Bombyx mori UFBP1 regulates apoptosis and promotes BmNPV proliferation by affecting the expression of ER chaperone BmBIP

Int J Biol Macromol. 2024 Nov 15:137681. doi: 10.1016/j.ijbiomac.2024.137681. Online ahead of print.

Abstract

Ubiquitin-fold modifier 1 (UFM1) is attached to protein substrates through the sequential activity of an E1 (UBA5) - E2 (UFC1) - E3 (UFL1) cascade. UFBP1 is a conserved UFL1-interacting protein in mammals. However, to date, no study has been conducted on UFBP1 in silkworm. In this study, we identified a UFBP1 ortholog in the B. mori genome. Spatiotemporal expression profiles showed that BmUFBP1 expression was high in the midgut and fatbody, and at the moth stage. BmUFBP1 knockdown inhibited ER chaperone BmBIP expression and BmNPV proliferation, while BmUFBP1 overexpression increased BmNPV proliferation, and BmBIP rescued BmUFBP1-regulated BmNPV proliferation. Mechanistically, Apoptosis and ATF6 signaling are involved in BmUFBP1-regulated BmBIP expression and BmNPV proliferation. These results suggest that BmUFBP1 facilitates BmNPV proliferation via ATF6-BIP signaling, and provide a potential molecular target for BmNPV prevention and silkworm breeding.

Keywords: Apoptosis; BmNPV; BmUFBP1; ER stress; Unfolded protein response.