ArticleScientific reports2013
The α-helical regions of KERP1 are important in Entamoeba histolytica adherence to human cells.
Article in Scientific reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
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- A Review: Natural and Synthetic Compounds TargetingMembranes · 2022Review
- Review
- Entamoeba histolytica under Oxidative Stress: What Countermeasure Mechanisms Are in Place?Cells · 2017Review
- Identification of S-Nitrosylated (SNO) Proteins inFrontiers in cellular and infection microbiology · 2017Article
- Chew on this: amoebic trogocytosis and host cell killing by Entamoeba histolytica.Trends in parasitology · 2015Review
- The Minor Capsid Protein VP11 of Thermophilic Bacteriophage P23-77 Facilitates Virus Assembly by Using Lipid-Protein Interactions.Journal of virology · 2015Article
- Integrating computational modeling and functional assays to decipher the structure-function relationship of influenza virus PB1 protein.Scientific reports · 2014Article
- Evolutionary genomics and population structure of Entamoeba histolytica.Computational and structural biotechnology journal · 2014Review
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
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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