In Entamoeba histolytica, a BspA family protein is required for chemotaxis toward tumour necrosis factor
Authors:Anne Silvestre1, 2, 3, 4, Aurélie Plaze1, 2, Patricia Berthon3, 4, Roman Thibeaux1, 2, Nancy Guillen1, 2 and Elisabeth Labruyère1, 2
doi: 10.15698/mic2015.07.214
Volume 2, pp. 235 to 246, published 06/07/2015.
1 Institut Pasteur, Unité Biologie Cellulaire du Parasitisme, F-75015 Paris, France.
2 INSERM U786, F-75015 Paris, France.
3 INRA, UMR1282 Infectiologie et Santé Publique, F-37380 Nouzilly, France.
4 Université de Tours, UMR1282 Infectiologie et Santé Publique, F-37000 Tours, France.
Keywords:
Entamoeba histolytica, chemotaxi, tumour necrosis factor, BspA protein
Corresponding Author(s):
Conflict of interest statement:
The authors do not have any commercial or other associations that might constitute a conflict of interest.
Please cite this article as:
Anne Silvestre, Aurélie Plaze, Patricia Berthon, Roman Thibeaux, Nancy Guillen, and Elisabeth Labruyère (2015). In Entamoeba histolytica, a BspA family protein is required for chemotaxis toward tumour necrosis factor. Microbial Cell 2(7): 235-246.
© 2015 Silvestre et al. This is an open-access article released under the terms of the Creative Commons Attribution (CC BY) license, which allows the unrestricted use, distribution, and reproduction in any medium, provided the original author and source are acknowledged.
Abstract:
Background: Entamoeba histolytica cell migration is essential for the development of human amoebiasis (an infectious disease characterized by tissue invasion and destruction). The tissue inflammation associated with tumour necrosis factor (TNF) secretion by host cells is a well-documented feature of amoebiasis. Tumour necrosis factor is a chemoattractant for E. histolytica, and the parasite may have a TNF receptor at its cell surface. Methods: confocal microscopy, RNA Sequencing, bioinformatics, RNA antisense techniques and histological analysis of human colon explants were used to characterize the interplay between TNF and E. histolytica. Results: an antibody against human TNF receptor 1 (TNFR1) stained the E. histolytica trophozoite surface and (on immunoblots) binds to a 150-kDa protein. Proteome screening with the TNFR1 sequence revealed a BspA family protein in E. histolytica that carries a TNFR signature domain and six leucine-rich repeats (named here as “cell surface protein”, CSP, in view of its cellular location). Cell surface protein shares structural homologies with Toll-Like receptors, colocalizes with TNF and is internalized in TNF-containing vesicles. Reduction of cellular CSP levels abolished chemotaxis toward TNF and blocked parasite invasion of human colon. Conclusions: there is a clear link between TNF chemotaxis, CSP and pathogenesis.