Trypanosoma cruzi: Involvement of glycoinositolphospholipids in the attachment to the luminal midgut surface of Rhodnius prolixus

• Published in: Experimental parasitology 2007-06, Vol.116 (2), p.120-128
• Main Authors: Nogueira, Nadir F.S., Gonzalez, Marcelo S., Gomes, José Eugênio, de Souza, Wanderley, Garcia, Eloi S., Azambuja, Patricia, Nohara, Lilian L., Almeida, Igor C., Zingales, Bianca, Colli, Walter
• Format: Article
• Language: English
• Subjects: Animals; binding sites; Biological and medical sciences; cell adhesion; Cell Adhesion - physiology; Chagas Disease - parasitology; Chagas Disease - transmission; Dose-Response Relationship, Drug; electrospray ionization-mass spectrometry; epimastigotes; ESI-MS; Fundamental and applied biological sciences. Psychology; GIPLS; Glycoinositolphospholipids; Glycolipids - chemistry; Glycolipids - physiology; glycophospholipids; glycosylphosphatidylinositol; GPI; hematophagous insects; host-parasite relationships; Humans; Immunohistochemistry; infection; insect vectors; Insect Vectors - parasitology; Life cycle. Host-agent relationship. Pathogenesis; lipopeptidophosphoglycan; lipophosphoglycan; LPG; LPPG; Microscopy, Confocal; Microscopy, Video; Midgut; perimicrovillar membranes; Phospholipids - chemistry; Phospholipids - physiology; PMM; Protozoa; Rabbits; Rhodnius - parasitology; Rhodnius prolixus; Spectrometry, Mass, Electrospray Ionization; TFA; Triatomid–parasite interaction; trifluoroacetic acid; Trypanosoma cruzi; Trypanosoma cruzi - chemistry; Trypanosoma cruzi - drug effects; Trypanosoma cruzi - physiology; β-Gal f; β-Galactofuranose
• ISSN: 0014-4894; 1090-2449
• DOI: 10.1016/j.exppara.2006.12.014

Trypanosoma cruzi epimastigotes adhere in vivo to the luminal surface of their triatomid vector digestive tract by molecular mechanisms, as yet, unknown. Here, we show that the administration of 0.5 μM epimastigote major surface glycoinositolphospholipids (GIPLs) to the infected bloodmeal inhibits up to 90% parasite infection in Rhodnius prolixus. The parasite behavior was investigated in vitro using fragments of the insect midgut. The addition of GIPLs in concentration as low as 50–100 nM impaired 95% the attachment of epimastigotes. Previous treatment of GIPLs with trifluoroacetic acid to remove the terminal β-galactofuranosyl residues reversed 50% the epimastigote in vitro attachment. The binding sites of purified GIPLs on the luminal surface of the posterior midgut were exposed by immunofluorescence microscopy. These observations indicate that GIPLs are one of the components involved in the adhesion of T. cruzi to the luminal insect midgut surface and possibly one of the determinants of parasite infection in the insect vector.