Publication: Increased capsid oligomerization is deleterious to dengue virus particle production
Issued Date
2021-01-01
Resource Type
ISSN
14652099
00221317
00221317
Other identifier(s)
2-s2.0-85114100271
Rights
Mahidol University
Rights Holder(s)
SCOPUS
Bibliographic Citation
Journal of General Virology. Vol.102, No.8 (2021)
Suggested Citation
Sutha Sangiambut, Natcha Promphet, Suwipa Chaiyaloom, Chunya Puttikhunt, Panisadee Avirutnan, Watchara Kasinrerk, Nopporn Sittisombut, Prida Malasit Increased capsid oligomerization is deleterious to dengue virus particle production. Journal of General Virology. Vol.102, No.8 (2021). doi:10.1099/JGV.0.001635 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/77346
Research Projects
Organizational Units
Authors
Journal Issue
Thesis
Title
Increased capsid oligomerization is deleterious to dengue virus particle production
Abstract
The capsid protein (C) of dengue virus is required for viral infectivity as it packages viral RNA genome into infectious particles. C exists as a homodimer that forms via hydrophobic interactions between the α2 and α4 helices of monomers. To identify C region(s) important for virus particle production, a complementation system was employed in which single-round infectious particles are generated by trans-encapsidation of a viral C-deleted genome by recombinant C expressed in mosquito cells. Mutants harbouring a complete α3 deletion, or a dual Ile65-/Trp69-to-Ala substitution in the α3 helix, exhibited reduced production of infectious virus. Unexpectedly, higher proportions of oligomeric C were detected in cells expressing both mutated forms as compared with the wild-type counterpart, indicating that the α3 helix, through its internal hydrophobic residues, may down-modulate oligomerization of C during particle formation. Compared with wild-type C, the double Ile65-/Trp69 to Ala mutations appeared to hamper viral infectivity but not C and genomic RNA incorporation into the pseudo-infectious virus particles, suggesting that increased C oligomerization may impair DENV replication at the cell entry step.