[The infectious ribonucleic acid of foot-and-mouth disease virus].
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Animals↗
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Multiple proteases in foot-and-mouth disease virus replication.
Translation of foot-and-mouth disease virus RNA in a rabbit reticulocyte lysate for short time intervals resulted in the production of the peptides P20a , P16, and P88 (Lab, Lb, and P1) (R. R. Rueckert , Recommendations of the 3rd European Study Group on Molecular Biology of Picornavirus, Urbino , Italy, 1983). If further translation was prevented, the structural protein precursor P88 was not cleaved, even after prolonged incubation. This result indicates that the mechanism of the cleavage between P20a -P16 and P88 and of that between P88 and P52 (P2) differs from the mechanism of the secondary cleavages which produce the structural proteins. Furthermore, treatment of foot-and-mouth disease virus-infected cells with the protease inhibitor D-valyl phenylalanyl lysyl chloromethyl ketone prevented the in vivo cleavage between P20a -P16 and P88 but had no effect on any of the other cleavage events. These results suggest that the cleavage of the foot-and-mouth disease virus polyprotein utilizes two different host proteases.
Animals↗
[Vaccination against foot and mouth disease: current state and perspectives].
Foot-and-mouth disease (FMD) is endemic in many parts of the world and poses a permanent threat for cloven-hoofed animals in all countries. The available vaccines against FMD are safe and efficacious. Combat of FMD by vaccination is controversial in currently FMD-free countries including the ones of the European Union. The article summarizes our knowledge concerning production and use of vaccines, virus persistence, differentiation between vaccinated and infected animals, vaccination programs and perspectives of vaccine development.
Animals↗
Serological probes for some foot-and-mouth disease virus nonstructural proteins.
Foot-and-mouth disease virus (FMDV) O1 Kaufbeuren-specific cDNA fragments were subcloned into the E. coli expression vector pRIT.2T. Fusion proteins thus produced in bacteria were purified by affinity chromatography and inoculated into rabbits. Three sera thus obtained were found to be monospecific for FMDV proteins 3A, 3C, and 3D, respectively. Two others were prevalently directed against protein 2C, but in addition, either to protein 2B or to protein 3A. Five out of six mature nonstructural virus proteins can therefore be separately investigated in FMDV-infected cells, either by indirect immunofluorescence or by radioimmunoprecipitation. Immunofluorescence shows all investigated proteins to be located exclusively in the cytoplasm. One of them, protein 2C, transiently forms aggregates at the periphery of cells. Radioimmunoprecipitation confirmed current knowledge on maturation of FMDV proteins. It was further used to characterize postinfectional sera with regard to FMDV-specific antibodies. Cattle and guinea pig were found to have responded differently to FMDV nonstructural antigens. Furthermore, antigenicity of yet to be described FMDV polypeptides was observed in the guinea pig.
Animals↗
Serial passage in tissue culture of mixed foot-and-mouth disease virus serotypes.
The foot-and-mouth disease (FMD) virus field specimen SAU/8/88 was previously shown to consist of a mixture of O and Asia 1 serotypes [15]. In this study, plaques representing the O and Asia 1 components isolated from the original epithelial virus suspension were used to construct mixtures of known ratios, and these were serially passaged in tissue culture. After each passage, the ratio of O to Asia 1 virus was calculated. The two virus populations were shown to be cycling through time. This cycling phenomenon has not been described before for FMD virus in tissue culture, but is consistent with current population theory.
Animals↗
Function of minor polypeptides in foot-and-mouth disease virus and poliovirus.
Foot-and-mouth disease virus and poliovirus each contain several minor polypeptides, in addition to the four structural proteins. One of these, the viral RNA polymerase, can also act as a nuclease, hydrolysing the RNA and thus destroying viral infectivity. It is tightly bound to the RNA and may be the packaging signal for assembly of the particle.
Aphthovirus↗
Identification of amino acid and nucleotide sequence of the foot-and-mouth disease virus RNA polymerase.
Foot-and-mouth disease virus (FMDV) RNA polymerase was purified from the polyethylene glycol (PEG)-treated supernatant of infected cell media by a combination of ion-exchange chromatography, membrane molecular filtration, and affinity chromatography. The purified RNA polymerase which migrated as a single band of 56,000 molecular weight on a polyacrylamide gel was subjected to automated Edman degradation and the sequence of the first 30 amino acid residues established. On the basis of previous evidence, which indicated that the RNA polymerase was the most 3'-translated polypeptide, plasmids containing cDNA mapping at the 3' end of the genome were characterized by restriction enzyme analysis and nucleotide sequencing. These investigations definitively established the derived amino acid sequence by confirmation of 28 of the amino terminal residues determined by amino acid sequence analysis; the location of the FMDV RNA polymerase coding region at the extreme 3' end of the genome, 96 nucleotides from the poly(A) tail; and the N-terminal cleavage point of the RNA polymerase from its precursor P100 was found to be a glutamic acid-glycine bond.
Amino Acid Sequence↗
Structure of a major immunogenic site on foot-and-mouth disease virus.
