Nucleotide and Amino Acid Sequences of the Metallo-β-Lactamase, ImiS, from
            <i>Aeromonas veronii</i>
            bv. sobria

Walsh, Timothy R.; Neville, William A.; Haran, M. H.; Tolson, D.; Payne, D. J.; Bateson, John H.; MacGowan, Alasdair; Bennett, Peter M.

doi:10.1128/aac.42.2.436

Cited by 48 publications

(26 citation statements)

References 24 publications

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“…Notwithstanding, BcII became one of the workhorses for structural and mechanistic studies on MBLs [16][17][18][19][20][21][22][23][24]. This scenario changed in the 1980s when an increasingly large number of clinical isolates of Bacteroides fragilis [25], Stenotrophomonas maltophilia [26], various Aeromonas [27,28] and Chryseobacterium [29][30][31] species were found to express diverse chromosomally encoded Zn(II) b-lactamases. Among Gram negative bacteria, a silent gene coding for an MBL was found in Bacillus anthracis [32].…”

Section: Emergence Of Antibiotic Resistance By Metallo-b-lactamasesmentioning

confidence: 99%

“…This group includes endogenous MBLs like A. hydrophilia CphA (Carbapenemhydrolyzing metallo-b-lactamase) [54], Aeromonas veronii ImiS (Imipenemase from A. veronii bv. sobria) [28] and Serratia fonticola Sfh-I [36]. Finally, subclass B3 MBLs, the most distant in phylogenetic terms [46], comprises endogenous enzymes sharing only 9 residues with the rest of MBLs.…”

Section: Mbls Superfamily and Classificationmentioning

confidence: 99%

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Overcoming differences: The catalytic mechanism of metallo‐β‐lactamases

2015

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Metallo-β-lactamases are the latest resistance mechanism of pathogenic and opportunistic bacteria against carbapenems, considered as last resort drugs. The worldwide spread of genes coding for these enzymes, together with the lack of a clinically useful inhibitor, have raised a sign of alarm. Inhibitor design has been mostly impeded by the structural diversity of these enzymes. Here we provide a critical review of mechanistic studies of the three known subclasses of metallo- β-lactamases, analyzed at the light of structural and mutagenesis investigations. We propose that these enzymes present a modular structure in their active sites that can be dissected into two halves: one providing the attacking nucleophile, and the second one stabilizing a negatively charged reaction intermediate. These are common mechanistic elements in all metallo-β-lactamases. Nucleophile activation does not necessarily requires a Zn(II) ion, but a Zn(II) center is essential for stabilization of the anionic intermediate. Design of a common inhibitor could be therefore approached based in these convergent mechanistic features despite the structural differences.

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Section: Emergence Of Antibiotic Resistance By Metallo-b-lactamasesmentioning

confidence: 99%

Section: Mbls Superfamily and Classificationmentioning

confidence: 99%

Overcoming differences: The catalytic mechanism of metallo‐β‐lactamases

2015

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“…This ImiS metallo-b-lactamase belongs to the molecular class B or group 3 and is 98 % identical to CphA, a metallo-b-lactamase found in A. hydrophila (Hernandez Valladares et al, 2000). ImiS is a monomeric enzyme able to hydrolyse carbapenems such as imipenem and meropenem but with poor activity against other blactams (Walsh et al, 1996(Walsh et al, , 1998.…”

Section: Introductionmentioning

confidence: 99%

Development of imipenem resistance in an Aeromonas veronii biovar sobria clinical isolate recovered from a patient with cholangitis

Sánchez‐Céspedes

Figueras

Aspíroz

et al. 2009

Journal of Medical Microbiology

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Several imipenem-susceptible and -resistant Aeromonas veronii biovar sobria isolates with different morphologies and antimicrobial susceptibilities recovered from bile samples of a patient with cholangitis were analysed. These isolates belonged to the same clone and the imipenemresistant strains showed overexpression of the imiS gene, encoding a chromosomal carbapenemase. These results should make clinicians aware of the possible emergence of multidrug-resistant A. veronii biovar sobria, perhaps as a consequence of previous treatment of a urinary tract infection with amoxicillin plus clavulanic acid.

