Distribution of  -Lactamases A and B in some Groups of Yersinia enterocolitica and their Role in Resistance

Cornelis, G.

doi:10.1099/00221287-91-2-391

Cited by 27 publications

(13 citation statements)

References 8 publications

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“…E. coli NLL-MetRS with mutations L13N, Y360L, and H301L was isolated from pJTN1 (7) by Nhe1 digestion and inserted into pQE80 (Qiagen). Kanamycin resistance was used for selection, because Y. enterocolitica is resistant to ampicillin (48) and nalidixic acid. The resulting plasmid, which carries NLL-MetRS under control of the endogenous E. coli MetG promoter, is termed pAM1 and has been deposited in Addgene.…”

Section: Methodsmentioning

confidence: 99%

Identification of secreted bacterial proteins by noncanonical amino acid tagging

Mahdavi

Szychowski

Ngo

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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Pathogenic microbes have evolved complex secretion systems to deliver virulence factors into host cells. Identification of these factors is critical for understanding the infection process. We report a powerful and versatile approach to the selective labeling and identification of secreted pathogen proteins. Selective labeling of microbial proteins is accomplished via translational incorporation of azidonorleucine (Anl), a methionine surrogate that requires a mutant form of the methionyl-tRNA synthetase for activation. Secreted pathogen proteins containing Anl can be tagged by azide-alkyne cycloaddition and enriched by affinity purification. Application of the method to analysis of the type III secretion system of the human pathogen Yersinia enterocolitica enabled efficient identification of secreted proteins, identification of distinct secretion profiles for intracellular and extracellular bacteria, and determination of the order of substrate injection into host cells. This approach should be widely useful for the identification of virulence factors in microbial pathogens and the development of potential new targets for antimicrobial therapy.proteomics | click chemistry | BONCAT | Yop

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Section: Methodsmentioning

confidence: 99%

Identification of secreted bacterial proteins by noncanonical amino acid tagging

Mahdavi

Szychowski

Ngo

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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“…Several 1-lactamases including 1-lactamases A and B were found to be produced by Y. enterocolitica strains (3)(4)(5) and associated with serotypes (3,14). Production of 3-lactamase is a resistance mechanism which could explain the clinical inefficiency of 1-lactamase-hydrolyzable antibiotics such as ampicillin and cephalothin against Y. enterocolitica infections (15,20,25).…”

mentioning

confidence: 99%

In vitro susceptibilities of 126 clinical isolates of Yersinia enterocolitica to 21 beta-lactam antibiotics

Hornstein¹,

Jupeau²,

Scavizzi³

et al. 1985

Antimicrob Agents Chemother

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The MICs of 21 P-lactam antibiotics were measured against 126 clinically significant and epidemiologically unrelated Yersinia enterocoEltica isolates. The most active antimicrobial agents tested (geometric means of MICs) were ceftriaxone, cefotaxime, ceftizoxime, and cefmenoxime (0.06 to 0.08 ,ug/ml). Mezlocillin (1.36 ig/ml) and piperacillin (1.57 ,ug/ml) were the most active penicillins. Aztreonam (5, 8-11, 17, 21, 30, 31), and the entire species was considered to be resistant to these 1-lactam antibiotics (23). Different patterns of ,B-lactam resistance were reported according to serotype (1, 5, 9, 10, 28).Several 1-lactamases including 1-lactamases A and B were found to be produced by Y. enterocolitica strains (3-5) and associated with serotypes (3, 14). Production of 3-lactamase is a resistance mechanism which could explain the clinical inefficiency of 1-lactamase-hydrolyzable antibiotics such as ampicillin and cephalothin against Y. enterocolitica infections (15,20,25).The recent availability of newer ,B-lactam antibiotics not actually hydrolyzed by ,B-lactamases gave rise to a renewed interest for these antibiotics. Marked in vitro activity of some newer 1-lactam antibiotics against Y. enterocolitica isolates has been reported (16,24,26,29).The purposes of the present study were to (i) determine comparatively countries) and the serotype (22 0 serotypes) of the clinical isolates are given in Table 1. The isolates were stored in semisolid conservation agar (catalog no. 63683; Institut Pasteur Production, Marnes-la-Coquette, France) at room temperature in the dark. All strains were susceptible by the agar dilution method to streptomycin, kanamycin, gentamicin, tetracycline, chloramphenicol, colistin, nalidixic acid, rifampin, trimethoprim (except three strains), and sulfonamides (except four strains).Antibiotics. The 21 antibiotics of known potency used in this study were kindly supplied by the manufacturing companies (or their subsidiary agents). For the purpose of generalization, these antibiotics were classified as follows: (i) Penicillins, including the old penicillins ampicillin and carbenicillin (Beecham, Paris, France) and the newer penicillins temocillin (Beecham), piperacillin (Lederle, Oullins, France), azlocillin and mezlocillin (Bayer, Puteaux, France), and apalcillin (Laboratoire Francais de Thdrapeutique, Bordeaux, France); (ii) aztreonam (Squibb, Neuilly s/Seine, France); a monobactam antibiotic; (iii) imipenem (formerly imipemide or N-formimidoyl thienamycin), a carbapenem antibiotic (Merck, Paris, France); (iv) cephalosporins, including the first-generation cephalosporins cephalothin (Lilly, Saint Cloud, France) and cephaloridine and cephalexin (Glaxo, Paris, France), the second-generation cephalosporins cefoxitin (Merck) and cefamandole (Lilly), and the third-generation cephalosporins cefotaxime (Roussel,

