RAA enzyme is a new family of class A extended-spectrum β-lactamase from the Riemerella anatipestifer RCAD0122 strain

2022 ◽  
Author(s):  
Hongyan Luo ◽  
Dekang Zhu ◽  
Mengru Li ◽  
Yunhan Tang ◽  
Wenyu Zhang ◽  
...  
Keyword(s):  
Amino Acid Sequence Identity ◽  
Natural Transformation ◽  
Kinetic Assay ◽  
Riemerella Anatipestifer ◽  
Sequence Identity ◽  
Class A ◽  
New Family ◽  
Extended Spectrum ◽  
Homologous Strain ◽  
Hydrolysis Activity

Whole genome sequencing of Riemerella anatipestifer isolate RCAD0122 revealed a chromosomally-located β-lactamases gene, bla RAA-1 , which encoded a novel class A extended-spectrum β-lactamases (ESBL), RAA-1. The RAA-1 shared ≤ 65% amino acid sequence identity with other characterized β-lactamases. The kinetic assay of native purified RAA-1 revealed ESBL-like hydrolysis activity. Furthermore, bla RAA-1 could be transferred to a homologous strain by natural transformation. However, the epidemiological study showed that the bla RAA-1 gene is not prevalent currently.

scholarly journals A Novel Extended-Spectrum β-Lactamase, SGM-1, from an Environmental Isolate of Sphingobium sp.

2013 ◽  
Vol 57 (8) ◽  
pp. 3783-3788 ◽  
Author(s):  
Toni L. Lamoureaux ◽  
Viktoria Vakulenko ◽  
Marta Toth ◽  
Hilary Frase ◽  
Sergei B. Vakulenko
Keyword(s):  
Amino Acid ◽  
Clavulanic Acid ◽  
Amino Acid Sequence Identity ◽  
Susceptibility Testing ◽  
Environmental Isolate ◽  
Significant Activity ◽  
Content Type ◽  
Sequence Identity ◽  
Class A ◽  
Extended Spectrum

ABSTRACTSGM-1 is a novel class A β-lactamase from an environmental isolate ofSphingobiumsp. containing all of the distinct amino acid motifs of class A β-lactamases. It shares 77 to 80% amino acid sequence identity with putative β-lactamases that are present on the chromosome of allSphingobiumspecies whose genomes were sequenced and annotated. Thus, SGM-type β-lactamases are native to this genus. Antibiotic susceptibility testing classifies SGM-1 as an extended-spectrum β-lactamase, conferring the highest level of resistance to penicillins. Although SGM-1 contains the conserved cysteine residues characteristic of class A carbapenemases, it does not confer resistance to the carbapenem antibiotics imipenem, meropenem, or doripenem but does increase the MIC of ertapenem 8-fold. SGM-1 hydrolyzes penicillins and the monobactam aztreonam with similar catalytic efficiencies, ranging from 105to 106M−1s−1. The catalytic efficiencies of SGM-1 for cefoxitin and ceftazidime were the lowest (102to 103M−1s−1) among the cephalosporins tested, while the catalytic efficiencies against all other cephalosporins varied from about 105to 106M−1s−1. SGM-1 exhibited measurable but not significant activity toward the carbapenems tested. SGM-1 also showed high affinity for clavulanic acid, tazobactam, and sulbactam (Ki< 1 μM); however, only clavulanic acid significantly reduced the MICs of β-lactams.

scholarly journals Chromosome-Encoded Broad-Spectrum Ambler Class A β-Lactamase RUB-1 from Serratia rubidaea

2016 ◽  
Vol 61 (2) ◽  
Author(s):  
Rémy A. Bonnin ◽  
Jennifer Didi ◽  
Ayla Ergani ◽  
Sandra Lima ◽  
Thierry Naas
Keyword(s):  
Amino Acid Sequence Identity ◽  
Consensus Sequence ◽  
Whole Genome ◽  
Content Type ◽  
Promoter Sequences ◽  
Sequence Identity ◽  
Class A ◽  
Rapid Amplification ◽  
Lactamase Gene ◽  
Serratia Rubidaea

