Identification and distribution of carbohydrate moieties on the salivary glands of Rhodnius prolixus and their possible involvement in attachment/invasion by Trypanosoma rangeli

Experimental Parasitology

Volumn 100, Issue 4, 2002, Pages 226-234

  Basseri, H R ^a   Tew, I F ^b   Ratcliffe, N A ^b  

^a TEHRAN UNIVERSITY OF MEDICAL SCIENCES   (Iran)

^b SWANSEA UNIVERSITY   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

FLUORESCEIN ISOTHIOCYANATE; GALACTOSE; LECTIN; N ACETYLGALACTOSAMINE; N ACETYLGLUCOSAMINE;

ANIMAL TISSUE; ARTICLE; BINDING AFFINITY; CARBOHYDRATE ANALYSIS; CONTROLLED STUDY; EPIMASTIGOTE; HOST PARASITE INTERACTION; IN VITRO STUDY; INSECT; NONHUMAN; PRIORITY JOURNAL; RHODNIUS PROLIXUS; SALIVARY GLAND; SPECIES INVASION; TRYPANOSOMA;

ADHESIONS; ANIMALS; CARBOHYDRATES; FLUORESCEIN-5-ISOTHIOCYANATE; FLUORESCENT DYES; INSECT VECTORS; LECTINS; MICROSCOPY, FLUORESCENCE; RHODNIUS; SALIVARY GLANDS; TRYPANOSOMA;

ANIMALIA; ARACHNIDA; HEXAPODA; INSECTA; PROTOZOA; RHODNIUS; RHODNIUS PROLIXUS; TRYPANOSOMA; TRYPANOSOMA RANGELI;

EID: 0036557776     PISSN: 00144894     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-4894(02)00026-7     Document Type: Article

References (42)

