Journal article
An unusual tryptophan-rich domain characterizes two secreted antigens of Plasmodium yoelii-infected erythrocytes
Molecular and biochemical parasitology, v 110(1), pp 11-21
2000
PMID: 10989141
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Abstract
Previously, we reported the characterization of pypAg-1, a novel protective membrane protein of
Plasmodium yoelii-infected erythrocytes. Immunization studies indicated that pypAg-1 contained at least two protective epitopes. One of these determinants was associated with the N-terminal portion of pypAg-1, that also included a 220 amino acid domain unusually rich in tryptophan residues. Using sera from mice immunized against
P. yoelii, we have identified a second related antigen, pypAg-3. The
pypag-3 cDNA encodes a 43 kDa blood-stage protein that is also characterized by the presence of a 220 residue tryptophan-rich domain. Of particular interest, sequence comparisons revealed that 24 tryptophan residues are positionally conserved between pypAg-1 and pypAg-3. Otherwise, the two antigens share limited sequence similarity. Full-length recombinant pypAg-3 was expressed, purified and used to produce a high titer polyclonal rabbit antiserum. As with pypAg-1, immunofluorescence studies showed that pypAg-3 is expressed in the cytoplasm and associated with the membrane of
P. yoelii infected erythrocytes. In addition, pypAg-1 and pypAg-3 appear to be secreted proteins, as both were detected in culture supernatants of
P. yoelii-infected erythrocytes. Finally, metabolically labeled pypAg-1 and pypAg-3 secreted from parasitized cells bind to the surface of uninfected, normal mouse erythrocytes. As such, the conservation of the unusual tryptophan-rich domain between two blood-stage malarial proteins with similar biological properties suggests that it may be important for protein export and/or function.
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Details
- Title
- An unusual tryptophan-rich domain characterizes two secreted antigens of Plasmodium yoelii-infected erythrocytes
- Creators
- James M BurnsEric K AdeekuCarla C BelkPatricia D Dunn
- Publication Details
- Molecular and biochemical parasitology, v 110(1), pp 11-21
- Publisher
- Elsevier
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Microbiology and Immunology
- Web of Science ID
- WOS:000089493300002
- Scopus ID
- 2-s2.0-0033827906
- Other Identifier
- 991014877911504721
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InCites Highlights
Data related to this publication, from InCites Benchmarking & Analytics tool:
- Web of Science research areas
- Biochemistry & Molecular Biology
- Parasitology