Development of high-affinity single chain Fv against foot-and-mouth disease virus

2016 ◽  
Vol 84 ◽  
pp. 50-55 ◽  
Author(s):  
Joon-Goo Jung ◽  
Gu Min Jeong ◽  
Sung Sun Yim ◽  
Ki Jun Jeong
Keyword(s):  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Single Chain ◽  
High Affinity ◽  
Single Chain Fv ◽  
Mouth Disease Virus ◽  
Foot And Mouth

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

Foot-and-mouth disease virus is a ligand for the high-affinity binding conformation of integrin α5β1: influence of the leucine residue within the RGDL motif on selectivity of integrin binding

Microbiology ◽  
2000 ◽  
Vol 81 (5) ◽  
pp. 1383-1391 ◽  
Author(s):  
Terry Jackson ◽  
Wendy Blakemore ◽  
John W. I. Newman ◽  
Nick J. Knowles ◽  
A. Paul Mould ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Disease Virus ◽  
Heparan Sulphate ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Binding Potential ◽  
Integrin Α5β1 ◽  
High Affinity ◽  
Mouth Disease Virus ◽  
Foot And Mouth

Field isolates of foot-and-mouth disease virus (FMDV) use RGD-dependent integrins as receptors for internalization, whereas strains that are adapted for growth in cultured cell lines appear to be able to use alternative receptors like heparan sulphate proteoglycans (HSPG). The ligand-binding potential of integrins is regulated by changes in the conformation of their ectodomains and the ligand-binding state would be expected to be an important determinant of tropism for viruses that use integrins as cellular receptors. Currently, αvβ3 is the only integrin that has been shown to act as a receptor for FMDV. In this study, a solid-phase receptor-binding assay has been used to characterize the binding of FMDV to purified preparations of the human integrin α5β1, in the absence of HSPG and other RGD-binding integrins. In this assay, binding of FMDV resembled authentic ligand binding to α5β1 in its dependence on divalent cations and specific inhibition by RGD peptides. Most importantly, binding was found to be critically dependent on the conformation of the integrin, as virus bound only after induction of the high-affinity ligand-binding state. In addition, the identity of the amino acid residue immediately following the RGD motif is shown to influence differentially the ability of FMDV to bind integrins α5β1 and αvβ3 and evidence is provided that α5β1 might be an important FMDV receptor in vivo.

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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