Abstract:
:Human parainfluenza virus type 3 (HPIV3) fuses the viral envelope with the host cell membrane through the concerted action of the fusion (F) protein and the hemagglutinin-neuraminidase (HN). Upon HN binding to sialic acid (SA), the F protein in a metastable prefusion form is activated to undergo a series of structural rearrangements into a stable postfusion form to actuate the fusion between membranes. Various domains of F protein of some other paramyxoviruses, including HPIV3, have been reported to be differently functional. However, it is not yet clear what roles HRB linker plays. To clarify the roles that HRB linker might play in the F-mediated membrane fusion process, here we examined the effects of mutations introduced into the HRB linker of HPIV3 F protein. Six Single amino acid mutants, three chimeric mutants, and one deletion mutant were obtained and analyzed for membrane fusion activity and cell surface expression. The results showed that the membrane fusion activity of mutants changed to varying degrees in comparison with wild-type (wt) F, and some mutants even forfeited fusogenicity absolutely. It is indicated that the HRB linker domain plays an important role in the F-mediated membrane fusion process.
journal_name
Virus Resjournal_title
Virus researchauthors
Liu Y,Xie W,Chi M,Wen H,Zhao L,Song Y,Liu N,Chi L,Wang Zdoi
10.1016/j.virusres.2019.197791subject
Has Abstractpub_date
2020-01-02 00:00:00pages
197791eissn
0168-1702issn
1872-7492pii
S0168-1702(19)30322-3journal_volume
275pub_type
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