Crystal Structure of Yeast Allantoicase Reveals a Repeated Jelly Roll Motif

Leulliot, Nicolas; Quevillon‐Chéruel, Sophie; Sorel, Isabelle; Graille, Marc; Meyer, Philippe; Liger, Dominique; Blondeau, Karine; Janin, Joël; Tilbeurgh, Herman van

doi:10.1074/jbc.m401336200

Cited by 24 publications

(18 citation statements)

References 36 publications

(23 reference statements)

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“…E. coli DH5␣ (Novagen, Darmstadt, Germany) and E. coli BL21(DE3) (Novagen) were used for cloning experiments (25) and E. coli C600 for mating-out assays. Plasmid pBK-CMV (Stratagene, Amsterdam, The Netherlands) was used for the initial cloning experiments and a modified pET9a plasmid (18) for the overexpression of the ␤-lactamase-encoding genes.…”

Section: Methodsmentioning

confidence: 99%

CMT-Type β-Lactamase TEM-125, an Emerging Problem for Extended-Spectrum β-Lactamase Detection

Robin

Delmas

Archambaud

et al. 2006

Antimicrob Agents Chemother

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The clinical strain Escherichia coli TO799 was resistant to penicillin-clavulanate combinations and ceftazidime and was not reproducibly detected as an extended-spectrum ␤-lactamase (ESBL) according to the standards of the Clinical Laboratory Standards Institute (CLSI; formerly NCCLS) and the national guidelines of the French Society for Microbiology (Comité de l'Antibiogramme de la Société Française de Microbiologie). A novel ␤-lactamase, designated TEM-125, was responsible for this phenotype. TEM-125 harbors a complex association of mutations previously described in the ESBL TEM-12 and in the inhibitor-resistant ␤-lactamase TEM-39. TEM-125 is the first complex mutant TEM to present hydrolytic activity against ceftazidime (k cat , 3.7 s ؊1 ) together with a high level of resistance to clavulanate (50% inhibitory concentration, 13.6 M). The discovery of such an ESBL, which is difficult to detect by the usual ESBL detection methods, confirms the emergence of a complex mutant TEM subgroup and highlights the need to evaluate detection methods so as to avoid possible therapeutic failures.Among Enterobacteriaceae, the most prevalent mechanism of acquired resistance to ␤-lactams is the production of ␤-lactamases such as the penicillinases TEM-1 and SHV-1, which hydrolyze penicillins and narrow-spectrum cephalosporins. In order to thwart these ␤-lactamases, two types of ␤-lactams were developed: ␤-lactam antibiotics resistant to the hydrolysis, such as expanded-spectrum cephalosporins (ceftazidime), and inhibitors of TEM and SHV penicillinases (clavulanic acid and tazobactam). However, the intensive use of these molecules was quickly followed by an evolution of TEM-and SHVtype ␤-lactamases.The first TEM-type extended-spectrum ␤-lactamases (ESBLs) were characterized in 1987 (28). They differ from the SHV and TEM penicillinases by a few amino acid substitutions which confer hydrolytic activity against expanded-spectrum cephalosporins. These ESBLs are susceptible to ␤-lactamase inhibitors. Clinical laboratories are urged by the CLSI (formerly NCCLS) (8) and the Comité de l'Antibiogramme de la Société Française de Microbiologie (CA-SFM) (9) to use the association of hydrolytic activity against expanded-spectrum cephalosporins and susceptibility to inhibitors as a specific means of detecting this type of enzyme.As the use of expanded-spectrum cephalosporins led to the selection of ESBLs, the clinical use of penicillin-␤-lactamase inhibitor combinations led from 1990 onwards to the selection of point mutants of TEM penicillinases resistant to inhibitors (3). However, the strains producing these enzymes, designated inhibitor-resistant TEMs (IRTs), are generally susceptible to cephalosporins (5).A few enzymes that combine ESBL and IRT mutations have recently emerged among the TEM ␤-lactamases. These new enzymes, designated complex mutant TEMs (CMTs), have been identified in different species of Enterobacteriaceae such as Escherichia coli, Klebsiella pneumoniae, Proteus mirabilis, and Enterobacter aerogenes (10,19,22,24,27). De...

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Section: Methodsmentioning

confidence: 99%

CMT-Type β-Lactamase TEM-125, an Emerging Problem for Extended-Spectrum β-Lactamase Detection

Robin

Delmas

Archambaud

et al. 2006

Antimicrob Agents Chemother

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“…E. coli DH5␣ (Novagen, Darmstadt, Germany) and E. coli BL21(DE3) (Novagen, Darmstadt, Germany) were used for the cloning experiments, and E. coli C600 was used for the mating-out assays. The plasmid pBK-CMV (Stratagene, Amsterdam, The Netherlands) was used for the initial cloning experiments, and a modified pET9a plasmid (20) was used for the overexpression of the ␤-lactamase-encoding genes.…”

Section: Methodsmentioning

confidence: 99%

TEM-109 (CMT-5), a Natural Complex Mutant of TEM-1 β-Lactamase Combining the Amino Acid Substitutions of TEM-6 and TEM-33 (IRT-5)