ABSTRACT Whole-genome sequencing of Serratia rubidaea CIP 103234T revealed a chromosomally located Ambler class A β-lactamase gene. The gene was cloned, and the β-lactamase, RUB-1, was characterized. RUB-1 displayed 74% and 73% amino acid sequence identity with the GIL-1 and TEM-1 penicillinases, respectively, and its substrate profile was similar to that of the latter β-lactamases. Analysis by 5′ rapid amplification of cDNA ends revealed promoter sequences highly divergent from the Escherichia coli σ70 consensus sequence. This work further illustrates the heterogeneity of β-lactamases among Serratia spp.

scholarly journals An Analysis of Why Highly Similar Enzymes Evolve Differently

Genetics ◽  
2003 ◽  
Vol 163 (2) ◽  
pp. 457-466
Author(s):  
Fahd K Majiduddin ◽  
Timothy Palzkill
Keyword(s):  
Antibiotic Therapy ◽  
Amino Acid Sequence Identity ◽  
Selective Pressure ◽  
Catalytic Efficiency ◽  
Gram Negative Bacteria ◽  
Wild Type ◽  
Gram Negative ◽  
Atomic Structures ◽  
Sequence Identity ◽  
Extended Spectrum

Abstract The TEM-1 and SHV-1 β-lactamases are important contributors to resistance to β-lactam antibiotics in gram-negative bacteria. These enzymes share 68% amino acid sequence identity and their atomic structures are nearly superimposable. Extended-spectrum cephalosporins were introduced to avoid the action of these β-lactamases. The widespread use of antibiotics has led to the evolution of variant TEM and SHV enzymes that can hydrolyze extended-spectrum antibiotics. Despite being highly similar in structure, the TEM and SHV enzymes have evolved differently in response to the selective pressure of antibiotic therapy. Examples of this are at residues Arg164 and Asp179. Among TEM variants, substitutions are found only at position 164, while among SHV variants, substitutions are found only at position 179. To explain this observation, the effects of substitutions at position 164 in both TEM-1 and SHV-1 on antibiotic resistance and on enzyme catalytic efficiency were examined. Competition experiments were performed between mutants to understand why certain substitutions preferentially evolve in response to the selective pressure of antibiotic therapy. The data presented here indicate that substitutions at position Asp179 in SHV-1 and Arg164 in TEM-1 are more beneficial to bacteria because they provide increased fitness relative to either wild type or other mutants.

scholarly journals SCO-1, a Novel Plasmid-Mediated Class A β-Lactamase with Carbenicillinase Characteristics from Escherichia coli

2007 ◽  
Vol 51 (6) ◽  
pp. 2185-2188 ◽  
Author(s):  
C. C. Papagiannitsis ◽  
A. Loli ◽  
L. S. Tzouvelekis ◽  
E. Tzelepi ◽  
G. Arlet ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Amino Acid Sequence Identity ◽  
Sequence Identity ◽  
Class A

ABSTRACT A novel class A β-lactamase (SCO-1) encoded by an 80-kb self-transferable plasmid from Escherichia coli is described. The interaction of SCO-1 with β-lactams was similar to that of the CARB-type enzymes. Also, SCO-1 exhibited a 51% amino acid sequence identity with the RTG subgroup of chromosomal carbenicillinases (RTG-1, CARB-5, and CARB-8).

scholarly journals Class A Carbapenemase FPH-1 from Francisella philomiragia

2012 ◽  
Vol 56 (6) ◽  
pp. 2852-2857 ◽  
Author(s):  
Marta Toth ◽  
Viktoria Vakulenko ◽  
Nuno T. Antunes ◽  
Hilary Frase ◽  
Sergei B. Vakulenko
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence Identity ◽  
Content Type ◽  
E Coli ◽  
New Class ◽  
Sequence Identity ◽  
Class A ◽  
High Level ◽  
Level Resistance

