scholarly journals Ebola virus host cell entry

Uirusu ◽  
2015 ◽  
Vol 65 (1) ◽  
pp. 71-82 ◽  
Author(s):  
Yasuteru SAKURAI
Keyword(s):  
Host Cell ◽  
Ebola Virus ◽  
Cell Entry ◽  
Host Cell Entry

scholarly journals Two-pore channels control Ebola virus host cell entry and are drug targets for disease treatment

Science ◽  
2015 ◽  
Vol 347 (6225) ◽  
pp. 995-998 ◽  
Author(s):  
Yasuteru Sakurai ◽  
Andrey A. Kolokoltsov ◽  
Cheng-Chang Chen ◽  
Michael W. Tidwell ◽  
William E. Bauta ◽  
...  
Keyword(s):  
Host Cell ◽  
Drug Targets ◽  
Ebola Virus ◽  
Cell Entry ◽  
Disease Treatment ◽  
Host Cell Entry

scholarly journals Comparative Analysis of Host Cell Entry of Ebola Virus From Sierra Leone, 2014, and Zaire, 1976

2015 ◽  
Vol 212 (suppl 2) ◽  
pp. S172-S180 ◽  
Author(s):  
Heike Hofmann-Winkler ◽  
Kerstin Gnirß ◽  
Florian Wrensch ◽  
Stefan Pöhlmann
Keyword(s):  
Comparative Analysis ◽  
Host Cell ◽  
Sierra Leone ◽  
Ebola Virus ◽  
Cell Entry ◽  
Host Cell Entry

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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