Robin

Delmas

Chanal

et al. 2005

Antimicrob Agents Chemother

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Escherichia coli CF349 exhibited a complex ␤-lactam resistance phenotype, including resistance to amoxicillin and ticarcillin alone and in combination with clavulanate and to some extended-spectrum cephalosporins. The double-disk synergy test was positive. CF349 harbored an 85-kb conjugative plasmid which encoded a ␤-lactamase of pI 5.9. The corresponding bla gene was identified by PCR and sequencing as a bla TEM gene. The deduced protein sequence revealed a new complex mutant of TEM-1 ␤-lactamase designated TEM-109 (CMT-5). TEM-109 contained both the substitutions Glu104Lys and Arg164His of the expanded-spectrum ␤-lactamase (ESBL) TEM-6 and Met69Leu of the inhibitor-resistant TEM-33 (IRT-5). TEM-109 exhibited hydrolytic activity against ceftazidime similar to that of TEM-6 (k cat , 56 s ؊1 and 105 s ؊1 , respectively; K m values, 226 and 247 M, respectively). The 50% inhibitory concentrations of clavulanate and tazobactam (0.13 M and 0.27 M, respectively) were 5-to 10-fold higher for TEM-109 than for TEM-6 (0.01 and 0.06 M, respectively) but were almost 10-fold lower than those for TEM-33. The characterization of this novel CMT, which exhibits a low level of resistance to inhibitors, highlights the emergence of this new ESBL type.The most prevalent mechanism of resistance to ␤-lactam antibiotics in members of the family Enterobacteriaceae is the production of ␤-lactamases belonging to Bush group 2b (6, 21). These enzymes are able to inactivate penicillins and narrowspectrum cephalosporins before they can reach their target.Extended-spectrum ␤-lactamases (ESBLs) were isolated first in Europe and then worldwide shortly after the introduction of oxyimino cephalosporins (28,30). According to the structural classification of Ambler et al.(1) and the functional classification of Bush and Jacoby (6), these first ESBLs were class A enzymes of the 2be group that arose subsequent to a few number of amino acid substitutions from the common plasmid-mediated TEM and SHV-1 ␤-lactamases. These enzymes confer resistance to penicillins, oxyimino cephalosporins, and aztreonam and are susceptible to ␤-lactam inhibitors.The use of ␤-lactamase inhibitors has also been followed by the emergence of resistant clinical isolates, which overproduce TEM-type ␤-lactamases (18) or which produce inhibitor-resistant TEM variants (IRTs) (3). As was the case for the ESBLs, IRTs arose from the common plasmid-mediated TEM and SHV-1 penicillinases subsequent to a few amino acid substitutions. These substitutions conferred resistance to inhibitors but not the ability to hydrolyze oxyimino ␤-lactams.A new subgroup of TEM-and SHV-type ␤-lactamases which harbors both mutations conferring extended-spectrum activity and resistance to inhibitors has emerged since the end of the 1990s in different species of the family Enterobacteriaceae: Escherichia coli, Klebsiella pneumoniae, Proteus mirabilis, and Enterobacter aerogenes. Four enzymes are derived from TEMtype enzymes and were designated complex mutant TEM (CMT-1 to CMT-4) (10,23,24,29). Another complex...

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“…Although AAA and the rat mannosebinding lectin, a C-type lectin, specifically recognize terminal L-fucose (L-Fuc), they do so through differing binding interactions (15), which illustrate convergent functional properties among unrelated lectin families. Most surprisingly, the F-type fold is also shared with several proteins of distinct functional properties, including the C-terminal domain of human blood coagulation factors V (16) and VIII (17), the C-terminal domain of bacterial sialidases (18), the N-terminal domain of a fungal galactose oxidase (19), a human ubiquitin ligase subunit (20), a domain of the single-strand DNA break repair complex (21), the b1 domain of neuropilin (22), and the yeast allantoicase (23). The structural analogy of these seemingly unrelated proteins is indicative of the archaic origin of this lectin fold.…”

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confidence: 99%

Characterization of a Binary Tandem Domain F-type Lectin from Striped Bass (Morone saxatilis)

Odom

Vasta

2006

Journal of Biological Chemistry

137

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Among other functions, lectins play an important role in the innate immune response of vertebrates and invertebrates by recognizing exposed glycans on the surface of potential pathogens. Despite the typically weak interaction of lectin domains with their carbohydrate ligands, they usually achieve high avidity through oligomeric structures or by the presence of tandem carbohydratebinding domains along the polypeptide. The recently described structure of the fucose-binding European eel agglutinin revealed a novel lectin fold (the "F-type" fold), which is shared with other carbohydrate-binding proteins and apparently unrelated proteins from prokaryotes to vertebrates, and a unique fucose-binding sequence motif. Here we described the biochemical and molecular characterization of a unique fucose-binding lectin (MsaFBP32) isolated from serum of the striped bass (Morone saxatilis), composed of two tandem domains that exhibit the eel carbohydrate recognition sequence motif, which we designate F-type. We also described a novel lectin family ("F-type") constituted by a large number of proteins exhibiting greater multiples of the F-type motif, either tandemly arrayed or in mosaic combinations with other domains, including a putative transmembrane receptor, that suggests an extensive functional diversification of this lectin family. Among the tandem lectins, MsaFBP32 and other tandem binary homologues appear unique in that although their N-terminal domain shows close similarity to the fucose recognition domain of the eel agglutinin, their C-terminal domain exhibits changes that potentially could confer a distinct specificity for fucosylated ligands. In contrast with the amniotes, in which the F-type lectins appear conspicuously absent, the widespread gene duplication in the teleost fish suggests these F-type lectins acquired increasing evolutionary value within this taxon.

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Crystal Structure of Yeast Allantoicase Reveals a Repeated Jelly Roll Motif

Cited by 24 publications

References 36 publications

CMT-Type β-Lactamase TEM-125, an Emerging Problem for Extended-Spectrum β-Lactamase Detection

CMT-Type β-Lactamase TEM-125, an Emerging Problem for Extended-Spectrum β-Lactamase Detection

TEM-109 (CMT-5), a Natural Complex Mutant of TEM-1 β-Lactamase Combining the Amino Acid Substitutions of TEM-6 and TEM-33 (IRT-5)

Characterization of a Binary Tandem Domain F-type Lectin from Striped Bass (Morone saxatilis)

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