scholarly journals Novel Plasmid-Mediated tet(X5) Gene Conferring Resistance to Tigecycline, Eravacycline, and Omadacycline in a Clinical Acinetobacter baumannii Isolate

2019 ◽  
Vol 64 (1) ◽  
Author(s):  
Liyuan Wang ◽  
Dejun Liu ◽  
Yuan Lv ◽  
Lanqing Cui ◽  
Yun Li ◽  
...  
Keyword(s):  
Amino Acid ◽  
Acinetobacter Baumannii ◽  
Binding Sites ◽  
Amino Acid Identity ◽  
Gene Variant ◽  
Content Type ◽  
Acid Identity ◽  
X Gene ◽  
High Level ◽  
Baumannii Isolate

ABSTRACT A novel, plasmid-mediated, high-level tigecycline resistance tet(X) gene variant, tet(X5), was detected in a clinical Acinetobacter baumannii isolate from China in 2017. Tet(X5) shows 84.5% and 90.5% amino acid identity to Tet(X3) and Tet(X4), respectively, with similar binding sites and a comparable affinity for tetracyclines. The tet(X5)-containing plasmid could only be transferred to A. baumannii via electrotransformation. This report follows the recent study describing the identification of tet(X3) and tet(X4).

scholarly journals Coproduction of 16S rRNA Methyltransferase RmtD or RmtG with KPC-2 and CTX-M Group Extended-Spectrum β-Lactamases in Klebsiella pneumoniae

2013 ◽  
Vol 57 (5) ◽  
pp. 2397-2400 ◽  
Author(s):  
Maria Fernanda C. Bueno ◽  
Gabriela R. Francisco ◽  
Jessica A. O'Hara ◽  
Doroti de Oliveira Garcia ◽  
Yohei Doi
Keyword(s):  
Amino Acid ◽  
16S Rrna ◽  
Klebsiella Pneumoniae ◽  
Amino Acid Identity ◽  
Aminoglycoside Resistance ◽  
Content Type ◽  
Acid Identity ◽  
Paulo State ◽  
Extended Spectrum ◽  
High Level

ABSTRACTEightKlebsiella pneumoniaeclinical strains with high-level aminoglycoside resistance were collected from eight hospitals in São Paulo State, Brazil, in 2010 and 2011. Three of them produced an RmtD group 16S rRNA methyltransferase, RmtD1 or RmtD2. Five strains were found to produce a novel 16S rRNA methyltransferase, designated RmtG, which shared 57 to 58% amino acid identity with RmtD1 and RmtD2. Seven strains coproduced KPC-2 with or without various CTX-M group extended-spectrum β-lactamases, while the remaining strain coproduced CTX-M-2.

scholarly journals PFM-Like Enzymes Are a Novel Family of Subclass B2 Metallo-β-Lactamases from Pseudomonas synxantha Belonging to the Pseudomonas fluorescens Complex

2019 ◽  
Vol 64 (2) ◽  
Author(s):  
Laurent Poirel ◽  
Mattia Palmieri ◽  
Michael Brilhante ◽  
Amandine Masseron ◽  
Vincent Perreten ◽  
...  
Keyword(s):  
Amino Acid ◽  
Pseudomonas Fluorescens ◽  
Bacterial Species ◽  
Amino Acid Identity ◽  
Chicken Meat ◽  
The Novel ◽  
Content Type ◽  
Acid Identity ◽  
Carbapenem Resistant ◽  
Encoding Genes

ABSTRACT A carbapenem-resistant Pseudomonas synxantha isolate recovered from chicken meat produced the novel carbapenemase PFM-1. That subclass B2 metallo-β-lactamase shared 71% amino acid identity with β-lactamase Sfh-1 from Serratia fonticola. The blaPFM-1 gene was chromosomally located and likely acquired. Variants of PFM-1 sharing 90% to 92% amino acid identity were identified in bacterial species belonging to the Pseudomonas fluorescens complex, including Pseudomonas libanensis (PFM-2) and Pseudomonas fluorescens (PFM-3), highlighting that these species constitute reservoirs of PFM-like encoding genes.

