The Plasmodium export element revisited

• Published in: PloS one Vol. 3; no. 2; p. e1560
• Main Authors: Hiss, Jan Alexander, Przyborski, Jude Marek, Schwarte, Florian, Lingelbach, Klaus, Schneider, Gisbert
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 06.02.2008; Public Library of Science (PLoS)
• Subjects: Amino acids; Analysis; Animals; Antigens; Biochemistry/Bioinformatics; Blood; Cell Biology/Membranes and Sorting; Cluster Analysis; Computational Biology; Conservation; Conserved sequence; Erythrocytes; Exports; Hydrophobic and Hydrophilic Interactions; Hydrophobicity; International conferences; Malaria; Molecular biology; Neurosciences; Parasites; Pathology/Cellular Pathology; Peptides; Plasmodium; Plasmodium falciparum; Plasmodium falciparum - chemistry; Protein Sorting Signals; Protein transport; Proteins; Proteome; Proteomes; Proteomics; Protozoan Proteins - chemistry; Trends; Vector-borne diseases; Virulence (Microbiology)
• ISSN: 1932-6203; 1932-6203
• DOI: 10.1371/journal.pone.0001560

We performed a bioinformatical analysis of protein export elements (PEXEL) in the putative proteome of the malaria parasite Plasmodium falciparum. A protein family-specific conservation of physicochemical residue profiles was found for PEXEL-flanking sequence regions. We demonstrate that the family members can be clustered based on the flanking regions only and display characteristic hydrophobicity patterns. This raises the possibility that the flanking regions may contain additional information for a family-specific role of PEXEL. We further show that signal peptide cleavage results in a positional alignment of PEXEL from both proteins with, and without, a signal peptide.