ABSTRACT
Foot-and-mouth disease (FMD) has caused severe economic losses to millions of farmers worldwide. In this work, the coding genes of 141-160 epitope peptide (EP141-160) of VP1 were inserted into the coat protein (CP) genes of MS2 in prokaryotic expression vector, and the recombinant protein self-assembled into virus-like particles (VLP). Results showed that the CP-EP141-160 VLP had a strong immunoreaction with the FMD virus (FMDV) antigen in vitro, and also had an effective immune response in mice. Further virus challenge tests were carried out on guinea pigs and swine, high-titer neutralizing antibodies were produced and the CP-EP141-160 VLP vaccine could protect most of the animals against FMDV.
Subject(s)
Antibodies, Neutralizing/biosynthesis , Antibodies, Viral/biosynthesis , Capsid Proteins/immunology , Foot-and-Mouth Disease Virus/genetics , Foot-and-Mouth Disease Virus/immunology , Foot-and-Mouth Disease/prevention & control , Vaccines, Virus-Like Particle/immunology , Viral Vaccines/immunology , Animals , Antibodies, Viral/immunology , Capsid Proteins/genetics , Enzyme-Linked Immunosorbent Assay , Epitopes , Foot-and-Mouth Disease/immunology , Freund's Adjuvant , Guinea Pigs , Levivirus/genetics , Mice , Neutralization Tests , Swine , Vaccines, Virus-Like Particle/administration & dosage , Viral Vaccines/administration & dosageABSTRACT
M2e is the external domain of M2 protein, a conservative transmembrane protein of the avian influenza A virus. Previous research had shown that the vaccine of the formation particle of M2e and hepatitis B virus core antigen (HBcAg) can fully protect mice against a lethal H5N1 subtype avian influenza virus (AIV) infection. As an effective approach against mucosal tissue infectious agent, mucosal vaccination requires effective and safe adjuvants. Here we have first fused two M2e peptide to the N terminal and the major immunodominant region (MIR) of the HBcAg protein simultaneously to create a fusion gene, named as M2eHBc+, and then inserted B subunit of Escherichia coli heat labile enterotoxin (LTB) into the N terminal of M2eHBc+ to construct the second fusion gene, named as LBM2eHBc+. These two fusion genes can be efficiently expressed in Escherichia coli cell and the yield peptide can self-assemble into virus-like particles (VLP). The mice immunization with two types of the purified particles by intranasal dropping and oral routes revealed that LTB can significantly enhance the mucosal immune responses of mice to co-expression M2eHBc+ particle form antigen.