scholarly journals Induction of immature dendritic cell apoptosis by foot and mouth disease virus is an integrin receptor mediated event before viral infection

2007 ◽  
Vol 102 (4) ◽  
pp. 980-991 ◽  
Author(s):  
Huali Jin ◽  
Chong Xiao ◽  
Gan Zhao ◽  
Xiaogang Du ◽  
Yang Yu ◽  
...  
Keyword(s):  
Dendritic Cell ◽  
Viral Infection ◽  
Disease Virus ◽  
Cell Apoptosis ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Immature Dendritic Cell ◽  
Integrin Receptor ◽  
Mouth Disease Virus ◽  
Foot And Mouth

scholarly journals Susceptibility to viral infection is enhanced by stable expression of 3A or 3AB proteins from foot-and-mouth disease virus

Virology ◽  
2008 ◽  
Vol 380 (1) ◽  
pp. 34-45 ◽  
Author(s):  
María F. Rosas ◽  
Yuri A. Vieira ◽  
Raúl Postigo ◽  
Miguel A. Martín-Acebes ◽  
Rosario Armas-Portela ◽  
...  
Keyword(s):  
Viral Infection ◽  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Stable Expression ◽  
Mouth Disease Virus ◽  
Foot And Mouth

scholarly journals Plasmacytoid dendritic cell activation by foot-and-mouth disease virus requires immune complexes

2006 ◽  
Vol 36 (7) ◽  
pp. 1674-1683 ◽  
Author(s):  
Laurence Guzylack-Piriou ◽  
Fabio Bergamin ◽  
Markus Gerber ◽  
Kenneth C. McCullough ◽  
Artur Summerfield
Keyword(s):  
Dendritic Cell ◽  
Disease Virus ◽  
Immune Complexes ◽  
Cell Activation ◽  
Plasmacytoid Dendritic Cell ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Dendritic Cell Activation ◽  
Mouth Disease Virus ◽  
Foot And Mouth

scholarly journals The αvβ6 integrin receptor for Foot-and-mouth disease virus is expressed constitutively on the epithelial cells targeted in cattle

2005 ◽  
Vol 86 (10) ◽  
pp. 2769-2780 ◽  
Author(s):  
Paul Monaghan ◽  
Sarah Gold ◽  
Jennifer Simpson ◽  
Zhidong Zhang ◽  
Paul H. Weinreb ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Disease Virus ◽  
Cultured Cells ◽  
Natural Infection ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Integrin Receptors ◽  
Integrin Receptor ◽  
Mouth Disease Virus ◽  
Foot And Mouth

Field strains of Foot-and-mouth disease virus (FMDV) use a number of αv-integrins as receptors to initiate infection on cultured cells, and integrins are believed to be the receptors used to target epithelial cells in animals. In this study, immunofluorescence confocal microscopy and real-time RT-PCR were used to investigate expression of two of the integrin receptors of FMDV, αvβ6 and αvβ3, within various epithelia targeted by this virus in cattle. These studies show that αvβ6 is expressed constitutively on the surfaces of epithelial cells at sites where infectious lesions occur during a natural infection, but not at sites where lesions are not normally formed. Expression of αvβ6 protein at these sites showed a good correlation with the relative abundance of β6 mRNA. In contrast, αvβ3 protein was only detected at low levels on the vasculature and not on the epithelial cells of any of the tissues investigated. Together, these data suggest that in cattle, αvβ6, rather than αvβ3, serves as the major receptor that determines the tropism of FMDV for the epithelia normally targeted by this virus.

High resolution surface structure of foot-and-mouth disease virus

1978 ◽  
Vol 36 (2) ◽  
pp. 376-377
Author(s):  
S. S. Breese ◽  
H. L. Bachrach
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
Surface Structure ◽  
Disease Virus ◽  
Potassium Phosphate ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Physical Measurements ◽  
Mouth Disease Virus ◽  
Foot And Mouth

Models for the structure of foot-and-mouth disease virus (FMDV) have been proposed from chemical and physical measurements (Brown, et al., 1970; Talbot and Brown, 1972; Strohmaier and Adam, 1976) and from rotational image-enhancement electron microscopy (Breese, et al., 1965). In this report we examine the surface structure of FMDV particles by high resolution electron microscopy and compare it with that of particles in which the outermost capsid protein VP3 (ca. 30, 000 daltons) has been split into smaller segments, two of which VP3a and VP3b have molecular weights of about 15, 000 daltons (Bachrach, et al., 1975).Highly purified and concentrated type A12, strain 119 FMDV (5 mg/ml) was prepared as previously described (Bachrach, et al., 1964) and stored at 4°C in 0. 2 M KC1-0. 5 M potassium phosphate buffer at pH 7. 5. For electron microscopy, 1. 0 ml samples of purified virus and trypsin-treated virus were dialyzed at 4°C against 0. 2 M NH4OAC at pH 7. 3, deposited onto carbonized formvar-coated copper screens and stained with phosphotungstic acid, pH 7. 3.

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