1. Arrighi R.B.G., Hurd H. The role of Plasmodium berghei ookinete proteins in binding to basal lamina components and transformation into oocysts. International Journal for Parasitology. 32:2002;91-98.
2. Azambuja P., Garcia E.S. Care and maintenance of triatomine colonies. Beard J.M., Louis C. The Molecular Biology of Insect Disease Vectors, A Methods Manual. 1997;56-64 Chapman & Hall, New York.
3. Barreau C., Touray M., Pimenta P.F., Miller L.H., Vernick K.D. Plasmodium gallinaceum; sporozoite invasion of Aedes aegypti salivary glands is inhibited by anti-gland antibodies and by lectins. Experimental Parasitology. 81:1995;332-343.
4. Basseri, H.R., 2001. Interaction between Trypanosoma rangeli and the salivary gland of blood-sucking bug Rhodnius prolixus. PhD thesis, University of Wales, Swansea.
5. Billingsley P.F., Sinden R.E. Determinants of malaria-mosquito specificity. Parasitology Today. 13:1997;297-301.
6. Bray R.S. Leishmania mexicana mexicana: attachment and uptake of promastigotes to and by macrophages in vitro. Journal of Protozoology. 30:1983;314-322.
7. Brennan J.D.G., Knet M., Dhar R., Fujika H., Kumar N. Anopheles gambiae salivary gland protein as putative targets for blocking transmission of malaria parasites. Proceedings of the National Academy of Sciences of the USA. 97:2000;13859-13864.
8. Burton S.L., Ellar D.J., Li J., Derbyshire D.J. N-acetylgalactosamine on the putative insect receptor aminopeptidase N is recognised by a site on the domain III lectin-like fold of a Bacillus thuringiensis insecticidal toxin. Journal of Molecular Biology. 287:1999;1011-1022.
9. Butters T.D., Hughes R.C. Lectin binding to mosquito Aedes aegyptii and human KB cells: structural comparisons of membrane oligosaccharides. Carbohydrate Research. 61:1978;159-168.
10. De Miranda-Santos I.K., Pereira M.E. Lectins discriminate between pathogenic and nonpathogenic South American trypanosomes. American Journal of Tropical Medicine and Hygiene. 33:1984;839-844.
11. Ellis D.S., Evans D.A., Stamford S. The penetration of the salivary glands of Rhodnius prolixus by Trypanosoma rangeli. Zeitschrift für Parasitenkunde. 62:1980;75-84.
12. Ferguson M.A. The surface glycoconjugates of trypanosomatid parasites. Philosophical Transactions of the Royal Society of London. Series B. 352:1997;1295-1302.
13. Hecker H., Schwarzenbach M., Rudin W. Development and interactions of Trypanosoma rangeli in and with the reduviid bug Rhodnius prolixus. Parasitology Research. 76:1990;311-318.
14. Hernandez A.G., Rodriguez N., Stojanovic D., Candelle D. The localization of a lectin-like component on the Leishmania cell surface. Molecular Biology Reports. 11:1986;149-153.
15. Ingram G.A., Molyneux D.H. Insect lectins: role in parasite-vector interactions. Kilpatrick D.C., Van Driessche E., Bog-hansen T.C. Lectin Reviews. vol. 1:1991;103-127 Sigma Chemical Company, St. Louis, MO.
16. Jacobson R.L., Doyle R.J. Lectin-parasite interactions. Parasitology Today. 12:1996;55-60.
17. Knowles B.H., Knight P.J., Ellar D.J. N-acetyl galactosamine is part of the receptor in insect gut epithelia that recognizes an insecticidal protein from Bacillus thuringiensis. Proceedings of the Royal Society of London. Series B. 245:1991;31-35.
18. Lis H., Sharon N. Lectin: carbohydrate-specific proteins that mediate cellular recognition. Chemistry Review. 98:1998;637-674.
19. Mello C.B., Nigam Y., Garcia E.S., Azambuja P., Newton R.P., Ratcliffe N.A. Studies on a haemolymph lectin isolated from Rhodnius prolixus and its interaction with Trypanosoma rangeli. Experimental Parasitology. 91:1999;289-296.
20. Mehlert A., Zitzman N., Richardson J.M., Treumann A., Ferguson M.A.J. The glycosylation of the variant surface glycoproteins and procyclic acidic repetitive proteins of Trypanosoma brucei. Molecular and Biochemical Parasitology. 91:1998;145-152.
21. Mohamed H.A., Ingram G.A., Molyneux D.H., Sawyer B.V. Use of fluorescein-labelled lectin binding of salivary gland to distinguish between Anopheles stephensi and Anopheles albimanus species and strains. Insect Biochemistry. 21:1991;767-773.
22. Morris A.C., James A.A. Culture and analysis of insect salivary glands. Crampton J.M., Beard C.B., Louis C. The Molecular Biology of Insect Disease Vectors: A Methods Manual. 1997;500-506 Chapman & Hall, London.
23. Nussenzveig R.H., Bentley D.L., Ribeiro J.M.C. Nitric oxide loading of the salivary nitric-oxide-carrying hemoproteins (nitrophorins) in the blood-sucking bug Rhodnius prolixus. The Journal of Experimental Biology. 198:1995;1093-1098.
24. Okolo C.J., Jenni L., Molyneux D.H., Wallbanks K.R. Surface carbohydrate differences of Glossina salivary glands and infectivity of Trypanosoma brucei gambiense to Glossina. Annales Societe Belgique de Medecine Tropicale. 70:1990;39-47.
25. Parodi A.J. Biosynthesis of protein-linked oligosaccharides in trypanosomatid flagellates. Parasitology Today. 9:1993;373-377.
26. Perrone J.B., DeMaio J., Spielman A. Regions of mosquito salivary glands distinguished by surface lectin-binding characteristics. Insect Biochemistry. 16(2):1986;313-318.
27. Pimenta P.F., Saraiva E.M., Sacks D.L. The comparative fine structure and surface glycoconjugate expression of three life stages of Leishmania major. Experimental Parasitology. 72:1991;191-204.
28. Ramasamy R., Wanniarachchi I.C., Srikrishnaraj K.A., Ramasamy M.S. Mosquito midgut glycoproteins and recognition sites for malaria parasites. Biochimica et Biophysica Acta. 1361:1997;114-122.
29. Ratcliffe N.A., Nigam Y., Mello C.B., Garcia E.S., Azambuja P. Trypanosoma cruzi and erythrocyte agglutinins: a comparative study of occurrence and properties in the gut and hemolymph of Rhodnius prolixus. Experimantal Parasitology. 83:1996;83-93.
30. Rosenberg R. Inability of Plasmodium knowlesi sporozoites to invade Anopheles freeborni salivary glands. American Journal of Tropica Medicine and Hygiene. 34:1985;687-691.
31. Rudin W., Hecker H. Lectin-binding sites in the midgut of the mosquitoes Anopheles stephensi Liston and Aedes aegypti L. (Diptera: Culicidae). Parasitology Research. 75:1989;268-279.
32. Sacks D.L., Hieny S., Sher A. Identification of cell surface carbohydrate and antigenic changes between noninfective and infective developmental stages of Leishmania major promastigotes. Journal of Immunology. 135:1985;564-569.
33. Sacks D.L., Saraiva E.M., Rowton E., Turco S.J., Pimenta P.F. The role of the lipophosphoglycan of Leishmania in vector competence. Parasitology. 108:1994;S55-S62.
34. Saraiva E.M., Pimenta P.F., Brodin T.N., Rowton E., Modi G.B., Sacks D.L. Changes in lipophosphoglycan and gene expression associated with the development of Leishmania major in Phlebotomus papatasi. Parasitology. 111:1995;275-287.
35. Schottelius J., Aisien M.S.O. Trypanosome-lectin interaction. Doyle R.J., Slifkin M. Lectin-Microorganism Interaction. 1994;225-248 Marcel Dekker, New York.
36. Schottelius J., Gabius H.J. Detection and quantitation of cell-surface sugar receptor(s) of Leishmania donovani by application of neoglycoenzymes. Parasitology Research. 78:1992;529-533.
37. Snary D. Receptors and recognition mechanisms of Trypanosoma cruzi. Transactions of the Royal Society of Tropical Medicine and Hygiene. 79:1985;587-590.
38. Stark K.R., James A.J. The salivary glands of disease vector. Beaty B.J., Marguardt W.C. The Biology of Disease Vector. 1996;333-347 University Press of Colorado, New York.
39. Takle C.B., Young A. A simple semi-defined culture medium for the growth of Trypanasoma rangeli. Transaction of Royal Society of Tropical Medicine and Hygiene. 82:1988;247.
40. Touray M.G., Warburg A., Laughinghouse A., Krettli A.U., Miller L.H. Developmentally regulated infectivity of malaria sporozoites for mosquito salivary glands and the vertebrate host. Journal of Experimental Medicine. 175:1992;1607-1612.
41. Volf P., Tesarova P., Nohynkova E.N. Salivary proteins and glycoproteins in phlebotomine sandflies of various species, sex and age. Medical and Veterinary Entomology. 14:2000;251-256.
42. Watkins R. Histology of Rhodnius prolixus infected with Trypanosoma rangeli. Journal of Invertebrate Pathology. 17:1971;59-66.