Characteristics of the Chromatographic Cleaning and Protectiveness of the LcrV Isoform of Yersinia pestis

Abstract

Electrophoretic, homogeneous, highly purified preparations of various isoforms of the immunodominant antigen V (LcrV protein) of Yersinia pestis have been obtained via chromatographic purification. A significant similarity in the chromatographic profiles of the LcrV antigen isoforms of different strains with tryptophan (W113) and glutamic acid (E113) residues at position 113, which differed from the isoform profile containing glycine residue LcrV (G113), has been recorded. The latter is characterized by the highest antigenic and protective activity as compared with other protein isoforms. This isoform almost completely protected the immunized group of animals and had the greatest ability to induce the production of antibodies, the titers of which reached 1 : 250 000.