Acetylation of citrate synthase inhibits Bombyx mori nucleopolyhedrovirus propagation by affecting energy metabolism.
Microb Pathog
; 173(Pt B): 105890, 2022 Dec.
Article
en En
| MEDLINE
| ID: mdl-36410583
ABSTRACT
Many studies have confirmed that virus infection cause changes in the expression level and post-translational modifications of tricarboxylic acid cycle (TCA) enzymes. In a previous study, we found that the acetylation level of lysine 336 of Bombyx mori citrate synthase (BmCS) was remarkably unregulated after Bombyx mori nucleopolyhedrovirus (BmNPV) infection. In the present study, we found that BmN cells infected with BmNPV could up-regulate BmCS transient expression and promote the acetylation modification of BmCS. Transient expression vectors for over-expression of wild-type Bmcs and K336 acetylation mimic mutant (K336Q) were constructed to analyze enzyme activity, revealing that acetylation of K336 significantly reduced its activity. The obtained results indicated that BmCS knock-down or K336 acetylation similarly suppressed BmN cellular ATP production and mitochondrial membrane potential. Furthermore, the acetylation of K336 and the reduction of BmCS expression contributed to weakening the replication lever of the BmNPV proliferation and the generation of progeny viruses. In sum, our study on the single lysine 336 acetylation and knock-down of Bmcs revealed the potential mechanism for inhibiting the proliferation of BmNPV, which may provide novel insights for the development of antiviral strategies.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Bombyx
/
Lisina
Límite:
Animals
Idioma:
En
Revista:
Microb Pathog
Asunto de la revista:
DOENCAS TRANSMISSIVEIS
/
MICROBIOLOGIA
Año:
2022
Tipo del documento:
Article