Conformational Preferences of a Peptide Corresponding to the Major Antigenic Determinant of Foot-and- Mouth Disease Virus: Implications for Peptide-Vaccine Approaches

1997 ◽  
Vol 341 (2) ◽  
pp. 360-369 ◽  
Author(s):  
Gonzalo de Prat-Gay
Keyword(s):  
Disease Virus ◽  
Antigenic Determinant ◽  
Peptide Vaccine ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Conformational Preferences ◽  
Mouth Disease Virus ◽  
Foot And Mouth

Synthesis of fusion proteins with multiple copies of an antigenic determinant of foot-and-mouth disease virus antibodies

Gene ◽  
1986 ◽  
Vol 49 (2) ◽  
pp. 189-197 ◽  
Author(s):  
Martien P. Broekhuijsen ◽  
Ton Blom ◽  
Jenny van Rijn ◽  
Peter H. Pouwels ◽  
Eric A. Klasen ◽  
...  
Keyword(s):  
Disease Virus ◽  
Fusion Proteins ◽  
Antigenic Determinant ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Multiple Copies

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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