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Structure of a malaria parasite antigenic determinant displayed on filamentous bacteriophage determined by NMR spectroscopy: Implications for the structure of continuous peptide epitopes of proteins

¹ Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA
² Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California 92093, USA
³ Cambridge Centre for Molecular Recognition, Department of Biochemistry, University of Cambridge, Cambridge CB2 1GA, England, UK

Reprint requests to: Dr. Stanley J. Opella, Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093; e-mail: sopella{at}ucsd.edu; fax: (858) 822-4821.

The NANP repeating sequence of the circumsporozoite protein of Plasmodium falciparum was displayed on the surface of fd filamentous bacteriophage as a 12-residue insert (NANP)₃ in the N-terminal region of the major coat protein (pVIII). The structure of the epitope determined by multidimensional solution NMR spectroscopy of the modified pVIII protein in lipid micelles was shown to be a twofold repeat of an extended and non-hydrogen-bonded loop based on the sequence NPNA, demonstrating that the repeating sequence is NPNA, not NANP. Further, high resolution solid-state NMR spectra of intact hybrid virions containing the modified pVIII proteins demonstrate that the peptides displayed on the surface of the virion adopt a single, stable conformation; this is consistent with their pronounced immunogenicity as well as their ability to mimic the antigenicity of their native parent proteins.

Keywords: Peptide epitope; phage display; NMR spectroscopy; malaria; vaccine

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This article has been cited by other articles:

				M. U. Ferreira, M. da Silva Nunes, and G. Wunderlich Antigenic Diversity and Immune Evasion by Malaria Parasites Clin. Vaccine Immunol., November 1, 2004; 11(6): 987 - 995. [Full Text] [PDF]