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    Interactions of amphipathic α-helical MEG proteins from Schistosoma mansoni with membranes

    Felizatti, A.P. and Zeraik, A.E. and Basso, L.G.M. and Kumagai, P.S. and Lopes, J.L.S. and Wallace, Bonnie and Araujo, A.P.U. and DeMarco, R. (2019) Interactions of amphipathic α-helical MEG proteins from Schistosoma mansoni with membranes. Biochimica et Biophysica Acta (BBA) - Biomembranes 1862 (3), p. 183173. ISSN 0005-2736.

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    Abstract

    Micro Exon Gene (MEG) proteins are thought to play major roles in the infection and survival of parasitic Schistosoma mansoni worms in host organisms. Here, the physical chemical properties of two small MEG proteins found in the genome of S. mansoni, named MEG-24 and MEG-27, were examined by a combination of biophysical techniques such as differential scanning calorimetry, tensiometry, circular dichroism, fluorescence, and electron spin resonance spectroscopies. The proteins are surface active and structurally arranged as cationic amphipathic α-helices that can associate with lipid membranes and cause their disruption. Upon adsorption to lipid membranes, MEG-27 strongly affects the fluidity of erythrocyte ghost membranes, whereas MEG-24 forms pores in erythrocytes without modifying the ghost membrane fluidity. Whole–mount in situ hybridization experiments indicates that MEG-27 and MEG-24 transcripts are located in the parasite esophagus and subtegumental cells, respectively, suggesting a relevant role of these proteins in the host-parasite interface. Taken together, these characteristics lead us to propose that these MEG proteins may interact with host cell membranes and potentially modulate the immune process using a similar mechanism as that described for α-helical membrane–active peptides.

    Metadata

    Item Type: Article
    Keyword(s) / Subject(s): Micro-exon gene proteins, Schistosoma mansoni, Pore-forming peptide, Peptide-lipid interactions
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    Depositing User: Administrator
    Date Deposited: 15 Jan 2020 09:31
    Last Modified: 16 Jan 2020 09:43
    URI: http://eprints.bbk.ac.uk/id/eprint/30588

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