Asset Details
Do you wish to reserve the book?
Structure of mouse coronavirus spike protein complexed with receptor reveals mechanism for viral entry
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Structure of mouse coronavirus spike protein complexed with receptor reveals mechanism for viral entry
Do you wish to request the book?
Structure of mouse coronavirus spike protein complexed with receptor reveals mechanism for viral entry
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Structure of mouse coronavirus spike protein complexed with receptor reveals mechanism for viral entry
2020
Overview
Coronaviruses recognize a variety of receptors using different domains of their envelope-anchored spike protein. How these diverse receptor recognition patterns affect viral entry is unknown. Mouse hepatitis coronavirus (MHV) is the only known coronavirus that uses the N-terminal domain (NTD) of its spike to recognize a protein receptor, CEACAM1a. Here we determined the cryo-EM structure of MHV spike complexed with mouse CEACAM1a. The trimeric spike contains three receptor-binding S1 heads sitting on top of a trimeric membrane-fusion S2 stalk. Three receptor molecules bind to the sides of the spike trimer, where three NTDs are located. Receptor binding induces structural changes in the spike, weakening the interactions between S1 and S2. Using protease sensitivity and negative-stain EM analyses, we further showed that after protease treatment of the spike, receptor binding facilitated the dissociation of S1 from S2, allowing S2 to transition from pre-fusion to post-fusion conformation. Together these results reveal a new role of receptor binding in MHV entry: in addition to its well-characterized role in viral attachment to host cells, receptor binding also induces the conformational change of the spike and hence the fusion of viral and host membranes. Our study provides new mechanistic insight into coronavirus entry and highlights the diverse entry mechanisms used by different viruses.
Publisher
Public Library of Science,Public Library of Science (PLoS)
Subject
/ Animals
/ Binding
/ Carcinoembryonic Antigen - chemistry
/ Carcinoembryonic Antigen - metabolism
/ Carcinoembryonic Antigen - ultrastructure
/ COVID-19
/ Domains
/ Humans
/ Medicine and Health Sciences
/ Mice
/ Murine hepatitis virus - chemistry
/ Murine hepatitis virus - physiology
/ Protease
/ Protein Conformation, alpha-Helical
/ Proteins
/ Receptors, Virus - chemistry
/ Receptors, Virus - metabolism
/ Receptors, Virus - ultrastructure
/ Recombinant Proteins - chemistry
/ Recombinant Proteins - metabolism
/ Research and Analysis Methods
/ Spike Glycoprotein, Coronavirus - chemistry
/ Spike Glycoprotein, Coronavirus - metabolism
/ Spike Glycoprotein, Coronavirus - ultrastructure
/ Stains
/ Trimers
/ Viruses
