scholarly journals Rapid and Efficient Cell-to-Cell Transmission of Avian Influenza H5N1 Virus in MDCK Cells Is Achieved by Trogocytosis

Pathogens ◽  
2021 ◽  
Vol 10 (4) ◽  
pp. 483
Author(s):  
Supasek Kongsomros ◽  
Suwimon Manopwisedjaroen ◽  
Jarinya Chaopreecha ◽  
Sheng-Fan Wang ◽  
Suparerk Borwornpinyo ◽  
...  

Viruses have developed direct cell-to-cell transfer strategies to enter target cells without being released to escape host immune responses and antiviral treatments. These strategies are more rapid and efficient than transmission through indirect mechanisms of viral infection between cells. Here, we demonstrate that an H5N1 influenza virus can spread via direct cell-to-cell transfer in Madin-Darby canine kidney (MDCK) cells. We compared cell-to-cell transmission of the H5N1 virus to that of a human influenza H1N1 virus. The H5N1 virus has been found to spread to recipient cells faster than the human influenza H1N1 virus. Additionally, we showed that plasma membrane exchange (trogocytosis) occurs between co-cultured infected donor cells and uninfected recipient cells early point, allowing the intercellular transfer of viral material to recipient cells. Notably, the H5N1 virus induced higher trogocytosis levels than the H1N1 virus, which could explain the faster cell-to-cell transmission rate of H5N1. Importantly, this phenomenon was also observed in A549 human lung epithelial cells, which are representative cells in the natural infection site. Altogether, our results provide evidence demonstrating that trogocytosis could be the additional mechanism utilized by the H5N1 virus for rapid and efficient cell-to-cell transmission.

1970 ◽  
Vol 7 (1) ◽  
pp. 75-79 ◽  
Author(s):  
F. W. Gay ◽  
J. K. Clarke ◽  
E. Dermott

2012 ◽  
Vol 44 (4) ◽  
pp. 297-307 ◽  
Author(s):  
Fawzi Rahmadiyan Zuhairi ◽  
◽  
Maharani Maharani ◽  
Marselina I. Tan ◽  

Physiology ◽  
2013 ◽  
Vol 28 (2) ◽  
pp. 93-116 ◽  
Author(s):  
Anastasia F. Thévenin ◽  
Tia J. Kowal ◽  
John T. Fong ◽  
Rachael M. Kells ◽  
Charles G. Fisher ◽  
...  

Gap junctions (GJs) are the only known cellular structures that allow a direct cell-to-cell transfer of signaling molecules by forming densely packed arrays or “plaques” of hydrophilic channels that bridge the apposing membranes of neighboring cells. The crucial role of GJ-mediated intercellular communication (GJIC) for all aspects of multicellular life, including coordination of development, tissue function, and cell homeostasis, has been well documented. Assembly and degradation of these membrane channels is a complex process that includes biosynthesis of the connexin (Cx) subunit proteins (innexins in invertebrates) on endoplasmic reticulum (ER) membranes, oligomerization of compatible subunits into hexameric hemichannels (connexons), delivery of the connexons to the plasma membrane (PM), head-on docking of compatible connexons in the extracellular space at distinct locations, arrangement of channels into dynamic spatially and temporally organized GJ channel plaques, as well as internalization of GJs into the cytoplasm followed by their degradation. Clearly, precise modulation of GJIC, biosynthesis, and degradation are crucial for accurate function, and much research currently addresses how these fundamental processes are regulated. Here, we review posttranslational protein modifications (e.g., phosphorylation and ubiquitination) and the binding of protein partners (e.g., the scaffolding protein ZO-1) known to regulate GJ biosynthesis, internalization, and degradation. We also look closely at the atomic resolution structure of a GJ channel, since the structure harbors vital cues relevant to GJ biosynthesis and turnover.


2014 ◽  
Vol 164 (5) ◽  
pp. 359-365 ◽  
Author(s):  
Venugopal Thayanithy ◽  
Elizabeth L. Dickson ◽  
Clifford Steer ◽  
Subbaya Subramanian ◽  
Emil Lou

2004 ◽  
Vol 199 (2) ◽  
pp. 283-293 ◽  
Author(s):  
Clare Jolly ◽  
Kirk Kashefi ◽  
Michael Hollinshead ◽  
Quentin J. Sattentau

Direct cell–cell transfer is an efficient mechanism of viral dissemination within an infected host, and human immunodeficiency virus 1 (HIV-1) can exploit this mode of spread. Receptor recognition by HIV-1 occurs via interactions between the viral surface envelope glycoprotein (Env), gp120, and CD4 and a chemokine receptor, CCR5 or CXCR4. Here, we demonstrate that the binding of CXCR4-using HIV-1–infected effector T cells to primary CD4+/CXCR4+ target T cells results in rapid recruitment to the interface of CD4, CXCR4, talin, and lymphocyte function–associated antigen 1 on the target cell, and of Env and Gag on the effector cell. Recruitment of these membrane molecules into polarized clusters was dependent on Env engagement of CD4 and CXCR4 and required remodelling of the actin cytoskeleton. Transfer of Gag from effector to target cell was observed by 1 h after conjugate formation, was independent of cell–cell fusion, and was probably mediated by directed virion fusion with the target cell. We propose that receptor engagement by Env directs the rapid, actin-dependent recruitment of HIV receptors and adhesion molecules to the interface, resulting in a stable adhesive junction across which HIV infects the target cell.


Cell Reports ◽  
2021 ◽  
Vol 35 (10) ◽  
pp. 109189
Author(s):  
Eleanna Kara ◽  
Alessandro Crimi ◽  
Anne Wiedmer ◽  
Marc Emmenegger ◽  
Claudia Manzoni ◽  
...  

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