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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

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Author(s):
Felizatti, Ana P. [1] ; Zeraik, Ana E. [1] ; Basso, Luis G. M. [2] ; Kumagai, Patricia S. [1] ; Lopes, Jose L. S. [3] ; Wallace, B. A. [4] ; Araujo, Ana P. U. [1] ; DeMarco, Ricardo [1]
Total Authors: 8
Affiliation:
[1] Univ Sao Paulo, Inst Fis Sao Carlos, Av Joao Dagnone 1100, BR-13563120 Sao Carlos, SP - Brazil
[2] Univ Sao Paulo, Fac Filosofia Ciencias & Letras Ribeirao Preto, Av Bandeirantes 3900, BR-14040901 Ribeirao Preto, SP - Brazil
[3] Univ Sao Paulo, Inst Fis, Rua Matao 1371, BR-05508090 Sao Paulo, SP - Brazil
[4] Univ London, Birkbeck Coll, Inst Struct & Mol Biol, Malet St, London WC1E 7HX - England
Total Affiliations: 4
Document type: Journal article
Source: BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES; v. 1862, n. 3 MAR 1 2020.
Web of Science Citations: 0
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 a-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 a-helical membrane active peptides. (AU)

FAPESP's process: 14/09361-9 - Study of micro-exon genes (MEGs) of the human parasite Schistosoma mansoni and of the interaction of their protein products with human cells
Grantee:Ricardo de Marco
Support Opportunities: Regular Research Grants
FAPESP's process: 14/00206-0 - Structure and function of SARS-CoV spike glycoprotein fusion peptides
Grantee:Luís Guilherme Mansor Basso
Support Opportunities: Scholarships in Brazil - Post-Doctoral
FAPESP's process: 18/19546-7 - Molecular mechanisms of the binding, insertion, and orientation of antimicrobial peptides in model membranes
Grantee:Jose Luiz de Souza Lopes
Support Opportunities: Regular Research Grants
FAPESP's process: 15/50347-2 - Biophysical studies of the structure/function of antimicrobial peptides and enzymes isolated from extremophile organisms
Grantee:Ana Paula Ulian de Araujo
Support Opportunities: Regular Research Grants