scholarly journals Relationship of the Antigenic Structure of Foot-and-Mouth Disease Virus to the Process of Infection

1971 ◽  
Vol 13 (1) ◽  
pp. 85-93 ◽  
Author(s):  
D. J. Rowlands ◽  
D. V. Sangar ◽  
F. Brown
Keyword(s):  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Antigenic Structure ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Relationship Of

scholarly journals Mapping of antigenic sites of foot-and-mouth disease virus serotype Asia 1 and relationships with sites described in other serotypes

2013 ◽  
Vol 94 (3) ◽  
pp. 559-569 ◽  
Author(s):  
Santina Grazioli ◽  
Francesca Fallacara ◽  
Emiliana Brocchi
Keyword(s):  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Antigenic Structure ◽  
Antigenic Sites ◽  
Fmdv Serotype ◽  
Fmdv Serotypes ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Serotype Asia 1

Knowledge of the antigenic structure of foot-and-mouth disease virus (FMDV) has relevance in the development of diagnostic assays, in the evaluation of the antigenic variability and in the selection of appropriate vaccine strains. Antigenic sites have been investigated only in FMDVs of serotypes O, A and C, while it would be valuable to extend studies also to other serotypes. This paper reports the identification of antigenic sites involved in virus neutralization in the FMDV serotype Asia 1 by using a new panel of mAbs and their relation with sites described in other serotypes is discussed. Out of 24 mAbs raised against the FMDV serotype Asia 1, 10 neutralize viral infectivity and were used to select FMDV mutants resistant to neutralization. On the basis of their reactivity profile with virus mutants, the 10 neutralizing mAbs were clustered in four groups corresponding to four independent antigenic sites. By comparing the amino acid sequence of the parental virus and of virus mutants, the amino acids crucial for the four sites were mapped at the following positions: VP1 140–142, VP2 67–79, VP3 58/59 and VP3 218. Three of the four neutralizing sites identified and mapped on FMDV serotype Asia 1 correspond structurally and functionally to analogous sites described in FMDV serotypes O, A and C, enforcing the evidence that these are dominant antigenic sites in the FMDV structure. The fourth site, located at the C terminus of VP3, is a new independent site, described for the first time in FMDV.

scholarly journals Diagnosis Based on 1D Gene Analysis of the Foot-And-Mouth Disease Virus

2020 ◽  
pp. 227-234
Author(s):  
Choe SunIl ◽  
Jin MyongIl ◽  
Hwang GwangJo ◽  
Choe KyongHo ◽  
IM MyongDok ◽  
...  
Keyword(s):  
Nucleotide Sequence ◽  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Viral Disease ◽  
Mouth Disease ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Relationship Of ◽  
Fmdv Type ◽  
Mutation Region

A foot and mouth disease (FMD) is an acute, febrile and high contagious viral disease in many cloven hoofed domestic animals and more than 70 wild ones, resulting in severe finantial loss throughout the world. Choosing the correct seeds for foot-and-mouth disease (FMD) is an important issue in protecting this disease, and it is urgently necessary to establish a plan for vaccination in areas affected by FMD and to protect new foot-and-mouth disease. The genetic diversity and antigenic diversity of foot-and-mouth disease virus (FMDV) make eradication through vaccination difficult. Variable antigenic types exist in different geographic areas, and research projects on existing antigenic types are necessary to select vaccine in such an environment. From this, in this paper, oligonucleotide primers for detection and Selecting Serotype of FMDV were newly designed and synthesized. In addition, the nucleotide sequence of the 1D gene was aligned, the mutation region was determined, and the homology and phylogenetic relationship of the nucleotide sequence were analyzed. The antigenicity of the FMDV type O strains in the Democratic People's Republic of Korea and the correspondence between them were examined. The neutralization reaction was used to examine antigenicity between FMDV to select waxy seeds. To prevent FMD through this primer design and experimental method, the nucleic acid of FMDV was amplified by RT-PCR. Then, the nucleotide sequence of the 1D gene corresponding to the virus VP1 protein was analyzed and compared to select a seed vaccine strain.

scholarly journals A Similar Pattern of Interaction for Different Antibodies with a Major Antigenic Site of Foot-and-Mouth Disease Virus: Implications for Intratypic Antigenic Variation

1998 ◽  
Vol 72 (1) ◽  
pp. 739-748 ◽  
Author(s):  
Nuria Verdaguer ◽  
Noemi Sevilla ◽  
Mari Luz Valero ◽  
David Stuart ◽  
Emiliana Brocchi ◽  
...  
Keyword(s):  
Disease Virus ◽  
Similar Pattern ◽  
Antigenic Variation ◽  
Antigenic Site ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Antigenic Peptide ◽  
Antigenic Structure ◽  
Mouth Disease Virus ◽  
Foot And Mouth

ABSTRACT The three-dimensional structures of the Fab fragment of a neutralizing antibody raised against a foot-and-mouth disease virus (FMDV) of serotype C1, alone and complexed to an antigenic peptide representing the major antigenic site A (G-H loop of VP1), have been determined. As previously seen in a complex of the same antigen with another antibody which recognizes a different epitope within antigenic site A, the receptor recognition motif Arg-Gly-Asp and some residues from an adjacent helix participate directly in the interaction with the complementarity-determining regions of the antibody. Remarkably, the structures of the two antibodies become more similar upon binding the peptide, and both undergo considerable induced fit to accommodate the peptide with a similar array of interactions. Furthermore, the pattern of reactivities of five additional antibodies with versions of the antigenic peptide bearing amino acid replacements suggests a similar pattern of interaction of antibodies raised against widely different antigens of serotype C. The results reinforce the occurrence of a defined antigenic structure at this mobile, exposed antigenic site and imply that intratypic antigenic variation of FMDV of serotype C is due to subtle structural differences that affect antibody recognition while preserving a functional structure for the receptor binding site.

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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