scholarly journals Engineering a Single-Chain Fv Antibody to αvβ6 Integrin Using the Specificity-Determining Loop of a Foot-and-Mouth Disease Virus

2008 ◽  
Vol 382 (2) ◽  
pp. 385-401 ◽  
Author(s):  
Heide Kogelberg ◽  
Berend Tolner ◽  
Gareth J. Thomas ◽  
Danielle Di Cara ◽  
Shane Minogue ◽  
...  
Keyword(s):  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Single Chain ◽  
Single Chain Fv ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Fv Antibody ◽  
Αvβ6 Integrin ◽  
Single Chain Fv Antibody

scholarly journals Mapping of antigenic determinants on a SAT2 foot-and-mouth disease virus using chicken single-chain antibody fragments

2012 ◽  
Vol 167 (2) ◽  
pp. 370-379 ◽  
Author(s):  
Pamela A. Opperman ◽  
Francois F. Maree ◽  
Wouter Van Wyngaardt ◽  
Wilna Vosloo ◽  
Jacques Theron
Keyword(s):  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Antibody Fragments ◽  
Mouth Disease ◽  
Antigenic Determinants ◽  
Single Chain ◽  
Single Chain Antibody ◽  
Mouth Disease Virus ◽  
Foot And Mouth

scholarly journals Rules of engagement between αvβ6 integrin and foot-and-mouth disease virus

2017 ◽  
Vol 8 (1) ◽  
Author(s):  
Abhay Kotecha ◽  
Quan Wang ◽  
Xianchi Dong ◽  
Serban L. Ilca ◽  
Marina Ondiviela ◽  
...  
Keyword(s):  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Αvβ6 Integrin

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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