolitica strains were likely to possess genes for both BlaA-and BlaB-related enzymes, the differences in â-lactam susceptibility were predominantly due to differences in BlaA and BlaB expression which depended on the biovar and, in some cases, on the individual strain [32,33] Enterobacteriaceae that naturally express their â-lactamases at low levels are not uncommon and include several species, e.g., Proteus mirabilis, E. coli, Shigella spp. [34] and Edwardsiella tarda [35].…”

Section: Discussionmentioning

confidence: 99%

Natural antibiotic susceptibility and biochemical profiles of Yersinia enterocolitica-like strains: Y. bercovieri, Y. mollaretii, Y. aldovae and ‘Y. ruckeri'

Stock

Henrichfreise

Wiedemann

2002

Journal of Medical Microbiology

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β-Lactamase expression in Yersinia enterocolitica biovars 1A, 1B and 3

Cited by 25 publications

References 11 publications

Molecular typing and virulence markers of Yersinia enterocolitica strains from human, animal and food origins isolated between 1968 and 2000 in Brazil

Molecular typing and virulence markers of Yersinia enterocolitica strains from human, animal and food origins isolated between 1968 and 2000 in Brazil

Contribution of BlaA and BlaB β-Lactamases to Antibiotic Susceptibility of Yersinia enterocolitica Biovar 1B

Natural antibiotic susceptibility and biochemical profiles of Yersinia enterocolitica-like strains: Y. bercovieri, Y. mollaretii, Y. aldovae and ‘Y. ruckeri'

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