Archived
This content is available here strictly for research, reference, and/or recordkeeping and as such it may not be fully accessible. If you work or study at University of Kentucky and would like to request an accessible version, please use the SensusAccess Document Converter.
Abstract
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.
Document Type
Article
Publication Date
11-24-2021
Digital Object Identifier (DOI)
https://doi.org/10.3390/v13122353
Funding Information
This research was funded by NIH/NIAID grant number AI051517 to R.E.D.
Related Content
Data is available upon request from the corresponding author.
Repository Citation
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.
https://uknowledge.uky.edu/biochem_facpub/194
Notes/Citation Information
Published in Viruses, v. 13, issue 12, 2353.
© 2021 by the authors. Licensee MDPI, Basel, Switzerland.
This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).