scholarly journals Novel Biphenyl-Oxidizing Bacteria and Dioxygenase Genes from a Korean Tidal Mudflat

2011 ◽  
Vol 77 (11) ◽  
pp. 3888-3891 ◽  
Author(s):  
Tae Kwon Lee ◽  
Jaejin Lee ◽  
Woo Jun Sul ◽  
Shoko Iwai ◽  
Benli Chai ◽  
...  
Keyword(s):  
Amino Acid ◽  
Stable Isotope ◽  
16S Rrna ◽  
Amino Acid Identity ◽  
Stable Isotope Probing ◽  
Content Type ◽  
Acid Identity ◽  
Rrna Sequences ◽  
Mudflat Sediments ◽  
16S Rrna Sequences

ABSTRACTGene-targeted FLX titanium pyrosequencing integrated with stable isotope probing (SIP) using [13C]biphenyl substrate revealed that tidal mudflat sediments harbor novel aromatic ring hydroxylating dioxygenases (ARHD). More than 80% of the detected ARHD genes comprise four clades (0.5 distance) with 49 to 70% amino acid identity to sequences in public databases. The 16S rRNA sequences enriched in the13C fraction were from theBetaproteobacteria, bacilli (primarilyPaenibacillus-like), and unclassified phyla.

scholarly journals Identification of FosA8, a Plasmid-Encoded Fosfomycin Resistance Determinant from Escherichia coli, and Its Origin in Leclercia adecarboxylata

2019 ◽  
Vol 63 (11) ◽  
Author(s):  
Laurent Poirel ◽  
Xavier Vuillemin ◽  
Nicolas Kieffer ◽  
Linda Mueller ◽  
Marie-Christine Descombes ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid Identity ◽  
Natural Resistance ◽  
Whole Genome ◽  
Content Type ◽  
Acid Identity ◽  
E Coli ◽  
Fosfomycin Resistance ◽  
High Level ◽  
Level Resistance

ABSTRACT A plasmid-located fosfomycin resistance gene, fosA8, was identified from a CTX-M-15-producing Escherichia coli isolate recovered from urine. Identification of this gene was obtained by whole-genome sequencing. It encoded FosA8, which shares 79% and 78% amino acid identity with the most closely related FosA2 and FosA1 enzymes, respectively. The fosA8 gene was located on a transferable 50-kb plasmid of IncN type encoding high-level resistance to fosfomycin. In silico analysis and cloning experiments identified fosA8 analogues (99% identity) in the genome of Leclercia decarboxylata, which is an enterobacterial species with natural resistance to fosfomycin. This finding adds L. decarboxylata to the list of enterobacterial species that are a reservoir of fosA-like genes which have been captured from the chromosome of a progenitor and are then acquired by E. coli.

scholarly journals Interference between avian endogenous ev/J 4.1 and exogenous ALV-J retroviral envelopes

2003 ◽  
Vol 84 (12) ◽  
pp. 3233-3238 ◽  
Author(s):  
Caroline Denesvre ◽  
Denis Soubieux ◽  
Gaelle Pin ◽  
Dominique Hue ◽  
Ginette Dambrine
Keyword(s):  
Amino Acid ◽  
Envelope Protein ◽  
Avian Leukosis Virus ◽  
Amino Acid Identity ◽  
Acid Identity ◽  
New Family ◽  
Endogenous Sequence ◽  
High Level

A new family of avian retroviral endogenous sequences designated ev/J or EAV-HP has been identified recently. Here an additional avian ev/J 4.1 endogenous sequence, ev/J 4.1 Rb, is reported. ev/J 4.1 Rb has the most extensive amino acid identity ever described for an endogenous envelope protein with the ALV-J avian leukosis virus. Here, we also demonstrate that ev/J 4.1 Rb functionally pseudotypes murine leukaemia virions and leads to a complete reciprocal interference with ALV-J envelopes. This is the first demonstration of such a high level of envelope interference between endogenous and exogenous avian retroviruses. Our results provide additional clues on the co-evolution of retroviral sequences among vertebrates.

scholarly journals Association of the Emerging Carbapenemase NDM-1 with a Bleomycin Resistance Protein in Enterobacteriaceae and Acinetobacter baumannii

