Leishmania major, the agent of local CL, like most Leishmania spp., express predominantly three classes of molecules to form a surface glycocalyx: protein-free lipophosphoglycan (LPG), the glycosylphosphatidylinositol-anchored highly glycosylated proteophosphoglycan and glycoproteins (gp) of which gp63, a 63 kDa surface proteinase, is the most prominent. gp63, also described as leishmanolysin or major surface protease, is a zinc metalloprotease and has been reported to mediate entry into macrophages, enhancing phagocytosis and survival within the macrophage. gp63 is expressed with> 500 000 copies (0.5-1% of total cell protein) and distributed over the entire promastigote body, including flagellum and flagellar pocket, and can be capped with antibodies which denotes that it is free to move in the plane of the membrane.