Hm. Flinn et al., EXPRESSION OF A HYDROPHILIC SURFACE PROTEIN IN INFECTIVE STAGES OF LEISHMANIA-MAJOR, Molecular and biochemical parasitology, 65(2), 1994, pp. 259-270
A family of differentially expressed genes from Leishmania major conta
ins one sequence (Gene B) that encodes a novel, hydrophilic protein fo
und on the surface of infective parasite stages. The 177-residue, acid
ic Gene B protein is characterised by an amino acid repetitive element
, comprising 45% of the total molecule, that is related to the cell-wa
ll binding domain of protein A from Staphylococcus aureus. No identifi
able signal peptide, membrane-spanning domain or consensus for glycosy
lphosphatidylinositol anchor attachment to the cell surface is found e
lsewhere in the deduced protein sequence. In vitro, the Gene B protein
fractionates with the parasite cell surface glycoconjugates, lipophos
phoglycan and the glycoinositolphospholipids. This protein is the firs
t characterised surface peptide marker for infective stages of the Lei
shmania life cycle.