Abstract
The structure of the Ascaris allergen, ABA-1 was characterized at several levels. Purified allergen monomers eluted from reducing PAGE were found to reassociate into dimers in phosphate buffered saline containing 0.9 mM Ca2+. This association may involve the formation of disulfide bonds between monomers. The primary amino acid sequence was used to predict secondary structure and compare the allergen to other known proteins sequences. ABA-1 appears to be highly helical protein of two domains. Sequence analysis reveals short regions (25 amino acids) of high homology (76%) between ABA-I and the major body wall myosin of Onchocerca volvulus. In addition, ABA-1 has sequence similarity to a family of EF-hand containing calcium binding proteins called S100 proteins. The dimerization and two-domain structure of ABA- 1 is consistant with the possibility that ABA-1 is a member of the S100 family of calcium binding proteins.
| Translated title of the contribution | Structural characteristics of the Ascaris allergen, ABA-1 |
|---|---|
| Original language | French |
| Pages (from-to) | 41-48 |
| Number of pages | 8 |
| Journal | Parasite |
| Volume | 2 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - Mar 1995 |
| Externally published | Yes |
ASJC Scopus Subject Areas
- Parasitology
- Animal Science and Zoology
- veterinary (miscalleneous)
- Insect Science
- Infectious Diseases
PubMed: MeSH publication types
- Journal Article
- Research Support, Non-U.S. Gov't
