Open AccessA Critical Domain of Ebolavirus Envelope Glycoprotein Determines Glycoform and Infectivity
Author(s) -
Haruhiko Fujihira,
Katsuaki Usami,
Keita Matsuno,
Hideyuki Takeuchi,
Kaori Denda-Nagai,
Yoshihiro Furukawa,
Yasuro Shinohara,
Ayato Takada,
Yoshihiro Kawaoka,
Tatsuro Irimura
Publication year - 2018
Publication title -
scientific reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.24
H-Index - 213
ISSN - 2045-2322
DOI - 10.1038/s41598-018-23357-8
Subject(s) - infectivity , ebolavirus , glycoprotein , virology , envelope (radar) , transmissibility (structural dynamics) , biology , domain (mathematical analysis) , computational biology , computer science , ebola virus , virus , physics , genetics , mathematics , telecommunications , mathematical analysis , radar , vibration isolation , quantum mechanics , vibration
Ebolaviruses comprises 5 species that exert varying degrees of mortality/infectivity in humans with Reston ebolaviruses (REBOV) showing the lowest and Zaire ebolaviruses (ZEBOV) showing the highest. However, the molecular basis of this differential mortality/infectivity remains unclear. Here, we report that the structural features of ebolavirus envelope glycoproteins (GPs) and one of their counter receptors, macrophage galactose-type calcium-type lectin (MGL/CD301), play crucial roles in determining viral infectivity. The low infectivity of REBOV mediated by the interaction between GPs and MGL/CD301 dramatically increased when the N-terminal 18 amino acids (33rd through 50th) of GPs were replaced with that of ZEBOV. Furthermore, structural analysis of glycans of GPs revealed that N -glycans were more extended in REBOV than in ZEBOV. N -glycan extension was reversed by the replacement of aforementioned N-terminal 18 amino acid residues. Therefore, these data strongly suggest that extended N -glycans on GPs reduce MGL/CD301-mediated viral infectivity by hindering the interaction between GPs and MGL/CD301 preferentially binds O -glycans.