Role of N-linked glycosylation of the Hendra virus fusion protein

James Richard Carter, Cara Theresia Pager, Stephen Derrick Fowler, Rebecca Ellis Dutch

Research output: Contribution to journalArticlepeer-review

40 Scopus citations


The Hendra virus fusion (F) protein contains five potential sites for N-linked glycosylation in the ectodomain. Examination of F protein mutants with single asparagine-to-alanine mutations indicated that two sites in the F 2 subunit (N67 and N99) and two sites in the F1 subunit (N414 and N464) normally undergo N-linked glycosylation. While N-linked modification at N414 is critical for protein folding and transport, F proteins lacking carbohydrates at N67, N99, or N464 remained fusogenically active. As N464 lies within heptad repeat B, these results contrast with those seen for several paramyxovirus F proteins.

Original languageEnglish
Pages (from-to)7922-7925
Number of pages4
JournalJournal of Virology
Issue number12
StatePublished - Jun 2005

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology


Dive into the research topics of 'Role of N-linked glycosylation of the Hendra virus fusion protein'. Together they form a unique fingerprint.

Cite this