Skip to main page content
Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Comparative Study
, 69 (2), 83-93

The Cleavage Activation and Sites of Glycosylation in the Fusion Protein of Hendra Virus

Affiliations
Comparative Study

The Cleavage Activation and Sites of Glycosylation in the Fusion Protein of Hendra Virus

W P Michalski et al. Virus Res.

Abstract

Hendra virus (HeV) is an unclassified member of the Paramyxoviridae family that causes systemic infections in humans, horses, cats, guinea pigs and flying foxes. The fusion protein (F(0)) of members of the Paramyxoviridae family that cause systemic infections in vivo contains a basic amino acid-rich region at which the protein is activated by cleavage into two subunits (F(1) and F(2)). HeV F(0) lacks such a domain. We have determined the cleavage site in HeV F(0) by sequencing the amino terminus of the F(1) subunit and in view of the potential effect of glycosylation on the cleavage process have ascertained the sites at which F(0) is glycosylated. The results indicate that unlike other members of the family that replicate in cultured cells and cause systemic infections in vivo, cleavage of HeV F(0) occurs at a single lysine (reside 109) in the sequence Asp-Val-Lys- downward arrow-Leu. Although HeV genotypically resembles members of the Respirovirus and Rubulavirus genera in having potential N-linked glycosylation sites in both the F(1) and F(2) subunits, we show that phenotypically HeV may more closely resemble members of the Morbillivirus genus that contain N-linked glycans only in the F(2) subunit.

Similar articles

See all similar articles

Cited by 20 PubMed Central articles

See all "Cited by" articles

Publication types

LinkOut - more resources

Feedback