Susceptibilities of nontuberculosis mycobacterial species to amoxicillin-clavulanic acid alone and in combination with antimycobacterial agents

Utrup, Linda J.; Moore, Thomas; Actor, Paul; Poupard, James A.

doi:10.1128/aac.39.7.1454

Cited by 18 publications

(14 citation statements)

References 26 publications

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“…␤-Lactamases have returned to the spotlight in recent years due to the use of treatments combining penicillins with clavulanic acid for infections caused by mycobacteria, which are acid-fast, rodshaped bacteria (109)(110)(111)(112). Many enzymatic studies have been carried out on Mycobacterium tuberculosis (BlaC), Mycobacterium abscessus (MAB-1), and Mycobacterium fortuitum (BlaF/MFO-1) (Table 1) (4,22,23,113).…”

Section: Enzymes Produced By Gram-positive Bacteriamentioning

confidence: 99%

A Structure-Based Classification of Class A β-Lactamases, a Broadly Diverse Family of Enzymes

Slama²,

et al. 2016

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SUMMARYFor medical biologists, sequencing has become a commonplace technique to support diagnosis. Rapid changes in this field have led to the generation of large amounts of data, which are not always correctly listed in databases. This is particularly true for data concerning class A β-lactamases, a group of key antibiotic resistance enzymes produced by bacteria. Many genomes have been reported to contain putative β-lactamase genes, which can be compared with representative types. We analyzed several hundred amino acid sequences of class A β-lactamase enzymes for phylogenic relationships, the presence of specific residues, and cluster patterns. A clear distinction was first made between dd-peptidases and class A enzymes based on a small number of residues (S70, K73, P107, 130SDN132, G144, E166, 234K/R, 235T/S, and 236G [Ambler numbering]). Other residues clearly separated two main branches, which we named subclasses A1 and A2. Various clusters were identified on the major branch (subclass A1) on the basis of signature residues associated with catalytic properties (e.g., limited-spectrum β-lactamases, extended-spectrum β-lactamases, and carbapenemases). For subclass A2 enzymes (e.g., CfxA, CIA-1, CME-1, PER-1, and VEB-1), 43 conserved residues were characterized, and several significant insertions were detected. This diversity in the amino acid sequences of β-lactamases must be taken into account to ensure that new enzymes are accurately identified. However, with the exception of PER types, this diversity is poorly represented in existing X-ray crystallographic data.

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Section: Enzymes Produced By Gram-positive Bacteriamentioning

confidence: 99%

A Structure-Based Classification of Class A β-Lactamases, a Broadly Diverse Family of Enzymes

Slama²,

et al. 2016

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“…However, the effectiveness of b-lactam/b-lactamase inhibitor combinations has been shown in vitro for M. tuberculosis (Chambers et al, 1995;Cynamon & Palmer, 1983;Segura et al, 1998;Sorg & Cynamon, 1987), M. avium (Casal et al, 1987), M. fortuitum (Utrup et al, 1995;Wong et al, 1988) and M. smegmatis (Yabu et al, 1985). Clinical evidence suggests that b-lactam antibiotics in combination with b-lactamase inhibitors may be useful in the treatment of M. tuberculosis infection (Chambers et al, 1998;Nadler et al, 1991).…”

Section: Introductionmentioning

confidence: 99%

Genetic analysis of the β-lactamases of Mycobacterium tuberculosis and Mycobacterium smegmatis and susceptibility to β-lactam antibiotics

