Residues in the hendra virus fusion protein transmembrane domain are critical for endocytic recycling

Andreea Popa, James R. Carter, Stacy E. Smith, Lance Hellman, Michael G. Fried, Rebecca Ellis Dutch

Research output: Contribution to journalArticlepeer-review

23 Scopus citations

Abstract

Hendra virus is a highly pathogenic paramyxovirus classified as a biosafety level four agent. The fusion (F) protein of Hendra virus is critical for promoting viral entry and cell-to-cell fusion. To be fusogenically active, Hendra virus F must undergo endocytic recycling and cleavage by the endosomal/lysosomal protease cathepsin L, but the route of Hendra virus F following internalization and the recycling signals involved are poorly understood. We examined the intracellular distribution of Hendra virus F following endocytosis and showed that it is primarily present in Rab5- and Rab4-positive endosomal compartments, suggesting that cathepsin L cleavage occurs in early endosomes. Hendra virus F transmembrane domain (TMD) residues S490 and Y498 were found to be important for correct Hendra virus F recycling, with the hydroxyl group of S490 and the aromatic ring of Y498 important for this process. In addition, changes in association of isolated Hendra virus F TMDs correlated with alterations to Hendra virus F recycling, suggesting that appropriate TMD interactions play an important role in endocytic trafficking.

Original languageEnglish
Pages (from-to)3014-3026
Number of pages13
JournalJournal of Virology
Volume86
Issue number6
DOIs
StatePublished - Mar 2012

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

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