Attachment of foot-and-mouth disease virus (FMDV) to its cellular receptor involves a long and highly antigenic loop containing the conserved sequence, Arg-Gly-Asp, a motif known to be a recognition element in many integrin-dependent cell adhesion processes. In our original crystal structure of FMDV the Arg-Gly-Asp-containing loop ('the loop'), located between beta-strands G and H of capsid protein VP1, was disordered and hence essentially invisible. We previously surmised that its disorder is enhanced by a disulphide bond linking the base of the loop (Cys 134) to Cys 130 of VP2 (ref. 8). We report here the crystal structure of the virus in which this disulphide is reduced. Reduced virus retains infectivity and serological experiments suggest that some of the loop's internal structure is conserved. But here its structure has become sufficiently ordered to allow us to describe an unambiguous conformation, which we relate to some key biological properties of the virus.
Aphthovirus↗
The location of the ploy(C) tract in the RNA of foot-and-mouth disease virus.
Fragments of foot-and-mouth disease virus RNA of decreasing size, containing the 3' poly(A) sequence have been prepared by alkali treatment and sucrose gradient centrifugation followed by oligo(dT)-cellulose affinity chromatography. Polyacrylamide gel electrophoresis of the ribonuclease T1 resistant oligonucleotides from these polyadenylated fragments has enabled us to locate the position of some of the longer oligonucleotides on the RNA. In particular the poly C tract has been shown to be near the 5' end of the RNA; The possible function of the poly(C) tract is discussed in the light of these findings.
Aphthovirus↗
An extended genetic recombination map for foot-and-mouth diseases virus.
The original foot-and-mouth diseases virus recombination map (Lake, Priston & Slade, 1975), which include 35 mutagen-induced ts mutants, has been extended both in detail and size by the mapping of a further 33 ts mutants (9 mutagen-induced and 24 spontaneous). The size increase from 0.57% to 3.27% maximum recombination fequency was principally due to the use of a new standardization technique for recombination fequencies but, in addition, the original map distance was increased by approx. 30% due to the mapping of new mutations. As in the original map, there was a marked concentration of mutations near the guanidine (gs) locus, i.e. 83% of the mutants had mutations in the third of the map adjacent to the gs locus.
Aphthovirus↗
Isolation and characterization of trypsin-resistant O1 variants of foot-and-mouth disease virus.
Strains of foot-and-mouth disease virus of types O1 and A10 were isolated which showed no significant loss of infectivity upon trypsinization. These 'trypsin-resistant' (TR) viruses were obtained by serial passage in BHK cells of virus that was trypsin-treated before inoculation of the cells. Three O1 isolates were cloned and studied further. Cell attachment of those TR O1 variants (OTR1) was not reduced by trypsinization, unlike that of parent virus. The polypeptide compositions of TR viruses as determined by SDS-polyacrylamide gel electrophoresis were identical with those of parent virus, with the exception of OTR1 which contained an additional polypeptide approx, 3000 daltons larger than VP1. After trypsinization, which normally cleaves VP1, the polypeptide composition of the three TR viruses (including OTR1) and of parent virus did not show any significant difference. In OTR1 both the additional virus protein and VP1 were cleaved into a P18 molecule and smaller fragments. The surface location of this additional polypeptide was confirmed by iodination experiments. It was shown by immunodiffusion experiments that only OTR1 differed from the parent virus. This antigenic change was present on the trypsin-sensitive part of the virus since trypsinized TR viruses (including OTR1) were antigenically identical to trypsinized parent virus. The electrophoretic mobilities of the three OTR viruses isolated, and of parent virus, differed somewhat before trypsinization. After trypsin-treatment, the mobilities of TR viruses were all increased to the same level; however, their rate of migration was lower than that of trypsin-treated parent virus. This lower mobility of trypsin-treated OTR viruses was the only difference which could be associated with retained infectivity.
Antigens, Viral↗
Modification of the leader protein (Lb) of foot-and-mouth disease virus.
Translation of foot-and-mouth disease virus RNA for extended periods in rabbit reticulocyte lysates results in the appearance of a previously undescribed protein. A protein with similar properties can also be detected in BHK cells at late times after virus infection. Specific immunoprecipitation has shown that this protein (Lb') is closely related to the smaller of the two leader proteins, Lb, although it migrates with an apparently higher Mr in SDS-polyacrylamide gels. The conversion of Lb to Lb' can be mimicked by treatment with carboxypeptidase B. It is suggested that C-terminal trimming of Lb to produce Lb' results in an increase in negative charge and is responsible for its slower migration in SDS-PAGE.
Aphthovirus↗
Deconvolution of fully overlapped reflections from crystals of foot-and-mouth disease virus O1 G67.
Foot-and-mouth disease virus O(1) G67 forms crystals that appear similar to those of the closely related viruses O(1)K and O(1)BFS, both of which belong to space group I23. Statistical disorder in the O(1) G67 crystals means, however, that the measured diffraction data possess higher symmetry consistent with point group 432. It is shown that this is due to intimate twinning, with mosaic blocks randomly distributed between the two orientations. This results in a twofold loss of information due to the exact superimposition of non-identical reflections from the two orientations. A simple procedure has been devised to deconvolute these overlapped reflections by applying constraints in both real and reciprocal space. This procedure works well, providing interpretable electron-density maps for this virus. Other applications are discussed.
