Abstract

Abstract : Recombinant and synthetic peptide technology has allowed new approaches to the study of parasitic diseases. A major benefit of these advances is the ease with which entire genes can be isolated and sequenced at the nucleotide level. This information can help answer questions on genomic organization and evolution. Moreover, we can deduce the entire amino acid sequence of a particular protein without having sufficient protein to visualize on an acrylamide gel. The challenge of translating the nucleotide sequence into a biologically relevant and functional protein remains. We intend to focus attention on a particular way to accomplish that translation, i.e., the use of polypeptides derived from the deduced sequence to probe or model a function or property of the protein. It is often easier to obtain large amounts of relatively pure recombinant or synthetic polypeptides than the original protein. Caveats about the use of such peptides cannot be overstated. Proteins are not simply linear entities but often have essential tertiary and quaternary elements that cannot be duplicated by short peptides. The region selected may be internal in the final protein or processed or modified at an early stage of synthesis. Despite these pitfalls, a substantial insight has been achieved in studies with recombinant and synthetic peptides. Ongoing work in seven laboratories concerned is summarized. Keywords: Antigens, Host-parasite relations, Mice, Plasmodium, Malaria, Reprints.

Full Text
Published version (Free)

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call