Defective sorting of the thrombospondin-related anonymous protein (TRAP) inhibits Plasmodium infectivity

Thrombospondin-related anonymous protein (TRAP) is a type 1 transmembrane protein that plays an essential role in gliding motility and cell invasion by Plasmodium sporozoites. It is stored in micronemes-secretory organelles located primarily in the apical end of the parasites and is also found on th...

Full description

Saved in:
Bibliographic Details
Published in:Molecular and biochemical parasitology 2003-02, Vol.126 (2), p.263-273
Main Authors: Bhanot, Purnima, Frevert, Ute, Nussenzweig, Victor, Persson, Cathrine
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Fluorescent Antibody Technique, Indirect
Infectivity
Localization
Microscopy, Immunoelectron
Molecular Sequence Data
Mutagenesis, Insertional
Open Reading Frames
Plasmodium
Plasmodium - pathogenicity
Plasmodium - physiology
Plasmodium - ultrastructure
Protozoan Proteins - genetics
Protozoan Proteins - physiology
Recombinant Proteins - metabolism
Sequence Alignment
Sequence Homology, Amino Acid
Sorting
Thrombospondins - physiology
Toxoplasma - genetics
TRAP
Tyrosine-motif
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Thrombospondin-related anonymous protein (TRAP) is a type 1 transmembrane protein that plays an essential role in gliding motility and cell invasion by Plasmodium sporozoites. It is stored in micronemes-secretory organelles located primarily in the apical end of the parasites and is also found on the parasite surface. The mechanisms that target TRAP and other sporozoite proteins to micronemes and subsequently to the parasite surface are not known. Here we report that the micronemal and surface localization of TRAP requires a tyrosine-based motif located in its cytoplasmic tail. This motif is analogous to the YXXΦ motif (Y: tyrosine, X: any amino acid; Φ: hydrophobic amino acid) that targets eukaryotic proteins to certain sub-cellular compartments and to the plasma membrane. Abrogating the Y motif substantially reduces micronemal and cell surface localization of TRAP. The infectivity of mutant parasites is substantially inhibited. However, there is no significant difference in the amounts of TRAP secreted into the culture medium by wild type and mutant parasites, suggesting that TRAP destined for secretion bypasses micronemal localization.
ISSN:0166-6851
1872-9428
DOI:10.1016/S0166-6851(02)00295-5