Abstract |
The circumsporozoite protein of the human malaria parasite Plasmodium falciparum contains multiple tandem repeats of the amino acid sequence Asn-Ala- Asn-Pro. The repeated sequence encompasses the immunodominant region of the protein, and antibodies raised against it are potent inhibitors of invasion and development of sporozoites in cultured hepatocytes. Using a modified build-up procedure, we have explored a large number of possible helical and near-helical conformations of a terminally blocked tetraicosapeptide, consisting of six repeats of the sequence Asn-Ala- Asn-Pro, and conclude that two helical conformations are energetically favored to the exclusion of all others. One of these conformations is longer, thinner, and left-handed and is likely to be adopted in nonpolar environments, while the other is shorter, broader, and right-handed and should be favored in aqueous solutions. We propose that the immunodominant region of the circumsporozoite protein of P. falciparum adopts one of these conformations in vivo.
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Authors | K D Gibson, H A Scheraga |
Journal | Proceedings of the National Academy of Sciences of the United States of America
(Proc Natl Acad Sci U S A)
Vol. 83
Issue 15
Pg. 5649-53
(Aug 1986)
ISSN: 0027-8424 [Print] United States |
PMID | 2426702
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, Non-P.H.S., Research Support, U.S. Gov't, P.H.S.)
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Chemical References |
- Antigens, Protozoan
- Antigens, Surface
- Epitopes
- Peptides
- Solvents
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Topics |
- Amino Acid Sequence
- Animals
- Antigens, Protozoan
(analysis)
- Antigens, Surface
(analysis)
- Epitopes
- Models, Molecular
- Peptides
- Plasmodium falciparum
(immunology)
- Protein Conformation
- Solvents
- Thermodynamics
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