NADH oxidase of Mycoplasma hyopneumoniae functions as a potential mediator of virulence.
Adhesion
Mycoplasma hyopneumoniae
NADH oxidase
Virulence factor
Journal
BMC veterinary research
ISSN: 1746-6148
Titre abrégé: BMC Vet Res
Pays: England
ID NLM: 101249759
Informations de publication
Date de publication:
02 Apr 2022
02 Apr 2022
Historique:
received:
04
01
2022
accepted:
25
03
2022
entrez:
3
4
2022
pubmed:
4
4
2022
medline:
6
4
2022
Statut:
epublish
Résumé
Mycoplasma hyopneumoniae (M. hyopneumoniae) is the etiological agent of enzootic pneumonia, a highly infectious swine respiratory disease that distributed worldwide. The pathogenesis and virulence factors of M. hyopneumoniae are not fully clarified. As an important virulence factor of bacteria, nicotinamide adenine dinucleotide (NADH) oxidase (NOX) participates in host-pathogen interaction, however, the function of NOX involved in the pathogenesis of M. hyopneumoniae is not clear. In this study, significant differences in NOX transcription expression levels among different strains of M. hyopneumoniae differed in virulence were identified, suggesting that NOX may be correlated with M. hyopneumoniae virulence. The nox gene of M. hyopneumoniae was cloned and expressed in Escherichia coli, and polyclonal antibodies against recombinant NOX (rNOX) were prepared. We confirmed the enzymatic activity of rNOX based on its capacity to oxidize NADH to NAD NOX is considered to be a potential virulence factor of M. hyopneumoniae and may play a significant role in mediating its pathogenesis.
Sections du résumé
BACKGROUND
BACKGROUND
Mycoplasma hyopneumoniae (M. hyopneumoniae) is the etiological agent of enzootic pneumonia, a highly infectious swine respiratory disease that distributed worldwide. The pathogenesis and virulence factors of M. hyopneumoniae are not fully clarified. As an important virulence factor of bacteria, nicotinamide adenine dinucleotide (NADH) oxidase (NOX) participates in host-pathogen interaction, however, the function of NOX involved in the pathogenesis of M. hyopneumoniae is not clear.
RESULTS
RESULTS
In this study, significant differences in NOX transcription expression levels among different strains of M. hyopneumoniae differed in virulence were identified, suggesting that NOX may be correlated with M. hyopneumoniae virulence. The nox gene of M. hyopneumoniae was cloned and expressed in Escherichia coli, and polyclonal antibodies against recombinant NOX (rNOX) were prepared. We confirmed the enzymatic activity of rNOX based on its capacity to oxidize NADH to NAD
CONCLUSIONS
CONCLUSIONS
NOX is considered to be a potential virulence factor of M. hyopneumoniae and may play a significant role in mediating its pathogenesis.
Identifiants
pubmed: 35366872
doi: 10.1186/s12917-022-03230-7
pii: 10.1186/s12917-022-03230-7
pmc: PMC8976378
doi:
Substances chimiques
Multienzyme Complexes
0
NAD
0U46U6E8UK
Oxidoreductases
EC 1.-
NADH oxidase
EC 1.6.-
NADH, NADPH Oxidoreductases
EC 1.6.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
126Subventions
Organisme : the Independent Research Project Program of Jiangsu Key Laboratory for Food Quality and Safety-State Key Laboratory Cultivation Base, Ministry of Science and Technology, China
ID : 2019sy004
Organisme : Jiangsu Agriculture Science and Technology Innovation Fund
ID : CX(21)3124
Organisme : National Natural Science Foundation of China
ID : 31800161
Organisme : National Natural Science Foundation of China
ID : 31800160
Informations de copyright
© 2022. The Author(s).
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