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Glycobiology vol 5 no 2 pp. 161-166, 1995
© 1995

review-article

Cell surface components of Leishmania: identification of a novel parasite lectin?

Deborah F. Smith and Desikan Rangarajan

Department of Biochemistry, Imperial College of Science, Technology and Medicine London SW7 2AZ, UK

Received on October 24, 1994; accepted on October 24, 1994

Protozoan parasites of the genus Leishmania have a glycoconjugate surface coat (the glycocalyx) that acts as the interface between the parasite and its external environment. The prinicipal components of the glycocalyx, the lipophosphoglycans and the glycoinositolphospholipids, have a variety of functions that facilitate parasite survival in both the extracellular and the intracellular stages of the life cycle. Recently, a novel hydrophilic Leishmania protein, the Gene B protein, has been identified on the surface of infective parasite stages. Attachment to the surface appears to be by association between a region of repeated amino acids in this molecule and components of the glycocalyx. As a consequence, the Gene B protein is exposed on the parasite surface while other peptides are buried beneath the glycocalyx. The putative functions of this unusual molecule are discussed.

differentially regulated genes glycoconjugates infective parasites Leishmania surface protein


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