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“…There is considerable disagreement as to the relative importance of beta-lactamases in bacterial resistance to beta-lactam antibiotics (20). Because of the lack of uniform correlation between in vitro minimal inhibitory concentration values and lability of these compounds to enzymatic hydrolysis (1,10,11), this lability, by itself, is not sufficient evidence to predict bacterial susceptibility. Despite this, it is probable that the action of these enzymes does contribute to resistance although not always as the limiting factor.…”

mentioning

confidence: 93%

Substrate Inhibition of Beta-Lactamases, a Method for Predicting Enzymatic Stability of Cephalosporins

Mahoney

Koppel

Turner

1976

Antimicrob Agents Chemother

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Selected cephalosporins, including cefamandole, cephaloridine, cephaloglycin, and cefoxitin, were examined for their ability to inhibit the enzymatic activity of and act as substrates for beta-lactamases produced by Enterobacter cloacae and Staphylococcus aureus. Enzyme inhibition was determined by Michaelis-Menten kinetic measurements and by a spot plate assay using a chromogenic substrate (Glaxo compound 87/312). These two methods provide comparable estimates of kinetic parameters. Inhibition of beta-lactamase, as measured by these two methods, was generally found to correlate with resistance to hydrolysis and is proposed as a preliminary method of assessing susceptibility of cephalosporins to beta-lactamase hydrolysis. Four 7-aOCH3, 7-aH cephalosporin analogue pairs were also examined. The presence of the 7-aOCH3 substituent invariably resulted in reduced susceptibility to enzymatic hydrolysis, regardless of the other C7 substituent. The 7-aOCH3 compounds were also better inhibitors than were their 7-aH analogues, with the exception that 7-aOCH3 compounds having C7 adipic acid substituents were less inhibitory to the S. aureus enzyme than were the corresponding 7-aH analogues. Response of these two enzymes to 7-aOCH3 and 7-aH cephalosporins suggests that beta-lactamase hydrolysis of these compounds involves attack at the alpha side of the betalactam ring.Two naturally occurring 7-a-methoxycephalosporins, 7-a-methoxycephalosporin C and deacetyl-3-O-carbamoyl-7-a-methoxycephalosporin C, were originally isolated from two species of Streptomyces by Nagarajan et al. (9). Both antibiotics exhibited greater activity against gram-negative organisms than did cephalosporin C or deacetyl-3-O-carbamoylcephalosporin C, their 7-hydrogen analogues, and the carbamoyloxymethyl derivative was reported (18) to be more active against gramnegative than gram-positive bacteria. Cefoxitin, a thienylacetyl derivative of deacetyl-3-0-carbamoyl-7-a-methoxycephalosporin C, has been reported to have activity against grampositive and gram-negative organisms (21). This 7-methoxylated cephalosporin generally showed resistance to the action of beta-lactamases from both gram-positive and gram-negative bacteria (14), and it was suggested that this characteristic contributed to the broad antimicrobial spectrum observed. There is considerable disagreement as to the relative importance of beta-lactamases in bacterial resistance to beta-lactam antibiotics (20). Because of the lack of uniform correlation between in vitro minimal inhibitory concentration values and lability of these compounds to enzymatic hydrolysis (1, 10, 11), this lability, by itself, is not sufficient evidence to predict bacterial susceptibility. Despite this, it is probable that the action of these enzymes does contribute to resistance although not always as the limiting factor. Given this assumption, the affinity of a betalactamase for a given cephalosporin should play a role in overall resistance of a beta-lactamaseproducing organism. The affinity (Ki) can be measured directl...

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Distribution of -Lactamases A and B in some Groups of Yersinia enterocolitica and their Role in Resistance

Cited by 27 publications

References 8 publications

Identification of secreted bacterial proteins by noncanonical amino acid tagging

Identification of secreted bacterial proteins by noncanonical amino acid tagging

In vitro susceptibilities of 126 clinical isolates of Yersinia enterocolitica to 21 beta-lactam antibiotics

Substrate Inhibition of Beta-Lactamases, a Method for Predicting Enzymatic Stability of Cephalosporins

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