RESUMO
Fragments encoding amino acids 76-130 in the linear conserved region (LCR) of A/Hubei/1/2010 (H5N1) HA2 was fused to hepatitis B core antigen (HBc) to generate a LCR-HBe virus-like particle (VLP). Results showed that the fusion protein of LCR-HBc was highly expressed in this prokaryotic expression system. The purified LCR-HBc particle stimulated high levels of IgG production in mice with a titer of > 1:12 800, and provided 50% cross-protection against lethal challenge by H1N1 viruses.
Assuntos
Animais , Feminino , Camundongos , Sequência de Aminoácidos , Glicoproteínas de Hemaglutininação de Vírus da Influenza , Alergia e Imunologia , Virus da Influenza A Subtipo H5N1 , Alergia e Imunologia , Vacinas contra Influenza , Alergia e Imunologia , Interferon gama , Pulmão , Patologia , Camundongos Endogâmicos BALB C , Dados de Sequência MolecularRESUMO
Hepatitis B virus core antigen (HBcAg) is a major viral nucleocapsid protein of HBV. It is a 21-22kD protein consisting of 183-185 amino acids. Because of its easy purification, strong immunogenicity, high expression level, and self-assembles into the virus-like particles (VLP), HBcAg could be an efficient and safe VLP carrier for developing vaccines for various pathogens. Up to now, HBcAg VLP carrier has been an important system to develop novel vaccines and many antigen epitope genes from viruses, bacteria and parasites were expressed successfully using the system.