Immunogenicity of two FMDV nonameric peptides encapsulated in liposomes in mice and the protective efficacy in guinea pigs.

It has been predicted that nonameric peptides I (VP1(26-34), RRQHTDVSF), II (VP1(157-165), RTLPTSFNY) and III (VP1(45-53), KEQVNVLDL) from the VP1 capsid protein of the foot-and-mouth disease virus (FMDV) are T cell epitopes. To investigate whether these peptides have immunological activity, BALB/c mice were immunized with peptide I, II or III conjugated with immunostimulating complexes (ISCOMs). A cytotoxic T lymphocyte assay was used to evaluate the cytotoxic activity induced by peptides along with by measuring peptide-specific T-cell proliferation and CD8(+) T lymphocyte numbers in whole blood and interferon (IFN)-γ production in peripheral blood mononuclear cells induced by peptides.

Reconstruction of a chicken BF2 protein complex and identification of binding nonamer peptides derived from avian influenza virus hemagglutinin.

In order to reconstruct the system for identification of short antigenic peptides, the chicken BF2 gene of Chinese Sanhuang (SH) chicken line was linked to the beta(2)m gene via (G4S)3, a linker encoding a 15-amino acid glycine-rich peptide, by splicing overlap extension PCR (SOE-PCR). The MBP-BF2-(G4S)3-beta(2)m fusion protein was expressed and purified in a pMAL-p2X/E. coli TB1 system.

Extensive analysis of different allelelic structures of the chicken BF2 and beta2m proteins.

No information is available to date on the different allelelic structures of the chicken MHC class I (BF2) and beta2m proteins. To elucidate the structure, new allelic beta2m and five different BF2 genes were expressed solubly and purified in a pMAL-p2X/E. coli TB1 system.

Structures and homology modeling of chicken major histocompatibility complex protein class I (BF2 and beta2m).

In order to elucidate the two-dimensional (2D) and three-dimensional (3D) structures of chicken major histocompatibility complex (MHC) class I protein (BF2 and beta2m) and further reconstruct their complex identifying the virus-derived antigenic peptides, the mature protein of BF2 and beta2m genes were expressed solubility in pMAL-p2X/Escherichia coli. TB1 system. The expressed MBP-BF2- and MBP-beta2m-fusion proteins were purified, and cleaved by the factor Xa protease.

Characterization of BF2 and beta2m in three Chinese chicken lines.

Twenty-four BF2 genes and 10 beta(2)m genes from Chinese Sanhuang (SH), Wuji (WJ), and Zhenzhu (ZZ) chicken lines were cloned, and the amino acid replacement rates of the BF2 polypeptide binding domain were investigated. For this purpose, 13 BF2 genes from the SH-chicken line (BF2*01sh-BF2*13sh), six BF2 genes from the WJ-chicken line (BF2*01wj-BF2*06wj), and five BF2 genes from the ZZ-chicken line (BF2*01zz-BF2*05zz) were analyzed. The overall conservation of BF2 alleles could be observed within the sequences, and relative conservation was also displayed in the peptide-binding domain, CD8(+) interaction sites, and beta(2)m contact sites.