2012 ◽  
Vol 56 (4) ◽  
pp. 1693-1697 ◽  
Author(s):  
Laurent Dortet ◽  
Patrice Nordmann ◽  
Laurent Poirel
Keyword(s):  
Acinetobacter Baumannii ◽  
Insertion Sequence ◽  
Amino Acid Identity ◽  
Experimental Conditions ◽  
Death Rates ◽  
Content Type ◽  
Acid Identity ◽  
E Coli ◽  
Carbapenemase Gene ◽  
Resistance Protein

ABSTRACTThe carbapenemase NDM-1 has been identified recently inEnterobacteriaceaeandAcinetobacter baumanniias a source of multidrug resistance, including resistance to carbapenems. By analyzing the immediate genetic environment of theblaNDM-1carbapenemase gene among a series of NDM-1-producing enterobacterial isolates, a novel gene (bleMBL, forblegene associated with the metallo-β-lactamase NDM-1) was identified. ThebleMBLgene encodes a novel bleomycin resistance protein (BRP), named BRPMBL, that shares weak similarities with known BRPs (less than 60% amino acid identity). The expression of BRPMBLconferred resistance to bleomycin and to bleomycin-like molecules inEnterobacteriaceaeandA. baumannii. TheblaNDM-1andbleMBLgenes were coexpressed under the control of the same promoter, located upstream of theblaNDM-1gene and at the extremity of the insertion sequence ISAba125. Most of the NDM producers possessed thebleMBLgene. Although BRPMBLdid not modify the growth or death rates ofEscherichia coliunder experimental conditions, it suppressed the mutation rate of hypermutableE. coliand therefore may stabilize the plasmid-borneblaNDM-1gene. This study suggests that the emerging carbapenemase NDM-1 is selected by bleomycin-like molecules, and that BRPMBLproducers (and consequently NDM producers) are better suited to various environments.

scholarly journals First Report of the Carbapenemase Gene blaOXA-499 in Acinetobacter pittii

2017 ◽  
Vol 61 (5) ◽  
Author(s):  
Roshan D'Souza ◽  
Naina Adren Pinto ◽  
Paul G. Higgins ◽  
Insik Hwang ◽  
Dongeun Yong ◽  
...  
Keyword(s):  
Amino Acid ◽  
Clinical Isolate ◽  
Amino Acid Identity ◽  
Content Type ◽  
Acid Identity ◽  
First Report ◽  
Carbapenemase Gene ◽  
Acinetobacter Pittii ◽  
Encoding Gene ◽  
First Time

ABSTRACT We identified the carbapenemase gene bla OXA-499, a variant of bla OXA-143, from a clinical isolate of Acinetobacter pittii for the first time. OXA-499 shared 93.1% amino acid identity with OXA-143, and the gene was located on the chromosome. By cloning the OXA-499-encoding gene into the pWH1266 vector and transforming it into susceptible Acinetobacter spp., we were able to show that OXA-499 confers resistance to carbapenems.

scholarly journals Exploration of Two Pectate Lyases from Caldicellulosiruptor bescii Reveals that the CBM66 Module Has a Crucial Role in Pectic Biomass Degradation

2020 ◽  
Vol 86 (16) ◽  
Author(s):  
Hamed I. Hamouda ◽  
Nasir Ali ◽  
Hang Su ◽  
Jie Feng ◽  
Ming Lu ◽  
...  
Keyword(s):  
Amino Acid ◽  
Plant Biomass ◽  
Degradation Products ◽  
Amino Acid Identity ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Module ◽  
Content Type ◽  
Acid Identity ◽  
Pectate Lyases ◽  
Caldicellulosiruptor Bescii

