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.
Flinn
H M
HM
Department of Biochemistry, Imperial College of Science, Technology and Medicine, London, UK.
Rangarajan
D
D
Smith
D F
DF
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