Preparation and Characterization of Nanoliposome Containing Isolated VP1 Protein of Foot and Mouth Disease Virus as a Model of Vaccine.

Abstract

Foot-and-mouth disease (FMD) is an acute and highly contagious disease in livestock, such as cattle, sheep, and pigs, leading to a lot of economic losses. The current FMD vaccines formulated by inactivated whole-virus and adjuvant successfully reduce disease outbreaks in many regions of the world. Immunological studies on FMD viruses revealed that the dominant epitope in arising neutral antibody response is amino acid residues constructing the G-H loop, constituting a surface loop of the structural protein, termed VP1. Liposomes as one of the most well-known vehicles are considered an important carrier in vaccine development, and their function is used to encapsulate purified VP1 protein based on their size, charge, and lipid content. Accordingly, the VP1 protein was isolated from the FMD virus. This study aimed to compare four methods of VP1 protein encapsulation in the liposome and the extruding effect, as follows: 1) VP1 protein was dissolved in dimethyl sulfoxide and added to the lipid film hydrated by ethanol, 2) the lipid film was hydrated by VP1 protein with 7M urea, 3) the lipid film was hydrated by VP1 protein and freeze-thawed, and 4) the lipid film was hydrated by VP1 protein. The highest encapsulation efficiency was 91% in the second method which purified protein-containing urea. The VP1 protein in the prepared liposome (1, 2-dimyristoyl-sn-glycero-3-phosphocholine: 1, 2-dimyristoyl-sn-glycero-3-phosphocholine: cholesterol) released more than 90% of protein content after 240 h.