Journal article
Remarks on the phylogeny and structure of fatty acid binding proteins from parasitic platyhelminths
International journal for parasitology, v 27(9), pp 1013-1023
1997
PMID: 9363483
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Four fatty acid binding proteins (FABPs) have been described in 4 parasitic platyhelminths:
Schistosoma mansoni, Schistosoma japonicum, Fasciola hepatica and
Echinococcus granulosus. FABPs form a multigenic family of cytosolic proteins widely distributed in metazoan tissues, the function of which is still poorly understood. These helminth proteins have recently received attention, since there are reports to indicate that
S. mansoni and
F. hepatica FABPs may be protective antigens. In addition, these proteins could play a major role in the parasites' life-cycles because platyhelminths are unable to synthesize
de novo most of their lipids. We have undertaken phylogenetic and structural analyses of platyhelminth FABPs in an attempt to characterize features of biological relevance. Phylogenetically, these FABPs appear to be more closely related to those of vertebrate heart, mammary gland, muscle, retina, skin, brain and myelin, although no clear functional relationships were established between them. We describe several conserved motifs characteristic of specific groups of FABPs. Hydrophilicity, flexibility and accessibility analyses revealed several major putative epitopes for the
E. granulosus FABP, EgDf1, that appear to be centred in loops of the EgDf1 3-dimensional structure modelled by molecular replacement.
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Details
- Title
- Remarks on the phylogeny and structure of fatty acid binding proteins from parasitic platyhelminths
- Creators
- Adriana Esteves - University of the RepublicLeo Joseph - Academy of Natural Sciences of Drexel UniversityMargot Paulino - University of the RepublicRicardo Ehrlich - University of the RepublicRachel Laura Ehrlich - Microbiology and Immunology
- Publication Details
- International journal for parasitology, v 27(9), pp 1013-1023
- Publisher
- Elsevier
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Microbiology and Immunology
- Web of Science ID
- WOS:A1997YB68600004
- Scopus ID
- 2-s2.0-0030880549
- Other Identifier
- 991019167855804721
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- Collaboration types
- Domestic collaboration
- International collaboration
- Web of Science research areas
- Parasitology