Journal Article↗
Inactivation of foot-and-mouth disease virus with ethylenimine.
Foot-and-mouth disease virus (FMDV) was inactivated by ethylenimine (EI) at three concentrations and two temperatures. Comparison of inactivation kinetics and the antigenic and immunogenic potency of EI and N-acetylethylenimine (AEI)-inactivated FMDV indicates that EI has nearly optimal characteristics as an inactivant for FMDV vaccine preparation. Although AEI-inactivated FMDV has proved to be a potent specific immunogen, an equivalent percentage of EI inactivated FMDV at substantially faster rates and produced an equally potent immunogen. In addition, EI inactivated FMDV at rates that were essentially linear throughout the loss of nearly all measurable infectivity.
Animals↗
[Immune response in mice induced by different doses of foot-and-mouth disease virus].
Response against foot-and-mouth disease virus 01 Campos on vaccinated female mice and suckling litter was estimated. Vaccine doses ranged between 0.05 and 30 micrograms of virus. The lower dose protected 39.5% of suckling litter whereas 100% protection was achieved using the higher doses. Serum neutralization indexes in females, at 45 days post vaccination, ranged from 3.60 to 4.86 for 0.05 microgram to 0.10 microgram and 4.86 to 5.50 for the high doses. Although the doses were excessively high (eq. 1 mu/g average live weight) and (OH)3Al was used as adjuvant, no adverse effect on the immune system was detected in any of the vaccinated animals.
Animals↗
Development and comparison of genome detection assays for the diagnosis of foot-and-mouth disease suspected clinical samples.
Detection of foot-and-mouth disease virus (FMDV) from clinical specimens by conventional sandwich enzyme-linked immunosorbent assay (ELISA) and virus isolation in cell culture is often compromised owing to limited sensitivity and inactivation during transit, respectively. A RT-PCR (oligoprobing) ELISA in both solid and aqueous phase hybridization formats targeting an across serotype conserved site at 3C-3D region was developed and its effectiveness was compared with that of the known targets at the IRES region. A non-isotopic RNA dot hybridization assay with colorimetric detection targeting both the IRES and the 3D region were also validated, which is capable of handling high throughput samples with ease. RT-PCR (oligoprobing) ELISA and dot hybridization assay showed 1000- and 10-fold greater sensitivity than the sandwich ELISA, respectively. Robustness of these diagnostic methods was explored by examining on sandwich ELISA-negative clinical samples. Both the assays developed in the present study were able to detect viral genomes in samples undetectable by conventional ELISA, thereby demonstrating 'proof of sensitivity'. Although the potential of these assays for providing definitive diagnosis in carrier hosts and in species where clinical disease is inapparent remains to be examined, nevertheless these assays can be adapted for comprehensive surveillance of foot-and-mouth disease in India.
3C Viral Proteases↗
Foot-and-mouth disease: a review of the virus and the symptoms.
Foot-and-mouth disease virus (FMDV) is the etiologic agent of foot-and-mouth disease (FMD), which is a disease of cattle, swine, and other cloven-footed animals. FMD is characterized by the formation of vesicles on the tongue, nose, muzzle, and coronary bands of infected animals. The virus has several unique characteristics that enable it to cause one of the most economically devastating diseases in today's world. The ease with which it may be transmitted by contact and aerosol, combined with its enhanced ability to initiate infections, virtually ensures that most, if not all, animals in a herd will contract FMD. The long-term survival of FMDV in infected animals' tissues and organs, especially when refrigerated, offers an opportunity for its national and international transmission through the food chain. Multiple serotypes and numerous subtypes reduce the effectiveness and reliability of vaccines. The possible development of carriers in vaccinated animals and those that have recovered from FMD provides additional potential sources of new outbreaks. These features create a disease that can have a major economic impact on farmers and entire nations.
Aerosols↗
Early antibody responses of cattle for foot-and-mouth disease quadrivalent double oil emulsion vaccine.
Foot-and-mouth disease (FMD) is an economically important disease of cloven-hoofed animals. The multiplicity of FMDV serotypes in animals poses a central problem in the policy of vaccination and is of much concern to health authorities. Hence it is the practice of vaccination with polyvalent vaccine for prophylactic measure. In the present report, we analysed the early antibody responses elicited by FMDV quadrivalent (FMDV O, A, C and Asia 1 serotypes) double emulsion (Montanide ISA 206) vaccines in cattle. We observed variations between various viral serotypes in eliciting early antibody response although neutralizing antibody response against all the four serotypes were detected as early as fourth day following vaccination. The duration of immunity also appeared to maintain for long period. The neutralizing antibody titres were maintained well above 2log(10) even after 6 months of vaccination irrespective of serotypes. Thus, allows the possibilities of two vaccinations per year for the maintenance of herd immunity.
Adjuvants, Immunologic↗