Cloning and sequencing of the blaZ gene encoding beta-lactamase III, a lipoprotein of Bacillus cereus 569/H

Hussain, Musaddeq; Pastor, F. I. Javier; Lampen, J. O.

doi:10.1128/jb.169.2.579-586.1987

Cited by 52 publications

(28 citation statements)

References 32 publications

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“…It is possible that either the enzyme is not processed or it is covalently modified, causing it to run aberrantly during SDS-PAGE. An example of the latter is the B. cereus BCIII 3-lactamase, which is a covalently modified lipoprotein with about half of the total activity membrane bound (20). The close association of CfxA with the membrane fraction may favor the possibility that CfxA is a covalently modified lipoprotein.…”

Section: Resultsmentioning

confidence: 99%

Genetic and biochemical analysis of a novel Ambler class A beta-lactamase responsible for cefoxitin resistance in Bacteroides species

Parker

Smith

1993

Antimicrob Agents Chemother

132

115

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A clinical isolate of Bacteroides vulgatus was resistant to tetracycline, clindamycin, ampicillin, cephaloridine, cefoxitin, and other 13-lactam antibiotics except imipenem. 13-Lactam resistance was mediated by a membraneassociated, clavulanate-sensitive cephalosporinase capable of degrading cephalosporins and penicillins. Cefoxitin also was degraded but at a slow rate. The cefoxitin resistance (Fxr) ,-Lactamase production is the most important mechanism of resistance to P-lactam antibiotics in gram-negative bacteria, and the Bacteroides fragilis group possesses a wide array of these enzymes. In general, the organisms are moderately or highly resistant to many cephalosporins and penicillins, but a-methoxyl cephamycins such as cefoxitin and the carbapenems have been highly active against Bacteroides species. In the United States, for example, imipenem resistance rates are presently low, at about 0.2%, and cefoxitin resistance (Fxr) rates have ranged up to 16% during the past decade (37, 38). High rates of Fxr are cause for concern since Fxr strains usually encountered are crossresistant to most other P-lactams (38). In the case of strains that possess metallo-p-lactamases, the cross-resistance includes the carbapenems (8, 39).Resistance of Bacteroides species to cefoxitin may involve a number of mechanisms including altered drug permeability, alterations of penicillin binding proteins, 1-lactamase production, or a combination of mechanisms (8,10,41). Excluding the relatively rare imipenem-hydrolyzing metalloenzymes, several P-lactamases capable of cefoxitin degradation have been described. These are generally cephalosporinases with a slow rate of cefoxitin hydrolysis, and they are sensitive to inhibition by clavulanate (9, 13). Recently, Aldridge et al. (1) have found that >93% of Fxr strains were still sensitive to 3-lactam-clavulanate combinations. Thus, based on these criteria, it is possible that the slow cefoxitinhydrolyzing cephalosporinases are one of the most widely disseminated mechanisms of Fxr in the Bacteroides species. In this regard, it has been suggested that these P-lactamases are not novel enzymes but rather that the strains are Fxr * Corresponding author.because of the production of much greater than normal levels of the conventional Bacteroides enzyme (36).The occurrence of high regional Fxr rates indicates the potential for clonal dissemination and/or horizontal transfer of the resistance phenotype. The transfer of Fxr by a conjugation-like mechanism has been demonstrated; however, plasmids were not involved in the transfer (10). The Fxr phenotype was mediated by the acquisition of a new P-lactamase. The present study was initiated to define the genetic basis for transmissible Fxr in Bacteroides species.The results revealed a novel genetic locus designated cfx4, which encodes an Ambler molecular class A 13-lactamase that appears to have diverged significantly from all other class A enzymes. MATERIALS AND METHODSBacterial strains and growth. Bacteroides cells were cultured anaerobically in su...

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Section: Resultsmentioning

confidence: 99%

Genetic and biochemical analysis of a novel Ambler class A beta-lactamase responsible for cefoxitin resistance in Bacteroides species

Parker

Smith

1993

Antimicrob Agents Chemother

132

115

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“…(i) Class A P-lactamases. Class A P-lactamase sequences were those from Bacillus licheniformis 749/C, Bacillus cereus 569/H (type I), TEM-1, Staphylococcus aureus PC-1 (1), PSE-3 encoded by plasmid Rmsi49, and Rhodopseudomonas capsulata (8); SHV-1 (also called PIT-2) (5); Bacillus cereus 5/B (50); Bacillus cereus 569/H (type III) (24); LEN-1 (Klebsiella pneumoniae) (3); Klebsiella oxytoca E23004 (4); PSE-4 (7); Actinomadura sp. strain R39 (22); Streptomyces albus G (11); Streptomyces lavendulae, Streptomyces badius, and Streptomyces fradiae (15); and Streptomyces aureofaciens (2).…”

