ampD homologs in biotypes of Yersinia enterocolitica: Implications in regulation of chromosomal AmpC-type cephalosporinases.
Amino Acid Sequence
Bacterial Proteins
/ chemistry
Gene Expression Regulation, Bacterial
Genes, Bacterial
Genotype
Humans
Models, Molecular
Multilocus Sequence Typing
N-Acetylmuramoyl-L-alanine Amidase
/ chemistry
Phylogeny
Protein Conformation
Yersinia Infections
/ microbiology
Yersinia enterocolitica
/ classification
beta-Lactamases
/ genetics
AmpC-type cephalosporinase
AmpD homologs
Biotypes
Regulation
Yersinia enterocolitica
Journal
Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases
ISSN: 1567-7257
Titre abrégé: Infect Genet Evol
Pays: Netherlands
ID NLM: 101084138
Informations de publication
Date de publication:
04 2019
04 2019
Historique:
received:
26
07
2018
revised:
07
01
2019
accepted:
29
01
2019
pubmed:
3
2
2019
medline:
16
1
2020
entrez:
3
2
2019
Statut:
ppublish
Résumé
Inducible 'AmpC-type' chromosomal cephalosporinases have been reported to be differentially expressed in different biotypes of Yersinia entercolocolitica. AmpD amidases are key regulators of the expression of ampC genes in Y. entercolocolitica as their inactivation results in hyper production of AmpC. To understand the differences in regulation of ampC expression in different biotypes of Y. enterocolitica, characteristics of ampD homologs were studied in strains of Y. enterocolitica belonging to five biotypes namely 1A, 1B, 2, 3 and 4. Our results indicated that the mechanisms which regulate expression of ampC might differ in different biotypes. While a three-step regulation mechanism seemed to be functional in biotypes 2, 3 and 4, a two-step regulation mechanism using other AmiD like proteins might be functional in biotypes 1A and 1B. The existence of ampD homolog(s)-mediated expression of ampC in other members of the family Enterobacteriaceae may provide further credence to our findings.
Identifiants
pubmed: 30710654
pii: S1567-1348(18)30550-1
doi: 10.1016/j.meegid.2019.01.033
pii:
doi:
Substances chimiques
Bacterial Proteins
0
AmpD protein, Bacteria
EC 3.5.1.28
N-Acetylmuramoyl-L-alanine Amidase
EC 3.5.1.28
AmpC beta-lactamases
EC 3.5.2.6
beta-Lactamases
EC 3.5.2.6
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
211-215Informations de copyright
Copyright © 2019. Published by Elsevier B.V.