ABSTRACTFPH-1 is a new class A carbapenemase fromFrancisella philomiragia. It produces high-level resistance to penicillins and the narrow-spectrum cephalosporin cephalothin and hydrolyzes these β-lactam antibiotics with catalytic efficiencies of 106to 107M−1s−1. When expressed inEscherichia coli, the enzyme confers resistance to clavulanic acid, tazobactam, and sulbactam and hasKivalues of 7.5, 4, and 220 μM, respectively, against these inhibitors. FPH-1 increases the MIC of the monobactam aztreonam 256-fold and the MIC of the broad-spectrum cephalosporin ceftazidime 128-fold, while the MIC of cefoxitin remains unchanged. MICs of the carbapenem antibiotics imipenem, meropenem, doripenem, and ertapenem are elevated 8-, 8-, 16-, and 64-fold, respectively, against anE. coliJM83 strain producing the FPH-1 carbapenemase. The catalytic efficiencies of the enzyme against carbapenems are in the range of 104to 105M−1s−1. FPH-1 is 77% identical to the FTU-1 β-lactamase fromFrancisella tularensisand has low amino acid sequence identity with other class A β-lactamases. Together with FTU-1, FPH-1 constitutes a new branch of the prolific and ever-expanding class A β-lactamase tree.

scholarly journals The Class A β-Lactamase FTU-1 Is Native to Francisella tularensis

2011 ◽  
Vol 56 (2) ◽  
pp. 666-671 ◽  
Author(s):  
Nuno T. Antunes ◽  
Hilary Frase ◽  
Marta Toth ◽  
Sergei B. Vakulenko
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Francisella Tularensis ◽  
Amino Acid Sequence Identity ◽  
Cysteine Residues ◽  
Content Type ◽  
Sequence Identity ◽  
Class A

ABSTRACTThe class A β-lactamase FTU-1 produces resistance to penicillins and ceftazidime but not to any other β-lactam antibiotics tested. FTU-1 hydrolyzes penicillin antibiotics with catalytic efficiencies of 105to 106M−1s−1and cephalosporins and carbapenems with catalytic efficiencies of 102to 103M−1s−1, but the monobactam aztreonam and the cephamycin cefoxitin are not substrates for the enzyme. FTU-1 shares 21 to 34% amino acid sequence identity with other class A β-lactamases and harbors two cysteine residues conserved in all class A carbapenemases. FTU-1 is the first weak class A carbapenemase that is native toFrancisella tularensis.

scholarly journals Chromosome-Encoded Narrow-Spectrum Ambler Class A β-Lactamase GIL-1 from Citrobacter gillenii

2007 ◽  
Vol 51 (4) ◽  
pp. 1365-1372 ◽  
Author(s):  
Thierry Naas ◽  
Daniel Aubert ◽  
Ayla Özcan ◽  
Patrice Nordmann
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Amino Acid Sequence Identity ◽  
Consensus Sequence ◽  
Promoter Sequences ◽  
Sequence Identity ◽  
Class A ◽  
Narrow Spectrum ◽  
Dna Fragment ◽  
Rapid Amplification

