scholarly journals A dual-receptor mechanism between integrins and ACE2 widens SARS-CoV-2 tissue tropism

2022 ◽  
Author(s):  
Danielle Nader ◽  
Timothy E Gressett ◽  
Md Lokman Hossen ◽  
Prem P Chapagain ◽  
Steven W. Kerrigan ◽  
...  
Keyword(s):  
Host Cell ◽  
Cell Entry ◽  
Tissue Tropism ◽  
Signalling Cascades ◽  
Host Cell Entry

In addition to the ACE2 receptor, SARS-CoV-2 binds to integrins to gain host cell entry and trigger pro-inflammatory integrin-mediated signalling cascades. Integrins, therefore, are likely candidates for a dual-receptor mechanism with ACE2 to explain the increased infectivity seen in SARS-CoV-2 models. As integrins are primarily expressed in vasculature and persistent vasculopathy is seen in COVID-19, examining the role of endothelial integrin involvement is crucial in uncovering the pathophysiology of SARS-CoV-2.

scholarly journals Viral Traits and Cellular Knock-Out Genotype Affect Dependence of BVDV on Bovine CD46

Pathogens ◽  
2021 ◽  
Vol 10 (12) ◽  
pp. 1620
Author(s):  
Hann-Wei Chen ◽  
Verena Huber ◽  
Kati Szakmary-Braendle ◽  
Kerstin Seitz ◽  
Marlene Moetz ◽  
...  
Keyword(s):  
Host Cell ◽  
Clonal Selection ◽  
High Variability ◽  
Cell Entry ◽  
Knock Out ◽  
Virus Susceptibility ◽  
Host Cell Entry ◽  
Reported Data ◽  
Selection Of

The role of bovine CD46 in the host cell entry of BVDV has been established for more than a decade. By generating novel MDBK CD46 knock-out clones, we confirm previously reported data on the CD46 motives important for BVDV binding and the importance of the G479R exchange within BVDV Erns to gain independence of bovine CD46 during entry. The comparison of different knock-out genotypes revealed a high variability of cellular susceptibility for a BVDV encoding the G479R exchange. These data highlight the effect of clonal selection of knock-outs on virus susceptibility, which should be considered when planning knock-out experiments.

scholarly journals A structure-based rationale for sialic acid independent host-cell entry of Sosuga virus

2019 ◽  
Vol 116 (43) ◽  
pp. 21514-21520 ◽  
Author(s):  
Alice J. Stelfox ◽  
Thomas A. Bowden
Keyword(s):  
Sialic Acid ◽  
Host Cell ◽  
Receptor Binding ◽  
Cell Attachment ◽  
Cell Entry ◽  
Head Region ◽  
Close Proximity ◽  
Host Cell Attachment ◽  
Host Cell Entry

The bat-borne paramyxovirus, Sosuga virus (SosV), is one of many paramyxoviruses recently identified and classified within the newly established genus Pararubulavirus, family Paramyxoviridae. The envelope surface of SosV presents a receptor-binding protein (RBP), SosV-RBP, which facilitates host-cell attachment and entry. Unlike closely related hemagglutinin neuraminidase RBPs from other genera of the Paramyxoviridae, SosV-RBP and other pararubulavirus RBPs lack many of the stringently conserved residues required for sialic acid recognition and hydrolysis. We determined the crystal structure of the globular head region of SosV-RBP, revealing that while the glycoprotein presents a classical paramyxoviral six-bladed β-propeller fold and structurally classifies in close proximity to paramyxoviral RBPs with hemagglutinin-neuraminidase (HN) functionality, it presents a receptor-binding face incongruent with sialic acid recognition. Hemadsorption and neuraminidase activity analysis confirms the limited capacity of SosV-RBP to interact with sialic acid in vitro and indicates that SosV-RBP undergoes a nonclassical route of host-cell entry. The close overall structural conservation of SosV-RBP with other classical HN RBPs supports a model by which pararubulaviruses only recently diverged from sialic acid binding functionality.

Influenza A virus uses the aggresome processing machinery for host cell entry

Science ◽  
2014 ◽  
Vol 346 (6208) ◽  
pp. 473-477 ◽  
Author(s):  
Indranil Banerjee ◽  
Yasuyuki Miyake ◽  
Samuel Philip Nobs ◽  
Christoph Schneider ◽  
Peter Horvath ◽  
...  
Keyword(s):  
Host Cell ◽  
Influenza A Virus ◽  
Influenza A ◽  
Cell Entry ◽  
Processing Machinery ◽  
Host Cell Entry
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