Disease relevance of Foot-and-Mouth Disease

• A DNA sequence coding for the immunogenic capsid protein VP3 of foot-and-mouth disease virus A12, prepared from the virion RNA, was ligated to a plasmid designed to express a chimeric protein from the Escherichia coli tryptophan promoter-operator system [1].
• Complete alanine scanning of intersubunit interfaces in a foot-and-mouth disease virus capsid reveals critical contributions of many side chains to particle stability and viral function [2].
• The demonstration of mutational changes in pX in 12 of 18 mutants suggests a role for this protein in determining the guanidine trait of poliovirus and corroborates studies with foot-and-mouth disease virus [3].
• Cleavage of eIF-4 gamma in human rhinoviruses and enteroviruses is carried out by the viral 2A proteinase; in aphthoviruses (i.e., foot-and-mouth disease viruses), the leader proteinase is responsible for this reaction [4].
• Swine inoculated with 10(9) PFU of a control Ad5 virus lacking the IFN gene and challenged 24 h later with FMDV developed typical signs of foot-and-mouth disease (FMD), including fever, vesicular lesions, and viremia [5].

High impact information on Foot-and-Mouth Disease

• Here, we report the X-ray structure of two complexes between foot-and-mouth disease virus 3D, VPg1, the substrate UTP and divalent cations, in the absence and in the presence of an oligoadenylate of 10 residues [6].
• Heparan sulfate has an important role in cell entry by foot-and-mouth disease virus (FMDV) [7].
• The foot-and-mouth disease virus encodes two forms of a cysteine proteinase (L protease) which bisects the eIF4G polypeptide into an N-terminal fragment containing the eIF4E binding site, and a C-terminal fragment which contains binding sites for eIF4A and eIF3 and which associates with the 40S ribosomal subunit [8].
• Structure of the major antigenic loop of foot-and-mouth disease virus complexed with a neutralizing antibody: direct involvement of the Arg-Gly-Asp motif in the interaction [9].
• We have cloned and sequenced the viral protein (VP1)-coding regions of two foot-and-mouth disease virus (FMDV) serotypes (C1 and A5) [10].

Chemical compound and disease context of Foot-and-Mouth Disease

• The foot and mouth disease virus, a picornavirus, encodes two forms of a cysteine proteinase (leader or L protease) that bisects the EIF4G polypeptide of the initiation factor complex eIF4F into N-terminal (Nt) and C-terminal (Ct) domains [11].
• N-acetyl-aziridine and a fluorescent alkylating agent, dansyl sulfonate aziridine, inactivated three different viruses, flock house virus, human rhinovirus-14, and foot and mouth disease virus [12].
• Lactose is tested as inducer of the main antigenic coat protein (VP1) of the foot and mouth disease (FMD) virus in a T7-RNA polymerase expression system [13].
• The conserved Arg-Gly-Asp (RGD) motif found in a hypervariable, mobile antigenic loop of foot-and-mouth disease virus (FMDV) is critically involved in virus attachment to cells by binding to an integrin, probably related to alphavbeta3 [14].
• The antigenic activity of a 19-mer peptide corresponding to the major antigenic region of foot-and-mouth disease virus and its retro-enantiomeric analogue was found to be completely abolished when they were tested in a biosensor system in trifluoroethanol [15].

Biological context of Foot-and-Mouth Disease

• The amino acid sequence Arg-Gly-Asp (RGD) is a highly conserved region located on the P1D protein of most sero- and subtypes of foot-and-mouth disease virus (FMDV)and participates in binding of FMDV to their target cells [16].
• The difficulty in cloning the foot-and-mouth disease virus cytidyl tract in Escherichia coli was circumvented by joining two separate cloned parts, representing the S and L fragments of the genome, and, in a second step, inserting a dC-dG homopolymer [17].
• A foot-and-mouth disease virus (FMDV) polymerase (3D) with amino acid replacements G118D, V239M and G373D (triple DMD mutant) was obtained from a molecular clone derived from a virus population treated with ribavirin, in the transition to error catastrophe (virus extinction through lethal mutagenesis) [18].
• Genetic heterogeneity in the foot-and-mouth disease virus Leader and 3C proteinases [19].
• The foot-and-mouth disease virus (FMDV) leader (L) proteinase is an important virulence determinant in FMDV infections [20].

Anatomical context of Foot-and-Mouth Disease

• Field isolates of foot-and-mouth disease virus (FMDV) have been shown to use the RGD-dependent integrin alphavbeta3 as a cellular receptor on cultured cells [21].
• The alpha(v)beta6 integrin receptor for Foot-and-mouth disease virus is expressed constitutively on the epithelial cells targeted in cattle [22].
• We have compared the efficiency of eIF4G cleavage in rabbit reticulocyte lysates during translation of mRNAs encoding the foot-and-mouth disease virus leader proteinase (Lpro) or the human rhinovirus 2Apro [23].
• Selection of T-cell epitopes from foot-and-mouth disease virus reflects the binding affinity to different cattle MHC class II molecules [24].
• The indirect technique of a micro-enzyme-labelled immunosorbent assay (MICROELISA) was standardized and found efficient in detecting the foot-and-mouth disease virus antigen in cell culture fluids, mice carcases and cattle tongue epithelium as well as the antibody titre of sera [25].

Gene context of Foot-and-Mouth Disease

• In agreement with previous publications, the HAV IRES is unique among all picornavirus IRESs in that it was inhibited if translation initiation factor eIF4G was cleaved by foot-and-mouth disease L-proteases [26].
• We have previously shown that replication of foot-and-mouth disease virus (FMDV) is highly sensitive to alpha/beta interferon (IFN-alpha/beta) [5].
• A recombinant, arginine-glycine-aspartic acid (RGD) motif from foot-and-mouth disease virus binds mammalian cells through vitronectin and, to a lower extent, fibronectin receptors [27].
• To ensure the equal expression of both subunits, we used the self-cleaving properties of the 2A oligopeptide from foot-and-mouth disease virus (FMDV) to express IL-12 as a single, long open reading frame (ORF) encoding p402Ap35 [28].
• A synthetic oligodeoxynucleotide corresponding to an antigenic determinant of the C-terminal part of the VP1 protein of foot-and-mouth disease virus was inserted into the phoE gene in an area corresponding to a cell surface-exposed region of the PhoE protein [29].

Analytical, diagnostic and therapeutic context of Foot-and-Mouth Disease

• Passage of foot-and-mouth disease virus (FMDV) in cell culture in the presence of the mutagenic base analog 5-fluorouracil or 5-azacytidine resulted in decreases of infectivity and occasional extinction of the virus [30].
• Sera from cattle vaccinated against either foot-and-mouth disease virus (FMDV) strains A10 Holland, O1 BFS, or C1 Detmold were tested in a serum neutralization test (SNT) and a liquid-phase blocking sandwich ELISA (LBE), and the titers were compared with the results of intradermolingual challenge tests [31].
• Foot-and-mouth disease. Challenge of cattle after multiple vaccinations [32].
• Use of short analytical ultracentrifugation runs for the isopycnic determination of foot-and-mouth disease virus concentration and density in autoformed caesium chloride gradients [33].
• Comparative quantification of foot-and-mouth disease virus (146 S antigen) by sucrose and potassium-bromide density gradient centrifugation [34].

References