Antiviral effects of a thiol protease inhibitor on foot-and-mouth disease virus.

1992 ◽  
Vol 66 (12) ◽  
pp. 7168-7175 ◽  
Author(s):  
L G Kleina ◽  
M J Grubman
2010 ◽  
Vol 87 (3) ◽  
pp. 307-317 ◽  
Author(s):  
Su-Mi Kim ◽  
Kwang-Nyeong Lee ◽  
Su-Jung Lee ◽  
Young-Joon Ko ◽  
Hyang-Sim Lee ◽  
...  

2019 ◽  
Vol 118 ◽  
pp. 109305 ◽  
Author(s):  
Gong Mei-jiao ◽  
Li Shi-fang ◽  
Chang Yan-yan ◽  
Shao Jun-jun ◽  
Sun Yue-feng ◽  
...  

Author(s):  
S. S. Breese ◽  
H. L. Bachrach

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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