SHV Lactamase Engineering Database: a reconciliation tool for SHV β-lactamases in public databases [PDF]
Background SHV β-lactamases confer resistance to a broad range of antibiotics by accumulating mutations. The number of SHV variants is steadily increasing.
Pleiss Juergen, Thai Quan K
doaj +3 more sources
First report of TEM-104-, SHV-99-, SHV-108-, and SHV-110-producing Klebsiella pneumoniae from Iran [PDF]
: INTRODUCTION: Extended-spectrum beta-lactamases (ESBLs) are bacterial enzymes capable of hydrolyzing beta-lactams. The aim of this study was to describe the prevalence of TEM- and SHV-type ESBL-producing Klebsiella pneumoniae strains in Zahedan ...
Shahram Shahraki-Zahedani +4 more
doaj +4 more sources
Study of a Natural Mutant SHV-Type β-Lactamase, SHV-104, from Klebsiella pneumoniae [PDF]
Klebsiella pneumoniae ML2011, a multiresistant isolate, was isolated from the Military Hospital of Tunis (Tunisia). The determination of the minimal inhibitory concentrations exhibited by K. pneumoniae ML2011 was performed by Etest.
Nahed Ben Achour +4 more
doaj +4 more sources
Survey and molecular genetics of SHV beta-lactamases in Enterobacteriaceae in Switzerland: two novel enzymes, SHV-11 and SHV-12 [PDF]
Sixty isolates of Enterobacteriaceae resistant to beta-lactam antibiotics were collected over a period of 2 years in Switzerland and screened by hybridization for the carriage of SHV genes. Thirty-four positive strains were found, and their SHV genes were amplified and sequenced.
M T, Nüesch-Inderbinen +2 more
openaire +2 more sources
Characterization of a novel SHV β-lactamase variant that resembles the SHV-5 enzyme [PDF]
An SHV type beta-lactamase frequently found in enterobacteria isolated in Greek hospitals was analyzed. The enzyme (SHV-5a) conferred resistance to ceftazidime and aztreonam. The DNA sequence of the structural gene was determined. The deduced amino acid sequence showed that positions 70-73 were occupied by the active site tetrad Ser-Thr-Phe-Lys.
E E, Prinarakis +4 more
openaire +2 more sources
Detection of new SHV-12, SHV-5 and SHV-2a variants of extended spectrum Beta-lactamase in Klebsiella pneumoniae in Egypt [PDF]
Les épidémies de Klebsiella pneumoniae présentant une résistance à la β-lactamase à spectre étendu (BLSE) aux céphalosporines de troisième génération ont considérablement augmenté dans les hôpitaux et les communautés du monde entier. L'objectif de l'étude était de caractériser les déterminants génétiques prévalents de l'activité du LBSE de types TEM ...
Newire, Enas A +4 more
openaire +3 more sources
A Genotype-Phenotype Correlation Study of SHV β-Lactamases Offers New Insight into SHV Resistance Profiles [PDF]
The SHV β-lactamases (BLs) have undergone strong allele diversification that has changed their substrate specificities. Based on 147 NCBI entries for SHV alleles, in silico mathematical models predicted 5 positions as relevant for the β-lactamase inhibitor (BLI)-resistant (2br) phenotype, 12 positions as relevant ...
Svetlana, Neubauer +9 more
openaire +2 more sources
Single amino acid substitution between SHV‐1 β‐lactamase and cefotaxime‐hydrolyzing SHV‐2 enzyme [PDF]
SHV‐2 β‐lactamase was purified from an overproducing variant of a clinical isolate of Escherichia coli resistant to cefotaxime. Pure protein was digested by trypsin and Lys‐C endoproteinase. Proteolytic peptides, isolated by reverse‐phase HPLC, were submitted to manual Edman degradation and aligned by homology with the sequence of SHV‐1 β‐lactamase.
Barthélémy, Michel +3 more
openaire +2 more sources
Emergence of an inhibitor-resistant beta-lactamase (SHV-10) derived from an SHV-5 variant [PDF]
An inhibitor-resistant beta-lactamase (SHV-10), derived from an SHV-5 variant (SHV-9), was found in an Escherichia coli clinical isolate. In SHV-10, Ser-130 was replaced by Gly. The enzyme partially retained its ability to hydrolyze penicillins, but its activity against cephalosporins was drastically reduced.
E E, Prinarakis +4 more
openaire +2 more sources
SHV-129: A Gateway to Global Suppressors in the SHV β-Lactamase Family? [PDF]
Enzymes are continually evolving in response to environmental pressures. In order to increase enzyme fitness, amino acid substitutions can occur leading to a changing function or an increased stability. These evolutionary drivers determine the activity of an enzyme and its success in future generations in response to changing conditions such as ...
Marisa L, Winkler, Robert A, Bonomo
openaire +2 more sources

