Influence of Serum Restriction on Foot-and-Mouth Disease Virus Infections in Cell Cultures II. Altered Viral Replication

2010 ◽  
Vol 22 (4) ◽  
pp. 295-301 ◽  
Author(s):  
Max Brugh
Keyword(s):  
Viral Replication ◽  
Disease Virus ◽  
Cell Cultures ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Virus Infections ◽  
Mouth Disease Virus ◽  
Foot And Mouth

scholarly journals Foot-and-mouth disease virus utilizes an autophagic pathway during viral replication

Virology ◽  
2011 ◽  
Vol 410 (1) ◽  
pp. 142-150 ◽  
Author(s):  
Vivian O'Donnell ◽  
Juan M. Pacheco ◽  
Michael LaRocco ◽  
Tom Burrage ◽  
William Jackson ◽  
...  
Keyword(s):  
Viral Replication ◽  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Mouth Disease Virus ◽  
Foot And Mouth

scholarly journals The Ability of Integrin αvβ3 To Function as a Receptor for Foot-and-Mouth Disease Virus Is Not Dependent on the Presence of Complete Subunit Cytoplasmic Domains

2001 ◽  
Vol 75 (1) ◽  
pp. 527-532 ◽  
Author(s):  
Sherry Neff ◽  
Barry Baxt
Keyword(s):  
Viral Replication ◽  
Disease Virus ◽  
High Efficiency ◽  
Cultured Cells ◽  
Foot And Mouth Disease ◽  
Integrin Αvβ3 ◽  
Mouth Disease ◽  
Cytoplasmic Domains ◽  
Mouth Disease Virus ◽  
Foot And Mouth

ABSTRACT The integrin αvβ3 has been shown to function as one of the integrin receptors on cultured cells for foot-and-mouth disease virus (FMDV), and high-efficiency utilization of the bovine homolog of this integrin is dependent on the cysteine-rich repeat region of the bovine β3 subunit. In this study we have examined the role of the cytoplasmic domains of the αv and β3 subunits in FMDV infection. We have found that truncations or extensions of these domains of either subunit, including deletions removing almost all of the cytoplasmic domains, had little or no effect on the ability of the integrin to function as a receptor for FMDV. The lysosomotropic agent monensin inhibited viral replication in cells transfected with either intact or cytoplasmic domain-truncated αvβ3. In addition, viral replication in transfected cells was inhibited by an αvβ3 function-blocking antibody but not by function-blocking antibodies to three other RGD-directed integrins, suggesting that these integrins are not involved in the infectious process. These results indicate that alterations to the cytoplasmic domains of either subunit, which lead to the inability of the integrin receptor to function normally, do not abolish the ability of the integrin to bind and internalize this viral ligand.

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