[Functional analysis of SpltMNPV envelope protein SL136].

ABSTRACT

Our previous research showed that the Spodoptera litura multinucleocapsid nucleopolyhedrovirus (SpltMNPV) Sl136 product had a function to befused with membrane when expressed alone. In this study, the Sl136 and its product were characterized. RT-PCR results showed that Sl136 could be transcribed at 6 hpost infection, indicating it was an early gene. Then the antiserum against SL136 protein was generated and utilized to verify that SL136 was a BV envelope protein, by using SDS-PAGE and Western blot. Two main protein bands in SpltMNPV-infected Sl-zsu-1 cells were detected; their molecular weights were about 86 kD and 65 kD, respectively. It was found that the size of smaller band coincided with amajor band of BV envelope proteins. SL136 protein was transferred to cell surfaces both in SpltMNPV-infected Sl-zsu-1 cells and recombinant Bac-Sl136-infected Hi5 cells, as detected by cell ELISA(cell enzyme-linked immunosorbant assay, CELISA). From the bioassay results, it was found that furin cleavage of SL136 was not necessary for viral propagation, and inhibition of its glycosylation decreased the BV virulence.