Asset Details
Do you wish to reserve the book?
Functional analysis of polymorphisms at the S1/S2 site of SARS-CoV-2 spike protein
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?
Functional analysis of polymorphisms at the S1/S2 site of SARS-CoV-2 spike protein
Do you wish to request the book?
Functional analysis of polymorphisms at the S1/S2 site of SARS-CoV-2 spike protein
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
Functional analysis of polymorphisms at the S1/S2 site of SARS-CoV-2 spike protein
2022
Overview
Several SARS-CoV-2 variants emerged that harbor mutations in the surface unit of the viral spike (S) protein that enhance infectivity and transmissibility. Here, we analyzed whether ten naturally-occurring mutations found within the extended loop harboring the S1/S2 cleavage site of the S protein, a determinant of SARS-CoV-2 cell tropism and pathogenicity, impact S protein processing and function. None of the mutations increased but several decreased S protein cleavage at the S1/S2 site, including S686G and P681H, the latter of which is found in variants of concern B.1.1.7 (Alpha variant) and B.1.1.529 (Omicron variant). None of the mutations reduced ACE2 binding and cell-cell fusion although several modulated the efficiency of host cell entry. The effects of mutation S686G on viral entry were cell-type dependent and could be linked to the availability of cathepsin L for S protein activation. These results show that polymorphisms at the S1/S2 site can modulate S protein processing and host cell entry.
Publisher
Public Library of Science,Public Library of Science (PLoS)
Subject
/ Analysis
/ Angiotensin-converting enzyme 2
/ Animals
/ Cleavage
/ COVID-19
/ Humans
/ Medicine and health sciences
/ Mutation
/ Plasmids
/ Polymorphism, Genetic - genetics
/ Proteins
/ Research and analysis methods
/ RNA
/ Severe acute respiratory syndrome
/ Severe acute respiratory syndrome coronavirus 2
/ Spike Glycoprotein, Coronavirus - genetics
/ Tropism
/ Viruses
