scholarly journals Influenza Virus M2 Protein Mediates ESCRT-Independent Membrane Scission

Cell ◽  
2010 ◽  
Vol 142 (6) ◽  
pp. 902-913 ◽  
Author(s):  
Jeremy S. Rossman ◽  
Xianghong Jing ◽  
George P. Leser ◽  
Robert A. Lamb
2019 ◽  
Vol 517 (3) ◽  
pp. 507-512 ◽  
Author(s):  
Younghun Jung ◽  
Byoungjae Kong ◽  
Seokoh Moon ◽  
Seok-Hyeon Yu ◽  
Jinhyo Chung ◽  
...  

Vaccine ◽  
2009 ◽  
Vol 28 (2) ◽  
pp. 523-531 ◽  
Author(s):  
Pravina Kitikoon ◽  
Amy L. Vincent ◽  
Bruce H. Janke ◽  
B. Erickson ◽  
Erin L. Strait ◽  
...  

2014 ◽  
Vol 10 (3) ◽  
pp. 180-188 ◽  
Author(s):  
Marine E. Bozdaganyan ◽  
Philipp S. Orekhov ◽  
Nicola L. Bragazzi ◽  
Donatella Panatto ◽  
Daniela Amicizia ◽  
...  

2010 ◽  
Vol 7 (1) ◽  
pp. 89 ◽  
Author(s):  
Zhenhua Zhang ◽  
Yongqing Li ◽  
Shufang Xu ◽  
Fuyong Chen ◽  
Li Zhang ◽  
...  

1996 ◽  
Vol 133 (4) ◽  
pp. 733-747 ◽  
Author(s):  
T Sakaguchi ◽  
G P Leser ◽  
R A Lamb

High level expression of the M2 ion channel protein of influenza virus inhibits the rate of intracellular transport of the influenza virus hemagglutinin (HA) and that of other integral membrane glycoproteins. HA coexpressed with M2 is properly folded, is not associated with GRP78-BiP, and trimerizes with the same kinetics as when HA is expressed alone. Analysis of the rate of transport of HA from the ER to the cis and medial golgi compartments and the TGN indicated that transport through the Golgi apparatus is delayed. Uncleaved HA0 was not expressed at the cell surface, and accumulation HA at the plasma membrane was reduced to 75-80% of control cells. The delay in intracellular transport of HA on coexpression of M2 was not observed in the presence of the M2-specific ion channel blocker, amantadine, indicating that the Golgi transport delay is due to the M2 protein ion channel activity equilibrating pH between the Golgi lumen and the cytoplasm, and not due to saturation of the intracellular transport machinery. The Na+/H+ ionophore, monensin, which also equilibrates pH between the Golgi lumen and the cytoplasm, caused a similar inhibition of intracellular transport as M2 protein expression did for HA and other integral membrane glycoproteins. EM data showed a dilation of Golgi cisternae in cells expressing the M2 ion channel protein. Taken together, the data suggest a similarity of effects of M2 ion channel activity and monensin on intracellular transport through the Golgi apparatus.


2019 ◽  
Vol 47 (06) ◽  
pp. 1307-1324 ◽  
Author(s):  
Jang-Gi Choi ◽  
Heeeun Lee ◽  
Young Soo Kim ◽  
Youn-Hwan Hwang ◽  
You-Chang Oh ◽  
...  

Aloe vera ethanol extract (AVE) reportedly has significant anti-influenza virus activity, but its underlying mechanisms of action and constituents have not yet been completely elucidated. Previously, we have confirmed that AVE treatment significantly reduces the viral replication of green fluorescent protein-labeled influenza A virus in Madin-Darby canine kidney (MDCK) cells. In addition, post-treatment with AVE inhibited viral matrix protein 1 (M1), matrix protein 2 (M2), and hemagglutinin (HA) mRNA synthesis and viral protein (M1, M2, and HA) expressions. In this study, we demonstrated that AVE inhibited autophagy induced by influenza A virus in MDCK cells and also identified quercetin, catechin hydrate, and kaempferol as the active antiviral components of AVE. We also found that post-treatment with quercetin, catechin hydrate, and kaempferol markedly inhibited M2 viral mRNA synthesis and M2 protein expression. A docking simulation suggested that the binding affinity of quercetin, catechin hydrate, and kaempferol for the M2 protein may be higher than that of known M2 protein inhibitors. Thus, the inhibition of autophagy induced by influenza virus may explain the antiviral activity of AVE against H1N1 or H3N2. Aloe vera extract and its constituents may, therefore, be potentially useful for the development of anti-influenza agents.


1998 ◽  
Vol 273 (11) ◽  
pp. 6518-6524 ◽  
Author(s):  
Jennifer R. Henkel ◽  
Ora A. Weisz

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