ABSTRACT Pectin deconstruction is the initial step in breaking the recalcitrance of plant biomass by using selected microorganisms that encode pectinolytic enzymes. Pectate lyases that cleave the α-1,4-galacturonosidic linkage of pectin are widely used in industries such as papermaking and fruit softening. However, there are few reports on pectate lyases with good thermostability. Here, two pectate lyases (CbPL3 and CbPL9) from a hyperthermophilic bacterium, Caldicellulosiruptor bescii, belonging to family 3 and family 9 polysaccharide lyases, respectively, were investigated. The biochemical properties of the two CbPLs were shown to be similar under optimized conditions of 80°C to 85°C and pH 8 to 9. However, the degradation products from pectin and polygalacturonic acids (pGAs) were different. A family 66 carbohydrate-binding module (CbCBM66) located in the N terminus of the two CbPLs shares 100% amino acid identity. A CbCBM66-truncated mutant of CbPL9 showed lower activities than the wild type, whereas CbPL3 with a CbCBM66 knockout portion was reported to have enhanced activities, thereby revealing the different effect of CbCBM66. Prediction by the I-TASSER server revealed that CbCBM66 is structurally close to BsCBM66 from Bacillus subtilis; however, the COFACTOR and COACH programs indicated that the substrate-binding sites between CbCBM66 and BsCBM66 are different. Furthermore, a substrate-binding assay indicated that the catalytic domains in the two CbPLs had strong affinities for pectate-related substrates, but CbCBM66 showed a weak interaction with a number of lignocellulosic carbohydrates. Finally, scanning electron microscopy (SEM) analysis and a total reducing sugar assay showed that the two enzymes could improve the saccharification of switchgrass. The two CbPLs are impressive sources for the degradation of plant biomass. IMPORTANCE Thermophilic proteins could be implemented in diverse industrial applications. We sought to characterize two pectate lyases, CbPL3 and CbPL9, from a thermophilic bacterium, Caldicellulosiruptor bescii. The two enzymes share a high optimum temperature, a low optimum pH, and good thermostability at the evaluated temperature. A family 66 carbohydrate-binding module (CbCBM66) was identified in the two CbPLs, sharing 100% amino acid identity. The deletion of CbCBM66 dramatically decreased the activity of CbPL9 but increased the activity and thermostability of CbPL3, suggesting different roles of CbCBM66 in the two enzymes. Moreover, the degradation products of the two CbPLs were different. These results revealed that these enzymes could represent potential pectate lyases for applications in the paper and textile industries.

Mutations in aarE, the ubiA Homolog of Providencia stuartii, Result in High-Level Aminoglycoside Resistance and Reduced Expression of the Chromosomal Aminoglycoside 2′-N-Acetyltransferase

1998 ◽  
Vol 42 (4) ◽  
pp. 959-962 ◽  
Author(s):  
Michael R. Paradise ◽  
Gregory Cook ◽  
Robert K. Poole ◽  
Philip N. Rather
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Identity ◽  
Second Step ◽  
Aminoglycoside Resistance ◽  
Acid Identity ◽  
E Coli ◽  
Small Colony ◽  
Providencia Stuartii ◽  
High Level

ABSTRACT The aarE1 allele was identified on the basis of the resulting phenotype of increased aminoglycoside resistance. TheaarE1 mutation also resulted in a small-colony phenotype and decreased levels of aac(2′)-Ia mRNA. The deduced AarE gene product displayed 61% amino acid identity to theEscherichia coli UbiA protein, an octaprenyltransferase required for the second step of ubiquinone biosynthesis. Complementation experiments in both Providencia stuartiiand E. coli demonstrated that aarE andubiA are functionally equivalent.

scholarly journals Heterogeneity of AmpC Cephalosporinases ofHafnia alvei Clinical Isolates Expressing Inducible or Constitutive Ceftazidime Resistance Phenotypes

2000 ◽  
Vol 44 (11) ◽  
pp. 3220-3223 ◽  
Author(s):  
Delphine Girlich ◽  
Thierry Naas ◽  
Samuel Bellais ◽  
Laurent Poirel ◽  
Amal Karim ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Identity ◽  
Clinical Isolates ◽  
Hafnia Alvei ◽  
Acid Identity ◽  
Genetic Environment ◽  
Low Level ◽  
High Level

ABSTRACT Ten unrelated Hafnia alvei clinical isolates were grouped according to either their low-level and inducible cephalosporinase production or their high-level and constitutive cephalosporinase production phenotype. Their AmpC sequences shared 85 to 100% amino acid identity. The immediate genetic environment ofampC genes was conserved in H. alvei isolates but was different from that found in other ampC-possessing enterobacterial species.

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