2005

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Mycobacteria produce β-lactamases and are intrinsically resistant to β-lactam antibiotics. In addition to the β-lactamases, cell envelope permeability and variations in certain peptidoglycan biosynthetic enzymes are believed to contribute to β-lactam resistance in these organisms. To allow the study of these additional mechanisms, mutants of the major β-lactamases, BlaC and BlaS, were generated in the pathogenic Mycobacterium tuberculosis strain H37Rv and the model organism Mycobacterium smegmatis strain PM274. The mutants M. tuberculosis PM638 (ΔblaC1) and M. smegmatis PM759 (ΔblaS1) showed an increase in susceptibility to β-lactam antibiotics, as determined by disc diffusion and minimal inhibitory concentration (MIC) assays. The susceptibility of the mutants, as assayed by disc diffusion tests, to penicillin-type β-lactam antibiotics was affected most, compared to the cephalosporin-type β-lactam antibiotics. The M. tuberculosis mutant had no detectable β-lactamase activity, while the M. smegmatis mutant had a residual type 1 β-lactamase activity. We identified a gene, blaE, encoding a putative cephalosporinase in M. smegmatis. A double β-lactamase mutant of M. smegmatis, PM976 (ΔblaS1ΔblaE : : res), had no detectable β-lactamase activity, but its susceptibility to β-lactam antibiotics was not significantly different from that of the ΔblaS1 parental strain, PM759. The mutants generated in this study will help determine the contribution of other β-lactam resistance mechanisms in addition to serving as tools to study the biology of peptidoglycan biosynthesis in these organisms.

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“…1998), Mycobacterium avium (Casal et al. 1987), M. fortuitum (Utrup et al. 1995) and M. smegmatis (Yabu et al.…”

Section: Discussionmentioning

confidence: 99%

“…Mycobacteria are generally resistant to the beta-lactam antibiotics mainly owing to the presence of b-lactamases (Kasik 1979;Kwon et al 1995). As an alternative treatment, the effectiveness of b-lactam ⁄ b-lactamase inhibitor combinations has been tried in vitro for M. tuberculosis (Chambers et al 1995;Segura et al 1998), Mycobacterium avium (Casal et al 1987), M. fortuitum (Utrup et al 1995) and M. smegmatis (Yabu et al 1985). Overcoming the b-lactam hydrolysis is the major challenge for the effective use of b-lactams in the treatment of tuberculosis and hence an understanding of M. tuberculosis b-lactamase is very important.…”

Section: Discussionmentioning

confidence: 99%

Molecular cloning, overexpression and biochemical characterization of hypothetical β-lactamases ofMycobacterium tuberculosisH37Rv

Nampoothiri

Rubex

Patel

et al. 2008

Journal of Applied Microbiology

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Aim: Molecular cloning, overexpression and biochemical characterization of the genes from the Mycobacterium tuberculosis H37Rv genome having hypothetical β‐lactamases activity. Methods and Results: Analysis of the M. tuberculosis H37Rv genome revealed that Rv2068c, Rv0406c and Rv3677c gene products were predicted to exhibit β‐lactamases activity. All the three genes were cloned in pET28a vector and overexpressed in C41 (DE3) Escherichia coli cells. The His‐tagged recombinant proteins were confirmed by immunoblotting and were shown to have β‐lactamase activity by the hydrolysis of nitrocefin and other β‐lactams. Catalytic parameters for all the recombinant proteins were derived followed by the enzyme inhibition studies. Antibiotic susceptibility studies using the recombinant strains showed an increased resistance against different classes of β‐lactam antibiotics. Conclusion: The study revealed the possibility of more than one gene in M. tuberculosis, encoding proteins having β‐lactamase or β‐lactamase‐like activity, giving wide spectrum of resistance against β‐lactams. Significance and Impact of the Study: Systematic study of hypothetical β‐lactamases of M. tuberculosis and related species and their correlation with β‐lactam and inhibitor susceptibility profile might be useful in developing new antibiotic regime for the treatment of tuberculosis caused by multiple drug resistant (MDR) strains.

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Susceptibilities of nontuberculosis mycobacterial species to amoxicillin-clavulanic acid alone and in combination with antimycobacterial agents

Cited by 18 publications

References 26 publications

A Structure-Based Classification of Class A β-Lactamases, a Broadly Diverse Family of Enzymes

A Structure-Based Classification of Class A β-Lactamases, a Broadly Diverse Family of Enzymes

Genetic analysis of the β-lactamases of Mycobacterium tuberculosis and Mycobacterium smegmatis and susceptibility to β-lactam antibiotics

Molecular cloning, overexpression and biochemical characterization of hypothetical β-lactamases ofMycobacterium tuberculosisH37Rv

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