Direct interaction between EgFABP1, a fatty acid binding protein from Echinococcus granulosus, and phospholipid membranes.

<h4>Background</h4>Growth and maintenance of hydatid cysts produced by Echinococcus granulosus have a high requirement for host lipids for biosynthetic processes, membrane building and possibly cellular and developmental signalling. This requires a high degree of lipid trafficking facili...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Jorge L Porfido, Gabriela Alvite, Valeria Silva, Malcolm W Kennedy, Adriana Esteves, Betina Corsico
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Arctic medicine. Tropical medicine RC955-962 Public aspects of medicine RA1-1270
Acceso en línea:	https://doaj.org/article/0c5b7c27b92d403689582f36c7b9ad8a
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:0c5b7c27b92d403689582f36c7b9ad8a
record_format	dspace
spelling	oai:doaj.org-article:0c5b7c27b92d403689582f36c7b9ad8a2021-11-18T09:15:39ZDirect interaction between EgFABP1, a fatty acid binding protein from Echinococcus granulosus, and phospholipid membranes.1935-27271935-273510.1371/journal.pntd.0001893https://doaj.org/article/0c5b7c27b92d403689582f36c7b9ad8a2012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23166848/?tool=EBIhttps://doaj.org/toc/1935-2727https://doaj.org/toc/1935-2735<h4>Background</h4>Growth and maintenance of hydatid cysts produced by Echinococcus granulosus have a high requirement for host lipids for biosynthetic processes, membrane building and possibly cellular and developmental signalling. This requires a high degree of lipid trafficking facilitated by lipid transporter proteins. Members of the fatty acid binding protein (FABP) family have been identified in Echinococcus granulosus, one of which, EgFABP1 is expressed at the tegumental level in the protoscoleces, but it has also been described in both hydatid cyst fluid and secretions of protoscoleces. In spite of a considerable amount of structural and biophysical information on the FABPs in general, their specific functions remain mysterious.<h4>Methodology/principal findings</h4>We have investigated the way in which EgFABP1 may interact with membranes using a variety of fluorescence-based techniques and artificial small unilamellar vesicles. We first found that bacterial recombinant EgFABP1 is loaded with fatty acids from the synthesising bacteria, and that fatty acid binding increases its resistance to proteinases, possibly due to subtle conformational changes induced on EgFABP1. By manipulating the composition of lipid vesicles and the ionic environment, we found that EgFABP1 interacts with membranes in a direct contact, collisional, manner to exchange ligand, involving both ionic and hydrophobic interactions. Moreover, we observed that the protein can compete with cytochrome c for association with the surface of small unilamellar vesicles (SUVs).<h4>Conclusions/significance</h4>This work constitutes a first approach to the understanding of protein-membrane interactions of EgFABP1. The results suggest that this protein may be actively involved in the exchange and transport of fatty acids between different membranes and cellular compartments within the parasite.Jorge L PorfidoGabriela AlviteValeria SilvaMalcolm W KennedyAdriana EstevesBetina CorsicoPublic Library of Science (PLoS)articleArctic medicine. Tropical medicineRC955-962Public aspects of medicineRA1-1270ENPLoS Neglected Tropical Diseases, Vol 6, Iss 11, p e1893 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Arctic medicine. Tropical medicine RC955-962 Public aspects of medicine RA1-1270
spellingShingle	Arctic medicine. Tropical medicine RC955-962 Public aspects of medicine RA1-1270 Jorge L Porfido Gabriela Alvite Valeria Silva Malcolm W Kennedy Adriana Esteves Betina Corsico Direct interaction between EgFABP1, a fatty acid binding protein from Echinococcus granulosus, and phospholipid membranes.
description	<h4>Background</h4>Growth and maintenance of hydatid cysts produced by Echinococcus granulosus have a high requirement for host lipids for biosynthetic processes, membrane building and possibly cellular and developmental signalling. This requires a high degree of lipid trafficking facilitated by lipid transporter proteins. Members of the fatty acid binding protein (FABP) family have been identified in Echinococcus granulosus, one of which, EgFABP1 is expressed at the tegumental level in the protoscoleces, but it has also been described in both hydatid cyst fluid and secretions of protoscoleces. In spite of a considerable amount of structural and biophysical information on the FABPs in general, their specific functions remain mysterious.<h4>Methodology/principal findings</h4>We have investigated the way in which EgFABP1 may interact with membranes using a variety of fluorescence-based techniques and artificial small unilamellar vesicles. We first found that bacterial recombinant EgFABP1 is loaded with fatty acids from the synthesising bacteria, and that fatty acid binding increases its resistance to proteinases, possibly due to subtle conformational changes induced on EgFABP1. By manipulating the composition of lipid vesicles and the ionic environment, we found that EgFABP1 interacts with membranes in a direct contact, collisional, manner to exchange ligand, involving both ionic and hydrophobic interactions. Moreover, we observed that the protein can compete with cytochrome c for association with the surface of small unilamellar vesicles (SUVs).<h4>Conclusions/significance</h4>This work constitutes a first approach to the understanding of protein-membrane interactions of EgFABP1. The results suggest that this protein may be actively involved in the exchange and transport of fatty acids between different membranes and cellular compartments within the parasite.
format	article
author	Jorge L Porfido Gabriela Alvite Valeria Silva Malcolm W Kennedy Adriana Esteves Betina Corsico
author_facet	Jorge L Porfido Gabriela Alvite Valeria Silva Malcolm W Kennedy Adriana Esteves Betina Corsico
author_sort	Jorge L Porfido
title	Direct interaction between EgFABP1, a fatty acid binding protein from Echinococcus granulosus, and phospholipid membranes.
title_short	Direct interaction between EgFABP1, a fatty acid binding protein from Echinococcus granulosus, and phospholipid membranes.
title_full	Direct interaction between EgFABP1, a fatty acid binding protein from Echinococcus granulosus, and phospholipid membranes.
title_fullStr	Direct interaction between EgFABP1, a fatty acid binding protein from Echinococcus granulosus, and phospholipid membranes.
title_full_unstemmed	Direct interaction between EgFABP1, a fatty acid binding protein from Echinococcus granulosus, and phospholipid membranes.
title_sort	direct interaction between egfabp1, a fatty acid binding protein from echinococcus granulosus, and phospholipid membranes.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/0c5b7c27b92d403689582f36c7b9ad8a
work_keys_str_mv	AT jorgelporfido directinteractionbetweenegfabp1afattyacidbindingproteinfromechinococcusgranulosusandphospholipidmembranes AT gabrielaalvite directinteractionbetweenegfabp1afattyacidbindingproteinfromechinococcusgranulosusandphospholipidmembranes AT valeriasilva directinteractionbetweenegfabp1afattyacidbindingproteinfromechinococcusgranulosusandphospholipidmembranes AT malcolmwkennedy directinteractionbetweenegfabp1afattyacidbindingproteinfromechinococcusgranulosusandphospholipidmembranes AT adrianaesteves directinteractionbetweenegfabp1afattyacidbindingproteinfromechinococcusgranulosusandphospholipidmembranes AT betinacorsico directinteractionbetweenegfabp1afattyacidbindingproteinfromechinococcusgranulosusandphospholipidmembranes
_version_	1718420885173436416

Direct interaction between EgFABP1, a fatty acid binding protein from Echinococcus granulosus, and phospholipid membranes.

Ejemplares similares