The UTP-glucose-1-phosphate uridylyltransferase of Brucella melitensis inhibits the activation of NF-κB via regulating the bacterial type IV secretion system.
Int J Biol Macromol
; 164: 3098-3104, 2020 Dec 01.
Article
in En
| MEDLINE
| ID: mdl-32827613
ABSTRACT
UDP-glucose pyrophosphorylase (UGPase) is an important pyrophosphatase that reversibly catalyzes the synthesis of UDP-glucose during glucose metabolism. We previously found that the deletion of UGPase may affect structure, growth, the virulence of Brucella, and the activation of cellular NF-κB. However, the exact mechanism of activation of NF-κB regulated by Brucella UGPase is still unclear. Here, we found for the first time that UGPase can regulate the expression of virB proteins (virB3, virB4, virB5, virB6, virB8, virB9, virB10, and virB11) of type IV secretion system (T4SS) as well as effectors (vceC, btpA, btpB, ricA, bspB, bspC, and bspF) of Brucella by promoting the expression of ribosomal S12 protein (rpsL), BMEI1825, and quinone of 2,4,5-trihydroxyphenylalanine (topA) proteins, and further inhibits the activation of cellular NF-κB and affects the virulence of Brucella. Our findings provide new insights into the mechanism used by Brucella to escape the immune recognition, which is expected to be of great value in the designing of Brucella vaccines and the screening of drug targets.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Brucellosis
/
NF-kappa B
/
Brucella melitensis
/
Type IV Secretion Systems
/
UTP-Glucose-1-Phosphate Uridylyltransferase
Type of study:
Prognostic_studies
Limits:
Animals
/
Humans
Language:
En
Journal:
Int J Biol Macromol
Year:
2020
Document type:
Article
Affiliation country:
China