Engaging the spikes: heparan sulfate facilitates SARS-CoV-2 spike protein binding to ACE2 and potentiates viral infection
Rajkumar Singh Kalra, Ramesh Kandimalla
Abstract
In a recent report published in Cell, Clausen et al. Molecular analysis identified that HS interacts with the receptor-binding domain (RBD) at the S1 subunit of the SARS-CoV-2 trimeric S-protein, which facilitates the opening of S-protein conformation for ACE2 binding. Ongoing COVID-19, caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has overly strained the global healthcare system with overwhelmed infectivity and incessant mortalities. Consorted efforts are globally being made to understand the mechanism for SARS-CoV-2 infection in the host to clinically intervene in the SARS-CoV-2 infection and its ever-evolving spread.
Topics & Concepts
Heparan sulfateCoronavirusGlycoproteinAngiotensin-converting enzyme 2VirologyInfectivityViral entryPlasma protein bindingBiologySevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2)Protein subunitReceptorBinding siteCell biologyCellChemistryCoronavirus disease 2019 (COVID-19)VirusBiochemistryMedicineViral replicationGeneDiseaseInfectious disease (medical specialty)PathologySARS-CoV-2 and COVID-19 ResearchCOVID-19 Clinical Research StudiesVenomous Animal Envenomation and Studies