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“…Up to date, the impact of the production of YEM-1 on the resistance pattern is unknown. Compared to the characterized sub-class B2 MBLs (14), such as CphA (15), SfhI (16) and ImiS (17), the amino acids involved in the two zinc binding sites were strictly conserved, (N116, H118 and H196 for Zn 1 and D120, C221 and H263 for Zn2). CphA is the most studied enzyme of the sub-class B2 MBLs (18–20).…”

Section: Introductionmentioning

confidence: 97%

Mutational effects on carbapenem hydrolysis of YEM-1, a new sub-class B2 metallo-β-lactamase fromYersinia mollaretii

Mercuri

Esposito

Blétard

et al. 2020

Preprint

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1The analysis of the genome sequence of Yersinia mollaretii (Y. mollaretii) ATCC 43969 indicates 2 the presence of the bla YEM gene coding for YEM-1, a putative subclass B2 metallo-β-lactamase. The 3 objectives of our work were to produce, purify and complete the kinetic characterization of Compared to the known subclass B2 metallo−β-lactamases, YEM-1 displayed a narrowest substrate 5 profile since it is only able to hydrolyse imipenem with a high catalytic efficiency but not all the 6 other carbapenems tested such as biapenem, meropenem, doripenem and ertapenem. A possible 7 explanation of this peculiar activity profile is the presence of tyrosine 67 (loop L1), threonine 156 8 (loop L2) and serine 236 (loop L3) respectively. We showed that the substitution of Y67 broadened 9 the activity profile of the enzyme for all carbapenems but still displayed a poor activity toward the 10 other β-lactam classes. The genus Yersinia belonging to the family of Enterobacteriaceae shows three mains groups of 31 human pathogen strains, Yersinia pestis (Y. pestis), Yersinia pseudotuberculosis (Y. pseudo-32 tuberculosis) and Yersinia enterolitica (Y. enterocolitica). Y. pestis, the bacterial agent of bubonic 33 plague, escapes the macrophages action and is the cause of a lethal bacteremia without antibiotic 34 treatments (1). A new threat is the emergence of a multidrug resistant Y. pestis strain (2). Y. 35 pseudotubercolis and Y. enterocolitica are important cause of gastroenteritis in human following the 36 ingestion of undercooked or contaminated pork and vegetables (3-4). Others Yersinia species like Y. 37 fredricksenii, Y. kristensenii, Y. intermedia, Y. mollaretii, Y. bercovieri and Y. rohdei are considered 38 as not pathogen for human (5-6). Our interest was focused on Y. mollaretii. This specie, previously 39 known as Y. enterocolitica-like organism biogroup A, was renamed Yersinia mollaretii and 40 assigned in the new biogroup 3A by Wauters et al (7). The majority of those strains were isolated 41 from environmental sources such as soil, drinking water, raw vegetables, and meat but few were 42 clinical isolates from patient stools affected by gastrointestinal disease. It was demonstrated that it 43 can colonize the low level of the human ileum but the absence of human virulence markers 44 classified this strain as non-pathogenic and saprophyte (8). The sequence genome of the reference 45 strain Y. mollaretii ATCC 43969 (numbered as CCUG26331, CDC2465-87, CIP103324 and 46 DSM18520 in other biobanks) was determined (NCBI Reference Sequence: 47 NZ_AALD02000006.1). Its analysis indicated the presence of two β-lactamase genes, namely blaB 48 coding for an AmpC-like enzyme and one coding for a putative sub-class B2 metallo β-lactamase 49 called YEM-1 (YErsinia Metallo-β-lactamase -GenBank: EEQ11779.1). It is interesting to note the 50 absence of the blaA gene encoding for an Extented Spectrum class A β-Lactamase found in other 51 Yersinia species (9-12). This observation is in good agreement with the phenotypic studies showing...

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Nucleotide and Amino Acid Sequences of the Metallo-β-Lactamase, ImiS, from Aeromonas veronii bv. sobria

Cited by 48 publications

References 24 publications

Overcoming differences: The catalytic mechanism of metallo‐β‐lactamases

Overcoming differences: The catalytic mechanism of metallo‐β‐lactamases

Development of imipenem resistance in an Aeromonas veronii biovar sobria clinical isolate recovered from a patient with cholangitis

Mutational effects on carbapenem hydrolysis of YEM-1, a new sub-class B2 metallo-β-lactamase fromYersinia mollaretii

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