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confidence: 99%

Comparison of the sequences of class A beta-lactamases and of the secondary structure elements of penicillin-recognizing proteins

Joris

Ledent

Dideberg

et al. 1991

Antimicrob Agents Chemother

155

136

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The sequences of class A ,I-lactamases were compared. Four main groups of enzymes were distinguished: those from the gram-negative organisms and bacilli and two distinct groups of Streptomyces spp. The Staphylococcus aureus PC1 enzyme, although somewhat closer to the enzyme from the Bacillus group, did not belong to any of the groups of I-lactamases. The similarities between the secondary structure elements of these enzymes and those of the class C P-lactamases and of the Streptomyces sp. strain R61 DD-peptidase were also analyzed and tentatively extended to the class D ,I-lactamases. A unified nomenclature of secondary structure elements is proposed for all the penicillin-recognizing enzymes.In the last few years, many different 13-lactamase (ii) Class C ,B-lactamases. Class C r-lactamase sequences were those from Escherichia coli K-12 (26); Citrobacter freundii 0S60 (34); Enterobacter cloacae P99, Q908R, and MHN1 (16); Serratia marcescens SR50 (38); and Pseudomonas aeruginosa (35).(iii) Class D ,3-lactamases. The aligned sequences of class D ,3-lactamases were those from OXA-1 (41), OXA-2 (9), and PSE-2 (23) (2), but the C-and N-terminal portions were deleted so that all compared sequences extended from residues 30 to 285 (ABL consensus numbering scheme). The final score represents the number of matches divided by the length of the shorter sequence, excluding the gaps. In the

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“…It is also known, however, that in B. licheniformis and in Bacillus cereus 569/H the Class A p-lactamase is present both as a membrane-bound hydrophobic form as well as a soluble exoenzyme (Nielsen & Lampen, 1982Hussain et al, 1987).…”

Section: P81173mentioning

confidence: 99%

Membrane-bound and extracellular β-lactamase production with developmental regulation in Streptomyces griseus NRRL B-2682

Deák¹,

SzabóA²,

Kálmáczhelyi³

et al. 1998

Microbiology

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A new type ofβ-lactamase has been isolated and characterized in Streptomyces griseus NRRL B-2682. The enzyme has membrane-bound and extracellular forms. Biochemical characterization of some of the properties of the enzyme showed that it belongs to the class A group of penicillinases. Comparison of the membrane-bound and extracellular forms of theβ-lactamases suggests that they seem to be differently processed forms of the same enzyme. The N-terminal amino acid sequence of the extracellular form of the β-lactamase showed a high degree of similarity to a D-aminopeptidase of another Streptomyces griseus strain. Secretion of the β-lactamase was affected by the differentiation state of the strain since in spontaneous non-sporulating mutants only the membrane-bound form was present. In accordance with this when sporulation of the wild-type strain was inhibited it failed to secrete extracellular β-lactamase. Addition of globomycin to the non-sporulating cells liberated the enzyme from the membrane, indicating that the protein is processed normally by signal peptidase II and a glyceride-thioether group, together with a fatty acid amide-linkage, is responsible for the attachment of the enzyme to the cellular membrane. Under sporulation-repressed conditions addition of peptidoglycan fragments and analogues or inhibition of cell wall biosynthesis by penicillin-G induced β-lactamase secretion and also restored sporulation both in solid and submerged cultures. These results confirm that β-lactamase secretion is tightly coupled to the sporulation process in S. griseus.

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Cloning and sequencing of the blaZ gene encoding beta-lactamase III, a lipoprotein of Bacillus cereus 569/H

Cited by 52 publications

References 32 publications

Genetic and biochemical analysis of a novel Ambler class A beta-lactamase responsible for cefoxitin resistance in Bacteroides species

Genetic and biochemical analysis of a novel Ambler class A beta-lactamase responsible for cefoxitin resistance in Bacteroides species

Comparison of the sequences of class A beta-lactamases and of the secondary structure elements of penicillin-recognizing proteins

Membrane-bound and extracellular β-lactamase production with developmental regulation in Streptomyces griseus NRRL B-2682

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