期刊
VIRUSES-BASEL
卷 13, 期 12, 页码 -出版社
MDPI
DOI: 10.3390/v13122353
关键词
Hendra virus; fusion protein; transmembrane domain; membrane fusion
类别
资金
- NIH/NIAID [AI051517]
Hendra virus uses two surface glycoproteins to infect host cells, with the TM region of the F protein playing a key role in stability and fusion. Mutations at residues M491 and L492 have been shown to alter F protein function, indicating their involvement in the fusion process.
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 beta-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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