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.
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This research was funded by NIH/NIAID grant number AI051517 to R.E.D.
Data is available upon request from the corresponding author.
Barrett, Chelsea T.; Neal, Hadley E.; Edmonds, Kearstin; Zamora, J. Lizbeth Reyes; Moncman, Carole L.; Popa, Andreea; Smith, Everett Clinton; Webb, Stacy R.; and Dutch, Rebecca Ellis, "Analysis of Hendra Virus Fusion Protein N-Terminal Transmembrane Residues" (2021). Molecular and Cellular Biochemistry Faculty Publications. 194.