Journal
CELL HOST & MICROBE
Volume 21, Issue 3, Pages 356-366Publisher
CELL PRESS
DOI: 10.1016/j.chom.2017.02.008
Keywords
-
Categories
Funding
- ECHO [711.011.006]
Ask authors/readers for more resources
Human beta1-coronavirus (beta 1CoV) OC43 emerged relatively recently through a single zoonotic introduction. Like relatedanimal beta 1CoVs, OC43 uses 9-O-acetylated sialic acid as receptor determinant. b1CoV receptor binding is typically controlled by attachment/fusion spike protein S and receptor-binding/receptor-destroying hemagglutinin-esterase protein HE. We show that following OC43's introduction into humans, HE-mediated receptor binding was selected against and ultimately lost through progressive accumulation ofmutations in the HE lectin domain. Consequently, virion-associated receptor-destroying activity toward multivalent glycoconjugates was reduced and altered such that some clustered receptor populations are no longer cleaved. Loss of HE lectin function was also observed for another respiratory human coronavirus, HKU1. This thus appears to be an adaptation to the sialoglycome of the human respiratory tract and for replication in human airways. The findings suggest that the dynamics of virion-glycan interactions contribute to host tropism. Our observations are relevant also to other human respiratory viruses of zoonotic origin, particularly influenza A virus.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available