Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2020 Jun 23;11:1480. doi: 10.3389/fimmu.2020.01480

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

Copyright © 2020 Morniroli, Giannì, Consales, Pietrasanta and Mosca.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

PMC Copyright notice

(A) Sialic acid recognition as an infection facilitator for Coronavirus strains. (1) MERS-CoV binds to non-acetylated sialoside receptors on the epithelial cells of the respiratory tract, promoting clustering and facilitating its binding to its receptor DPP4. (2) SARS-CoV binds to ACE2 receptor. (3) SARS-CoV-2 binds to ACE2 receptor, but a surface region in Spike protein is very similar to MERS-CoV spike sialic acid-binding region, suggesting a possible role of sialic acid recognition in infection initiation. (B) Sialic acid recognition as a host defense mechanism for Coronavirus strains. (1) MERS-CoV can bind to sialylated O-linked glycans covering mucins on mucosal cell surfaces, thus being trapped in the mucous layer and consequently eliminated through ciliary movement. (2) SARS-CoV passes through the mucous layer without being stopped by decoy alternative binding sites. (3) SARS-CoV-2 shares with MERS-CoV the sialic acid binding region of Spike protein, and could therefore bind to sialylated O-linked glycans similarly to MERS-CoV, thus possibly being eliminated through ciliary movement.