SAPOSIN-LIKE PROTEINS IN ANTI-INFECTIOUS IMMUNE RESPONSE

Crude extract of bacterially expressed, infectious bursal disease virus VPX/VP2 proteins induces protective immune response to the virus in chickens

Infectious bursal disease virus (IBDV) infects young chickens and causes serious lose to the poultry industry, worldwide. Previous attempts using purified bacterially expressed IBDV VP2 failed to elicit a protective immune response to the virus. This study was designed to investigate if the initial expressed protein contained neutralizing epitopes but became nonfunctional during purification st...

Heat Shock Proteins Enriched-Promastigotes of Leishmania major Inducing Th2 Immune Response in BALB/c Mice

Background: Heat shock proteins (HSP) are highly conserved molecules with many immunological functions. They are highly immunogenic with important role in cancer immunotherapy and in vaccine development against infectious diseases. As adjuvant, HSP can augment the immunogenicity of weak antigens and can stimulate antigen presenting cells. Although vaccines have been successful for many infec...

Highly Variable Immune-Response Proteins

Induction of Immune Response in Animal Model Using Recombinant Anti-NDV Vaccine

Background: Newcastle disease is a major avian disease that causes enormous economic loss in poultry industry. There have been a number of reports on the suitability of plant-based recombinant vaccine against this disease. Fusion (F) and hemagglutinin-neuraminidase (HN) epitopes of the Newcastle disease virus (NDV) represent the major immunogenic sites for development of recomb...

Saposin-like proteins (SAPLIP) carry out diverse functions on a common backbone structure.

A polypeptide motif characterized by the locations of six cysteines and several hydrophobic residues is found in saposins AD , sulfated glycoprotein-1, acid sphin-gomyelinase (ASM), acyloxyacyl hydrolase (AOAH), sur-factant protein B (SPB), and Entamoeba hktolytku pore-forming peptides (amoebapores) (1-4). The same motif is present, in an altered form, in plant aspartyl proteases (5). Each of t...