Abstract
Successful initiation and maintenance of the parasitic state for Leishmania species of protozoan parasites, requires identification and specific adhesion to host cells followed by internalization and establishment of an intracellular existence. Clearly any strategy to block initial promastigote binding or subsequent spread of amastigotes will require knowledge about the molecular nature of host parasite cellular interactions. A number of laboratories have made good progress in this area demonstrating some of the characteristics of the macrophage receptors and promastigote ligands. At this time, evidence exists for a complicated interaction with a number of receptors including the iC3b complement receptor CR3 and the mannosyl/fucosyl receptor (Blackwell et al., 1985; Channon et al., 1984). Particular emphasis has been placed on those which bind a major surface glycolipid (Handman and Goding, 1985) and glycoproteins (Chang and Chang, 1986; Russell and Wilhelm, 1986) as well as covalently linked complement fragments (Blackwell et al., 1985). Very little attention has been placed on the other components of the parasite surface to assess whether the former ligands are singularly important or whether an array of glycosylated molecular species can interact with macrophage receptors via a redundant set of oligosaccharides. It is frequently observed for example, that monoclonal antibodies developed against cell surface antigens cross-react with many molecules of varying molecular weights - a phenomenon readily explained by a restricted set of oligosaccharides held in common by varying protein and lipid species.
Keywords
- Leishmania Species
- Variable Surface Glycoprotein
- Parasite Surface
- Major Surface Glycoprotein
- Macrophage Receptor
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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References
Bordier C (1981) Phase separation of intetral membrane proteins in Triton X-114 solution J Biol Chem 256: 1604–1607
Blackwell JM, Ezekowitz RAB, Roberts MB, Channon JY, Sim RB, Gordon S (1985) Macrophage complement and lectin-like receptors bind Leishmania in the absence of serum J Exp Med 162: 324–331
Chang CS, Chang K-P (1986) Monoclonal antibody affinity purification of a Leishmania membrane glycoprotein and its inhibition of Leishmania- macrophage binding Proc Natl Acad Sci USA 83: 100–104
Channon JY, Roberts MB, Blackwell JM (1984) A study of the differential respiratory burst activity elicited by promastigotes and amastigotes of Leishmania donovani in murine resident peritoneal macrophages Immunol 53: 345–351
Handman E, Goding JW (1985) The Leishmania receptor for macrophages is a lipid-containing glycoconjugates EMB0 4: 329–336
Russell DG, Wilhelm H (1986) The involvement of the major surface glycoprotein (gp63) of Leishmania promastigotes in attachment to macrophages J Immunol 136: 2613–2610
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© 1987 Springer-Verlag Berlin Heidelberg
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Olafson, R.W., Wallis, A.E., McMaster, R. (1987). Structural Studies on Surface Glycoproteins of Leishmania Promastigotes: Isolation, Amino Acid Composition and Amino Terminal Sequence Studies. In: Chang, KP., Snary, D. (eds) Host-Parasite Cellular and Molecular Interactions in Protozoal Infections. NATO ASI Series, vol 11. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-72840-2_16
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DOI: https://doi.org/10.1007/978-3-642-72840-2_16
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-72842-6
Online ISBN: 978-3-642-72840-2
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