Beta-lactamase database (BLDB) – structure and function

Abstract

Beta-Lactamase Database (BLDB) is a comprehensive, manually curated public resource providing up-to-date structural and functional information focused on this superfamily of enzymes with a great impact on antibiotic resistance. All the enzymes reported and characterised in the literature are presented according to the class (A, B, C and D), family and subfamily to which they belong. All three-dimensional structures of β-lactamases present in the Protein Data Bank are also shown. The characterisation of representative mutants and hydrolytic profiles (kinetics) completes the picture and altogether these four elements constitute the essential foundation for a better understanding of the structure-function relationship within this enzymes family. BLDB can be queried using different protein- and nucleotide-based BLAST searches, which represents a key feature of particular importance in the context of the surveillance of the evolution of the antibiotic resistance. BLDB is available online at http://bldb.eu without any registration and supports all modern browsers.

Molecular characterization of carbapenem-resistant <i>Acinetobacter baumannii</i> isolated from pediatric burns patients in an Iranian hospital

“…MBL enzymes, including IMP, VIM, SPM, GIM, SIM, AIM, FIM, and NDM, are zincdependent carbapenemases; they are inhibited by EDTA and play a crucial role in drug resistance against carbapenems. OXAs, which are not inhibited by EDTA and/or clavulanic acid, are subdivided into six families, as follows: the OXA-23-like, OXA-24/40-like, OXA-51-like, OXA-58-like, OXA-143-like, and OXA-182-like families [4,5].…”

“…In the low-income countries, the incidence of carbapenem-resistant A. baumannii (CR-AB) infections is increasing at an alarming rate, especially among hospitalized burn patients [3]. Carbapenem resistance in A. baumannii is related to several combined mechanisms, such as the acquisition of β-lactamases, AmpC stable derepression, low outer membrane permeability, altered penicillin-binding proteins (PBPs), and less frequently, efflux pump overexpression [4]. Especially, oxacillinase (OXA)-type β-lactamases (Ambler class D enzymes) and metallo-β-lactamases (MBL; Ambler class B enzymes) have been identified worldwide from CR-AB strains.…”

PCR Detection of Oxacillinases in Bacteria

“…The sequences of genes encoding OXA that had been described 17 (last accessed in May 2019) were downloaded from the GenBank database. Comparison of nucleotide/ amino acid sequences and analytics were performed using the bioinformatics software Geneious Prime 2019.2.1 (Biomatters), and used to investigate the polarity and hydrophobicity.…”

“…The OXA enzymes have been subclassified by amino acid sequence similarities into 49 groups, according to the BLDB database. 17 In response to the growing number of the bla OXA genes, we have tried to design primers used to detect most OXA.…”

Transfer learning improves antibiotic resistance class prediction

“…MEGARes [29], NDARO [9], ARG-ANNOT [30], Mustard [31], FARME [32], SARG(v2) [10], Lahey list of β-lactamases [33], BLDB [34], LacED [35,36], CBMAR [37] , MUBII-TB-DB [38], and u-CARE [39]. We collected protein sequences from these databases with their annotations when available.…”