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The α-helical regions of KERP1 are important in Entamoeba histolytica adherence to human cells

Abstract : The lysine and glutamic acid rich protein KERP1 is a unique surface adhesion factor associated with virulence in the human pathogen Entamoeba histolytica. Both the function and structure of this protein remain unknown to this date. Here, we used circular dichroism, analytical ultracentrifugation and bioinformatics modeling to characterize the structure of KERP1. Our findings revealed that it is an α-helical rich protein organized as a trimer, endowed with a very high thermal stability (Tm = 89.6°C). Bioinformatics sequence analyses and 3D-structural modeling indicates that KERP1 central segments could account for protein trimerization. Relevantly, expressing the central region of KERP1 in living parasites, impair their capacity to adhere to human cells. Our observations suggest a link between the inhibitory effect of the isolated central region and the structural features of KERP1.
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Submitted on : Thursday, January 13, 2022 - 11:17:41 PM
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Perdomo et al KERP1 Sci Rep ja...
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Doranda Perdomo, Bruno Baron, Arturo Rojo-Domínguez, Bertrand Raynal, Patrick England, et al.. The α-helical regions of KERP1 are important in Entamoeba histolytica adherence to human cells. Scientific Reports, Nature Publishing Group, 2013, 3 (1), pp.1171. ⟨10.1038/srep01171⟩. ⟨pasteur-03525604⟩



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