Analysis of Hendra Virus Fusion Protein N-Terminal Transmembrane Residues.

Autor:	Barrett, Chelsea T., Neal, Hadley E., Edmonds, Kearstin, Zamora, J. Lizbeth Reyes, Moncman, Carole L., Popa, Andreea, Smith, Everett Clinton, Webb, Stacy R., Dutch, Rebecca Ellis
Předmět:	CHIMERIC proteins MEMBRANE proteins N-terminal residues MEMBRANE glycoproteins CARRIER proteins VIRAL envelope proteins VIRAL proteins HENDRA virus
Zdroj:	Viruses (1999-4915); Dec2021, Vol. 13 Issue 12, p2353-2353, 1p
Abstrakt:	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. [ABSTRACT FROM AUTHOR]
Databáze:	Complementary Index
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