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

Autor(es)

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]

Afiliação do(s) autor(es)

^[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

• Tipo de documento: Artigo Científico
• Fonte: BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES; v. 1862, n. 3 MAR 1 2020.
• Citações Web of Science: 0

Resumo

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)

• Processo FAPESP: 14/09361-9 - Estudo dos genes de micro-exon (MEGs) do parasita humano Schistosoma mansoni e da interação de seus produtos protéicos com células humanas
• Beneficiário: Ricardo de Marco
• Modalidade de apoio: Auxílio à Pesquisa - Regular
• Processo FAPESP: 14/00206-0 - Estrutura e função dos peptídeos de fusão da glicoproteína spike do SARS-CoV
• Beneficiário: Luís Guilherme Mansor Basso
• Modalidade de apoio: Bolsas no Brasil - Pós-Doutorado
• Processo FAPESP: 18/19546-7 - Mecanismos moleculares da ligação, inserção e orientação de peptídeos antimicrobianos em modelos de membrana
• Beneficiário: Jose Luiz de Souza Lopes
• Modalidade de apoio: Auxílio à Pesquisa - Regular
• Processo FAPESP: 15/50347-2 - Estudos biofísicos da estrutura/função de peptídeos antimicrobianos e enzimas isoladas de organismos extremófilos
• Beneficiário: Ana Paula Ulian de Araujo
• Modalidade de apoio: Auxílio à Pesquisa - Regular