scholarly journals How Influenza Virus Uses Host Cell Pathways during Uncoating

Cells ◽  
2021 ◽  
Vol 10 (7) ◽  
pp. 1722
Author(s):  
Etori Aguiar Moreira ◽  
Yohei Yamauchi ◽  
Patrick Matthias
Keyword(s):  
Host Cell ◽  
Conformational Changes ◽  
Viral Genome ◽  
Human Population ◽  
Influenza A ◽  
Virus Genome ◽  
Cell Entry ◽  
Infection Cycle ◽  
Late Endosomes ◽  
Host Cell Entry

Influenza is a zoonotic respiratory disease of major public health interest due to its pandemic potential, and a threat to animals and the human population. The influenza A virus genome consists of eight single-stranded RNA segments sequestered within a protein capsid and a lipid bilayer envelope. During host cell entry, cellular cues contribute to viral conformational changes that promote critical events such as fusion with late endosomes, capsid uncoating and viral genome release into the cytosol. In this focused review, we concisely describe the virus infection cycle and highlight the recent findings of host cell pathways and cytosolic proteins that assist influenza uncoating during host cell entry.

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

scholarly journals Molecular rationale for hantavirus neutralization by a reservoir host-derived monoclonal antibody

2020 ◽  
Author(s):  
Ilona Rissanen ◽  
Robert Stass ◽  
Stefanie A. Krumm ◽  
Jeffrey Seow ◽  
Ruben J.G. Hulswit ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Host Cell ◽  
Conformational Changes ◽  
Neutralizing Antibody ◽  
Crystallographic Analysis ◽  
Reservoir Host ◽  
Cell Entry ◽  
Cryo Electron Microscopy ◽  
Neutralizing Monoclonal Antibody ◽  
Host Cell Entry

AbstractThe intricate lattice of Gn and Gc glycoprotein spike complexes at the surface of hantaviruses facilitates host-cell entry and is the primary target of the neutralizing antibody-mediated immune response. Here, through study of a neutralizing monoclonal antibody (mAb 4G2) generated in a bank vole reservoir host following infection with Puumala virus (PUUV), we provide molecular-level insights into how antibody-mediated targeting of the hantaviral glycoprotein lattice effectively neutralizes the virus. Crystallographic analysis reveals that mAb 4G2 binds to a multi-domain site on Gc in the pre-fusion state, and that Fab binding is incompatible with the conformational changes of the Gc that are required for host cell entry. Cryo-electron microscopy of PUUV-like particles treated with Fab 4G2 demonstrates that the antibody binds to monomeric Gc at breaks in the Gn-Gc lattice, highlighting the immunological accessibility of Gc monomers on the mature hantavirus surface and the plastic nature of the higher-order lattice assembly. This work provides a structure-based blueprint for rationalizing antibody-mediated targeting of hantaviruses.

scholarly journals DESC1 and MSPL Activate Influenza A Viruses and Emerging Coronaviruses for Host Cell Entry

2014 ◽  
Vol 88 (20) ◽  
pp. 12087-12097 ◽  
Author(s):  
P. Zmora ◽  
P. Blazejewska ◽  
A.-S. Moldenhauer ◽  
K. Welsch ◽  
I. Nehlmeier ◽  
...  
Keyword(s):  
Host Cell ◽  
Influenza A ◽  
Cell Entry ◽  
Influenza A Viruses ◽  
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.

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