Mutational and functional analysis of N-linked glycosylation of envelope fusion protein F of Helicoverpa armigera nucleopolyhedrovirus

The envelope fusion (F) protein of baculoviruses is a heavily N-glycosylated protein that plays asignificant role in the virus infection cycle. N-Linked glycosylation of virus envelope glycoproteinis important for virus envelope glycoprotein folding and its function in general. There are sixpredicted N-glycosylation sites in the F (HaF) protein of Helicoverpa armigeranucleopolyhedrovirus (HearNPV). The N-glycosylation site located in the F2 subunit (N104) ofHaF has been identified and functionally characterized previously (Long et al., 2007). In thisstudy, the other five potential N-glycosylation sites located in the HaF1 subunit, namely, N293,N361, N526, N571 and N595, were analysed extensively to examine their N-glycosylation andrelative importance to the function of HaF. The results showed that four of these five potentialglycosylation sites in the F1 subunit, N293, N361, N526 and N571, were N-glycosylated inF proteins of mature HearNPV budded viruses (BVs) but that N595 was not. In general, theconserved site N526 was critical to the functioning of HaF, as absence of N-glycosylation ofN526 reduced the efficiency of HaF folding and trafficking, consequently decreasedfusogenicity and modified the subcellular localization of HaF proteins, and thus impaired virusproduction and infectivity. The absence of N-glycosylation at other individual sites was found tohave different effects on the fusogenicity and subcelluar distribution of HaF proteins in HzAM1cells. In summary, N-glycosylation plays comprehensive roles in HaF function and virusinfectivity, which is further discussed.

Bibliographic Details

Main Authors:	Shen, Shu, Wang, M., Li, Xin, Li, S., van Oers, M.M., Vlak, J.M., Braakman, I., Hu, Zhihong, Deng, F., Wang, H.
Format:	Article/Letter to editor biblioteca
Language:	English
Subjects:	Life Science,
Online Access:	https://research.wur.nl/en/publications/mutational-and-functional-analysis-of-n-linked-glycosylation-of-e
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