Analysis of hendra virus fusion protein n-terminal transmembrane residues

Chelsea T. Barrett, Hadley E. Neal, Kearstin Edmonds, J. Lizbeth Reyes Zamora, Andreea Popa, Everett Clinton Smith, Stacy R. Webb, Rebecca Ellis Dutch, Carole L. Moncman

Research output: Contribution to journalArticlepeer-review

1 Scopus citations


Hendra virus (HeV) is a zoonotic enveloped member of the family Paramyoxviridae. To successfully infect a host cell, HeV utilizes two surface glycoproteins: the attachment (G) protein to bind, and the trimeric fusion (F) protein to merge the viral envelope with the membrane of the host cell. The transmembrane (TM) region of HeV F has been shown to have roles in F protein stability and the overall trimeric association of F. Previously, alanine scanning mutagenesis has been performed on the C-terminal end of the protein, revealing the importance of β-branched residues in this region. Additionally, residues S490 and Y498 have been demonstrated to be important for F protein endocytosis, needed for the proteolytic processing of F required for fusion. To complete the analysis of the HeV F TM, we performed alanine scanning mutagenesis to explore the residues in the N-terminus of this region (residues 487–506). In addition to confirming the critical roles for S490 and Y498, we demonstrate that mutations at residues M491 and L492 alter F protein function, suggesting a role for these residues in the fusion process.

Original languageEnglish
Article number2353
Issue number12
StatePublished - Nov 2021

Bibliographical note

Funding Information:
Funding: This research was funded by NIH/NIAID grant number AI051517 to R.E.D.

Publisher Copyright:
© 2021 by the authors. Licensee MDPI, Basel, Switzerland.


  • Fusion protein
  • Hendra virus
  • Membrane fusion
  • Transmembrane domain

ASJC Scopus subject areas

  • Infectious Diseases
  • Virology


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