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© Institut Pasteur
Structure de macromolécules : dimère d'aquométhémoglobine de cheval. Dérivé toxique oxydé de l'hémoglobine, représentant 1 à 2% du total.
Publication : Scientific reports

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

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Scientific reports - 30 Jan 2013

Perdomo D, Baron B, Rojo-Domínguez A, Raynal B, England P, Guillén N

Link to Pubmed [PMID] – 23378906

Sci Rep 2013;3:1171

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.

http://www.ncbi.nlm.nih.gov/pubmed/23378906