scholarly journals The Different Tactics of Foot-and-Mouth Disease Virus to Evade Innate Immunity

2018 ◽  
Vol 9 ◽  
Author(s):  
Gisselle N. Medina ◽  
Fayna Díaz-San Segundo ◽  
Carolina Stenfeldt ◽  
Jonathan Arzt ◽  
Teresa de los Santos
Keyword(s):  
Innate Immunity ◽  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Mouth Disease Virus ◽  
Foot And Mouth

scholarly journals Advances in Foot-and-Mouth Disease Virus Proteins Regulating Host Innate Immunity

2020 ◽  
Vol 11 ◽  
Author(s):  
Jiangling Peng ◽  
Jiamin Yi ◽  
Wenping Yang ◽  
Jingjing Ren ◽  
Yuan Wen ◽  
...  
Keyword(s):  
Innate Immunity ◽  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Host Innate Immunity ◽  
Virus Proteins

scholarly journals Basal Level p53 Suppresses Antiviral Immunity against Foot-and-Mouth Disease Virus

Viruses ◽  
2019 ◽  
Vol 11 (8) ◽  
pp. 727
Author(s):  
Zhang ◽  
Chen ◽  
Liu ◽  
Qi ◽  
Gao ◽  
...  
Keyword(s):  
Innate Immunity ◽  
Disease Virus ◽  
Knockout Mice ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Clear Cut ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Immune Related Genes ◽  
Fmdv Replication

Tumor suppressor protein p53 (p53) is a master transcription factor that plays key roles in cell cycle arrest, apoptosis, senescence, and metabolism, as well as regulation of innate immunity during virus infection. In order to facilitate their replication and spreading, viruses have evolved to manipulate p53 function through different strategies, with some requiring active p53 while others demand reduction/inhibition of p53 activity. However, there are no clear-cut reports about the roles of p53 during the infection of foot-and-mouth disease virus (FMDV), the causative agent of a highly contagious foot-and-mouth disease (FMD) of cloven-hoofed animals. Here we showed that p53 level was dynamically regulated during FMDV infection, being degraded at the early infection stage but recovered to the basal level at the late stage. Cells depleted of p53 showed inhibited FMDV replication and enhanced expression of the immune-related genes, whereas overexpression of p53 didn’t affect the viral replication. Viral challenge assay with p53 knockout mice obtained similar results, with viral load decreased, histopathological changes alleviated, and lifespan extended in the p53 knockout mice. Together, these data demonstrate that basal level p53 is required for efficient FMDV replication by suppressing the innate immunity.

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.

Sign in / Sign up

Export Citation Format

Share Document