ABSTRACT A novel β-lactamase gene was cloned from the whole-cell DNA of an enterobacterial Citrobacter gillenii reference strain that displayed a weak narrow-spectrum β-lactam-resistant phenotype and was expressed in Escherichia coli. It encoded a clavulanic acid-inhibited Ambler class A β-lactamase, GIL-1, with a pI value of 7.5 and a molecular mass of ca. 29 kDa. GIL-1 had the highest percent amino acid sequence identity with TEM-1 and SHV-1, 77%, and 67%, respectively, and only 46%, 31%, and 32% amino acid sequence identity with CKO-1 (C. koseri), CdiA1 (C. diversus), and SED-1 (C. sedlaki), respectively. The substrate profile of the purified GIL-1 was similar to that of β-lactamases TEM-1 and SHV-1. The bla GIL-1 gene was chromosomally located, as revealed by I-CeuI experiments, and was constitutively expressed at a low level in C. gillenii. No gene homologous to the regulatory ampR genes of chromosomal class C β-lactamases was found upstream of the bla GIL-1 gene, which fits the noninducibility of β-lactamase expression in C. gillenii. Rapid amplification of DNA 5′ ends analysis of the promoter region revealed putative promoter sequences that diverge from what has been identified as the consensus sequence in E. coli. The bla GIL-1 gene was part of a 5.5-kb DNA fragment bracketed by a 9-bp duplication and inserted between the d-lactate dehydrogenase gene and the ydbH genes; this DNA fragment was absent in other Citrobacter species. This work further illustrates the heterogeneity of β-lactamases in Citrobacter spp., which may indicate that the variability of Citrobacter species is greater than expected.

Biochemical characterization of a glucoamylase from Saccharomycopsis fibuligera R64

Biologia ◽  
2011 ◽  
Vol 66 (1) ◽  
Author(s):  
Dessy Natalia ◽  
Keni Vidilaseris ◽  
Pasjan Satrimafitrah ◽  
Wangsa Ismaya ◽  
Purkan ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Amino Acid ◽  
Amino Acid Sequence Identity ◽  
Biochemical Characterization ◽  
Saccharomycopsis Fibuligera ◽  
Sequence Identity ◽  
Ic50 Value ◽  
High Amino Acid ◽  
Ph Range

AbstractGlucoamylase from the yeast Saccharomycopsis fibuligera R64 (GLL1) has successfully been purified and characterized. The molecular mass of the enzyme was 56,583 Da as determined by mass spectrometry. The purified enzyme demonstrated optimum activity in the pH range of 5.6–6.4 and at 50°C. The activity of the enzyme was inhibited by acarbose with the IC50 value of 5 μM. GLL1 shares high amino acid sequence identity with GLU1 and GLA1, which are Saccharomycopsis fibuligera glucoamylases from the strains HUT7212 and KZ, respectively. The properties of GLL1, however, resemble that of GLU1. The elucidation of the primary structure of GLL1 contributes to the explanation of this finding.

scholarly journals Petunia vein banding virus: Characterization of a New Tymovirus from Petunia × hybrida

Plant Disease ◽  
2000 ◽  
Vol 84 (7) ◽  
pp. 739-742 ◽  
Author(s):  
M. A. V. Alexandre ◽  
L. M. L. Duarte ◽  
E. B. Rivas ◽  
C. M. Chagas ◽  
M. M. Barradas ◽  
...  
Keyword(s):  
Nicotiana Benthamiana ◽  
Petunia Hybrida ◽  
Amino Acid Sequence Identity ◽  
Rio Grande Do Sul ◽  
Cytopathic Effects ◽  
Sequence Identity ◽  
Andean Potato ◽  
Plant Families ◽  
Nicandra Physalodes

Petunia plants from a nursery in the State of Rio Grande do Sul, Brazil, showed pronounced vein banding and contained isometric particles with diameters of approximately 45 and 30 nm. The larger ones apparently represent a caulimovirus, while the smaller ones, which included both empty shells and full particles, were identified as those of a new tymovirus for which we propose the name Petunia vein banding virus (PetVBV). Originally, PetVBV was transmitted only with difficulty to healthy petunia plants. However, from an experimentally infected petu-nia, it was later readily transmitted also to Nicotiana benthamiana and Nicandra physalodes, but not to other species in the Solanaceae or other plant families. It produces cytopathic effects typical for tymovirus infections. Its coat protein shows approximately 65% amino acid sequence identity with those of Eggplant mosaic and Andean potato latent viruses, to which it is also serologically more closely related than to any other tymoviruses.

Sign in / Sign up

Export Citation Format

Share Document