[Protection of naturally susceptible animals against foot-and-mouth disease with a peptide, synthesized on a lysine matrix]. / Zashchita estestvenno-vospriimchivykh zhivotnykh ot iashchura peptidom, sintezirovannym na lizinovoi matritse.

A peptide VP1-(142-158)-MAP (Multiple antigen peptide system) consisting of two parts: a lysine matrix made up of three levels of lysine residues coupled with each other and amino acid sequence 142-158 of VP1 of FMD virus strain A(22)550--has been synthesized. Guinea-pigs inoculated with 20 mkg of the peptide incorporated with Freund's complete adjuvant were protected against challenge with 500 ID50 of homologous FMD virus. Sheep were immunized with a single inoculation of the peptide in a dose of 1.0 mg. Cattle inoculated twice with 1.5 mg of the peptide with incomplete adjuvant on the basis of synthetic oil developed high virus-specific antibody titres both after the first (5.3-7.6 log2 ND50/0.1 ml) and the second inoculation (10.2-11.0 log2 ND50/0.1 ml). The peptide-immunized animals were resistant to challenge with homologous virulent virus in a dose of 10(4) ID50. The immunogenic and protective capacities of the peptide VP1-(142-158)-MAP were shown to be greater as compared with those of its linear analogue-peptide VP1-(141-160).

[Protection from foot-and-mouth disease virus in naturally-susceptible animals by a linear polymer of a synthetic peptide]. / Zashchita ot iashchura estestvenno-vospriimchivykh zhivotnykh lineinym polimerom sinteticheskogo peptida.

Linear polymer of a peptide corresponding to the fragment 142-155 of the foot-and-mouth disease virus A22(550) protein (VP1) was synthesized. Whereas the monomeric peptide was only slightly immunogenic, the polymer induced virus-neutralizing antibodies in rabbits and protected 100% guinea pigs. Sheep vaccinated once and cattle vaccinated twice were stable against infection with the homologous virulent foot-and-mouth disease virus.

[Primary structure of the gene for protein VP1 from foot-and-mouth disease virus serotype O1 isolated in the USSR]. / Pervichnaia struktura gena belka VP1 virusov iashchura serotipa O1, izolirovannykh v SSSR.

The nucleotides sequence has been determined for the viral RNA and some of its cDNAs coding for the major antigenic protein of the epidemic stomatitis O1-194 and O1-1618 VP1 viruses. The expressed microheterogeneity has been registered for the population of the strain O1-194.

[Primary structure of the 3'-terminal region of the RNA-polymerase gene in foot-and-mouth virus A22]. / Pervichnaia struktura 3'-kontsevoi oblasti gena RNK-polimerazy virusa iashchura A22.

This study was undertaken for the purpose of determining the primary structure of the 3' end gene of RNA polymerase of foot-and-mouth disease virus A22 550. Reported are isolation and purification of the virus, isolation of RNA, synthesis of cDNA, experience obtained from cloning as well as analysis of hybridisation and isolation of plasmid DNA. Nucleotide sequences, characterised by specific clones, were tested for potential needle structures. Also described are homology comparisons among FMD virus types A12, A10, O1, and C1.

[Primary structure of the gene for VP1 protein of the foot-and-mouth disease virus of Asia 1 serotype]. / Pervichnaia struktura gena belka VP1 virusa iashchura serotipa Aziia 1.

The nucleotide sequence of the cDNA for the viral RNA region coding for the main antigenic protein of the epidemic stomatitis virus of Asia 1 serotype has been identified. The amino acid sequences in the regions of VP1 protein antigenic determinants of the serotype Asia 1 virus and other serotypes viruses have been compared.

[Antigenic structure of foot-and-mouth virus. IV. Synthesis and immunogenic properties of new fragments of the VP1 protein of food-and-mouth virus strain A22]. / Antigennaia struktura virusa iashchura. IV. Sintez i immunogennye svoistva novykh fragmentov belka VP1 virusa iashchura shtama A22.

A synthesis of new fragments of VP1 protein with the specificity of A22 strain of foot-and-mouth disease virus is described. Immunization with the free 136-152 peptide and KLH-conjugates of the peptides 136-152 and 197-213 induced 60-80% protection of guinea pigs against challenge with the A22 virus. Synthetic peptides corresponding to the 10-24, 50-69 and 175-189 sequences of VP1 did not show any protective activity. We have found that uncoupled peptides 175-189 and 197-213 are able to induce antipeptide antibodies. However, these antibodies did not possess any neutralizing activity. Immunization of animals with the mixture of (136-152)O1K and (175-189)A22 has led to inhibition of the immune response to the (136-152)O1K fragment.

[Primary structure of the A22 RNA polymerase gene of the foot and mouth disease virus]. / Pervichnaia struktura gena RNK-polimerazy virusa iashchura A22.

Complete nucleotide sequence of gene RNA polymerase for the foot-and-mouth disease virus subtype A22 has been determined.

[Is the Arg-Gly-Asp sequence the site for foot-and-mouth disease virus binding with cell receptor?]. / Iavliaetsia li posledovatel'nost' Arg-Gly-Asp uchastkom sviazyvaniia virusa iashchura s kletochnym retseptorom?

The Arg-Gly-Asp sequence is being found in an increasing wide range of proteins with "adhesive" function. Studying a series of synthetic peptide fragments of VP1 protein of FMDV, we showed that peptides containing the Arg-Gly-Asp sequence, but not control peptides, inhibited FMDV binding to pig kidney cells in vitro, thus indicating participation of that sequence in FMDV binding to host cells.

[Synthetic peptides simulating the protective epitopes of VP1 protein of foot-and-mouth disease virus type O and A]. / Modelirovanie s pomoshch'iu sinteticheskikh peptidov protektivnykh épitopov belka VP1 virusa iashchura serotipov O i A.

In a search of novel approaches to cattle protection from foot-and-mouth disease we have prepared a series of peptides from the major antigenic region 130-160 of the VP1 protein. The 144-159 peptide as well as 141-152, 141-148, 148-159 segments (strain O1K) were inactive in all in vitro and in vivo experiments on virus inhibiting. On the other band, synthetic 136-152, 136-148 O1K sequences as well as 131-149, 140-149 A22 sequences afforded 50 to 100% protection, both in the free state and conjugated with keyhole limpet hemocyanin. Therefore the 136-145 region should be considered as an essential part of the major sequential epitope, necessary for full-scale antiviral immune response. We also believe that the 136-152 segment is so far the smallest peptide capable of eliciting virus neutralizing antibodies and antiviral protection without conjugation with a high-molecular carrier.