Cryo-EM analysis of the HCoV-229E spike glycoprotein reveals dynamic prefusion conformational changes.
Nat Commun
; 12(1): 141, 2021 01 08.
Article
in English
| MEDLINE | ID: covidwho-1387322
ABSTRACT
Coronaviruses spike (S) glycoproteins mediate viral entry into host cells by binding to host receptors. However, how the S1 subunit undergoes conformational changes for receptor recognition has not been elucidated in Alphacoronavirus. Here, we report the cryo-EM structures of the HCoV-229E S trimer in prefusion state with two conformations. The activated conformation may pose the potential exposure of the S1-RBDs by decreasing of the interaction area between the S1-RBDs and the surrounding S1-NTDs and S1-RBDs compared to the closed conformation. Furthermore, structural comparison of our structures with the previously reported HCoV-229E S structure showed that the S trimers trended to open the S2 subunit from the closed conformation to open conformation, which could promote the transition from pre- to postfusion. Our results provide insights into the mechanisms involved in S glycoprotein-mediated Alphacoronavirus entry and have implications for vaccine and therapeutic antibody design.
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Main subject:
CD13 Antigens
/
Coronavirus 229E, Human
/
Virus Internalization
/
Spike Glycoprotein, Coronavirus
Topics:
Vaccines
Limits:
Humans
Language:
English
Journal:
Nat Commun
Journal subject:
Biology
/
Science
Year:
2021
Document Type:
Article
Affiliation country:
S41467-020-20401-Y
Similar
MEDLINE
...
LILACS
LIS