The role of N-linked glycosylation in proteolytic processing and cell surface transport of the Cedar virus fusion protein.

ABSTRACT:

Background

N-linked glycans on viral glycoproteins have been shown to be important for protein expression, processing and intracellular transport. The fusion glycoprotein F of Cedar virus (CedV) contains six potential N-glycosylation sites.

Findings

To investigate their impact on cell surface transport, proteolytic cleavage and biological activity, we disrupted the consensus sequences by conservative mutations (Asn to Gln) and found that five of the six potential N-glycosylation sites are actually utilized. The individual removal of N-glycan g1 (N66), g2 (N79) and g3 (N98) in the CedV F₂ subunit had no or only little effect on cell surface transport, proteolytic cleavage and fusion activity of CedV F. Interestingly, removal of N-linked glycan g6 (N463) in the F

SUBMITTER: Fischer K 

PROVIDER: S-EPMC9400332 | biostudies-literature | 2022 Aug

REPOSITORIES: biostudies-literature