Expression of a hydrophilic surface protein in infective stages of Leishmania major.
A family of differentially expressed genes from Leishmania major contains one sequence (Gene B) that encodes a novel, hydrophilic protein found on the surface of infective parasite stages. The 177-residue, acidic Gene B protein is characterised by an amino acid repetitive element, comprising 45% of the total molecule, that is related to the cell-wall binding domain of protein A from Staphylococcus aureus. No identifiable signal peptide, membrane-spanning domain or consensus for glycosylphosphatidylinositol anchor attachment to the cell surface is found elsewhere in the deduced protein sequence. In vitro, the Gene B protein fractionates with the parasite cell surface glycoconjugates, lipophosphoglycan and the glycoinositolphospholipids. This protein is the first characterised surface peptide marker for infective stages of the Leishmania life cycle.
Department of Biochemistry, Imperial College of Science, Technology and Medicine, London, UK.
H M
HM
Flinn
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D
Rangarajan
D F
DF
Smith
D000595:Amino Acid Sequence; D000818:Animals; D016054:DNA, Protozoan / Q000032:analysis; D005455:Fluorescent Antibody Technique; D005786:Gene Expression Regulation; D018320:Leishmania major / Q000235:genetics* / Q000378:metabolism / Q000648:ultrastructure; D008565:Membrane Proteins / Q000235:genetics* / Q000378:metabolism; D016253:Microscopy, Immunoelectron; D018598:Minisatellite Repeats; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D015800:Protozoan Proteins / Q000235:genetics* / Q000378:metabolism; D014158:Transcription, Genetic
D016054:DNA, Protozoan; D008565:Membrane Proteins; D015800:Protozoan Proteins