B- and T-epitopes have been localized within the protective fragments of VP1 protein, viz., 136-152 of the O1K strain and 135-159 of the A22 strain of the foot-and-mouth disease virus (FMDV). Antibodies eliciting after immunization of various animals with the 135-159 A22 peptide are directed to different sites of the peptide. Immunogenicity of fragments of the 135-159 A22 peptide on mice correlates with their activity on T-cells of the same animals and protective activity on guinea pigs. The investigations were carried out using synthetic fragments of the 136-152-O1K and 135-159-A22 peptides.
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[Synthetic peptide designs based on immunoactive fragments of the VP1 protein of the foot-and-mouth disease virus strain A22].
Bioorg Khim
December 2000
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, GSP-7 Moscow, 117871 Russia.
Peptide constructs consisting of 44-53 aa were synthesized on the basis of sequences 135-159, 170-190 and 197-213 of VP1 from the foot-and-mouth disease A22 strain. Immunogenic and protective properties of the peptide constructs were studied in guinea pigs and mice of three lines. The constructs were shown to induce higher levels of antibodies and exhibit higher protective effects than the separate peptides.
View Article and Find Full Text PDFA peptide construct containing B-cell and T-cell epitopes from the foot-and-mouth disease viral VP1 protein induces efficient antiviral protection.
Vaccine
February 1999
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow.
A new peptide construct Palm135-158-GGA-170-188(Acm) has been synthesized and investigated in a number of in vitro and in vivo test systems. The construct contains a virus specific T-helper epitope within the 170-188 sequence of VP1, in addition to the main antigenic 135-158 region of the foot-and-mouth disease viral VP1 protein (strain A22). The construct has higher protective, antigenic, immunogenic and T-cell proliferative activity then the previously described shorter peptide Palm(2)135-159.
View Article and Find Full Text PDFSynthetic vaccine against foot-and-mouth disease based on a palmitoyl derivative of the VP1 protein 135-159 fragment of the A22 virus strain.
Vaccine
October 1996
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya, Moscow, Russian Federation.
The peptide Palm2 135-159, a dipalmitoyl derivative of the 135-159 fragment of VP1 protein of the foot-and-mouth disease virus strain A22 was synthesized. In the experiments on mice, guinea pigs and sheep Palm2 135-159 possesses greater immunogenic and protective activity than the nonacylated 135-159 peptide. The synthetic vaccine against foot-and-mouth disease for use in sheep was developed on the basis of the lipopeptide.
View Article and Find Full Text PDFNew virus-specific T-helper epitopes of foot-and-mouth disease viral VP1 protein.
FEBS Lett
October 1993
Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow.
Immunogenicity studies of synthetic peptides from different regions of VP1 protein of foot-and-mouth disease virus strain A22 revealed the following active fragments: 39-61, 50-69, 135-159, 175-189, 170-189 and 197-213. Testing of virus neutralizing antibody production in rabbits primed by peptides and then inoculated by the virus showed that only peptides 135-159 and 170-189 were able to induce the functional T-cell helper activity. Localization of virus-specific T-cell recognition sites in sequences 135-159 and 170-189 was confirmed in in vitro recognition experiments of the virus by peptide activated mice lymphocytes.
View Article and Find Full Text PDFB- and T-epitopes have been localized within the protective fragments of VP1 protein, viz., 136-152 of the O1K strain and 135-159 of the A22 strain of the foot-and-mouth disease virus (FMDV). Antibodies eliciting after immunization of various animals with the 135-159 A22 peptide are directed to different sites of the peptide.
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