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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Duclos, Bertrand Ricard-blum, Sylvie Launay, Guillaume Lisacek, Frédérique Peysselon, Franck |
| Description | Author Affiliation: Peysselon F ( UMR 5086 CNRS, Université Lyon 1, Bases Moléculaires et Structurales des Systèmes Infectieux, 7 passage du Vercors, 69367 Lyon Cedex 07, France. Electronic address: franck.peysselon@ibcp.fr.) |
| Abstract | Leishmaniasis is a vector-borne disease caused by the protozoa Leishmania . We have analyzed and compared the sequences of three experimental exoproteomes of Leishmania promastigotes from different species to determine their specific features and to identify new candidate proteins involved in interactions of Leishmania with the host. The exoproteomes differ from the proteomes by a decrease in the average molecular weight per protein, in disordered amino acid residues and in basic proteins. The exoproteome of the visceral species is significantly enriched in sites predicted to be phosphorylated as well as in features frequently associated with molecular interactions (intrinsic disorder, number of disordered binding regions per protein, interaction and/or trafficking motifs) compared to the other species. The visceral species might thus have a larger interaction repertoire with the host than the other species. Less than 10% of the exoproteomes contain heparin-binding and RGD sequences, and ~ 30% the host targeting signal RXLXE/D/Q. These latter proteins might thus be exported inside the host cell during the intracellular stage of the infection. Furthermore we have identified nine protein families conserved in the three exoproteomes with specific combinations of Pfam domains and selected eleven proteins containing at least three interaction and/or trafficking motifs including two splicing factors, phosphomannomutase, 2,3-bisphosphoglycerate-independent phosphoglycerate mutase, the paraflagellar rod protein-1D and a putative helicase. Their role in host– Leishmania interactions warrants further investigation but the putative ATP-dependent DEAD/H RNA helicase, which contains numerous interaction motifs, a host targeting signal and two disordered regions, is a very promising candidate. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 12 |
| Volume Number | 1834 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2013-12-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Host-Pathogen Interactions Physiology Leishmania Protein Sorting Signals Proteome Secretion Protozoan Proteins Amino Acid Motifs Animals Genetics Pathogenicity Leishmaniasis Metabolism Protein Structure, Tertiary Species Specificity Research Support, Non-U.S. Gov't Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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