Genetic and Biochemical Characterization of FUS-1 (OXA-85), a Narrow-Spectrum Class D β-Lactamase from<i>Fusobacterium nucleatum</i>subsp.<i>polymorphum</i>

Voha, Christine; Docquier, Jean Denis; Rossolini, Gian María; Fosse, T.

doi:10.1128/aac.00058-06

Cited by 27 publications

(13 citation statements)

References 37 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…During the preparation of this manuscript, Voha et al. reported the genetic and biochemical properties of the same class D β‐lactamase as found in our study, named FUS‐1, that was purified from a clinical isolate of F. nucleatum from France (32). This enzyme showed narrow‐spectrum hydrolysing activity, which is not consistent with the usual broad substrate specificity of many class D β‐lactamases that, in some cases, can cover carbapenem antibiotics (34).…”

Section: Discussionsupporting

confidence: 58%

Proteomic analysis of ampicillin‐resistant oral Fusobacterium nucleatum

Al‐Haroni

Skaug

Bakken

et al. 2007

Oral Microbiology and Immunology

View full text Add to dashboard Cite

Synthesis of a class D beta-lactamase by ampicillin-resistant F. nucleatum isolates could complicate antimicrobial treatment because these enzymes might confer resistance to many classes of beta-lactam antibiotics. The differences observed in protein synthesis between ampicillin-resistant and ampicillin-susceptible F. nucleatum may contribute to the antibiotic resistance and virulence of these bacteria.

show abstract

Section: Discussionsupporting

confidence: 58%

Proteomic analysis of ampicillin‐resistant oral Fusobacterium nucleatum

Al‐Haroni

Skaug

Bakken

et al. 2007

Oral Microbiology and Immunology

View full text Add to dashboard Cite

show abstract

“…MT-1 displayed a predicted 3D structure similar to that of SMB-1 from S. marcescens, whereas MT-OXA and MSI-OXA resembled FUS-1 (OXA-85), a narrow-spectrum class D ␤-lactamase identified in Fusobacterium nucleatum subsp. polymorphum (37). All metal-coordinating amino acid residues of subclass B1 MBLs were conserved in PEDO-3 (data not shown).…”

Section: Resultsmentioning

confidence: 91%

The Soil Microbiota Harbors a Diversity of Carbapenem-Hydrolyzing β-Lactamases of Potential Clinical Relevance

Gudeta

Bortolaia

Amos

et al. 2016

Antimicrob Agents Chemother

View full text Add to dashboard Cite

fThe origin of carbapenem-hydrolyzing metallo-␤-lactamases (MBLs) acquired by clinical bacteria is largely unknown. We investigated the frequency, host range, diversity, and functionality of MBLs in the soil microbiota. Twenty-five soil samples of different types and geographical origins were analyzed by antimicrobial selective culture, followed by phenotypic testing and expression of MBL-encoding genes in Escherichia coli, and whole-genome sequencing of MBL-producing strains was performed. Carbapenemase activity was detected in 29 bacterial isolates from 13 soil samples, leading to identification of seven new MBLs in presumptive Pedobacter roseus (PEDO-1), Pedobacter borealis (PEDO-2), Pedobacter kyungheensis (PEDO-3), Chryseobacterium piscium (CPS-1), Epilithonimonas tenax (ESP-1), Massilia oculi (MSI-1), and Sphingomonas sp. (SPG-1). Carbapenemase production was likely an intrinsic feature in Chryseobacterium and Epilithonimonas, as it occurred in reference strains of different species within these genera. The amino acid identity to MBLs described in clinical bacteria ranged between 40 and 69%. Remarkable features of the new MBLs included prophage integration of the encoding gene (PEDO-1), an unusual amino acid residue at a key position for MBL structure and catalysis (CPS-1), and overlap with a putative OXA ␤-lactamase (MSI-1). Heterologous expression of PEDO-1, CPS-1, and ESP-1in E. coli significantly increased the MICs of ampicillin, ceftazidime, cefpodoxime, cefoxitin, and meropenem. Our study shows that MBL producers are widespread in soil and include four genera that were previously not known to produce MBLs. The MBLs produced by these bacteria are distantly related to MBLs identified in clinical samples but constitute resistance determinants of clinical relevance if acquired by pathogenic bacteria.

show abstract

“…polymorphum, a gram-negative anaerobic rod (164). OXA-85 shares only 25 to 44% identity with other class D ␤-lactamases.…”

Section: Naturally Occurring Class D ␤-Lactamasesmentioning

confidence: 99%

Diversity, Epidemiology, and Genetics of Class D β-Lactamases

Poirel

Naas

Nordmann

2010

Antimicrob Agents Chemother

543

485

View full text Add to dashboard Cite

Class D ␤-lactamase-mediated resistance to ␤-lactams has been increasingly reported during the last decade. Those enzymes also known as oxacillinases or OXAs are widely distributed among Gram negatives. Genes encoding class D ␤-lactamases are known to be intrinsic in many Gram-negative rods, including Acinetobacter baumannii and Pseudomonas aeruginosa, but play a minor role in natural resistance phenotypes. The OXAs (ca. 150 variants reported so far) are characterized by an important genetic diversity and a great heterogeneity in terms of ␤-lactam hydrolysis spectrum. The acquired OXAs possess either a narrow spectrum or an expanded spectrum of hydrolysis, including carbapenems in several instances. Acquired class D ␤-lactamase genes are mostly associated to class 1 integron or to insertion sequences.

show abstract

Genetic and Biochemical Characterization of FUS-1 (OXA-85), a Narrow-Spectrum Class D β-Lactamase fromFusobacterium nucleatumsubsp.polymorphum

Cited by 27 publications

References 37 publications

Proteomic analysis of ampicillin‐resistant oral Fusobacterium nucleatum

Proteomic analysis of ampicillin‐resistant oral Fusobacterium nucleatum

The Soil Microbiota Harbors a Diversity of Carbapenem-Hydrolyzing β-Lactamases of Potential Clinical Relevance

Diversity, Epidemiology, and Genetics of Class D β-Lactamases

Contact Info

Product

Resources

About