Atomic fidelity of subunit-based chemically-synthesized antimalarial vaccine components

Manuel E. Patarroyo, Gladys Cifuentes, Nora L. Martínez, Manuel A. Patarroyo

Research output: Contribution to journalReview articlepeer-review

14 Scopus citations

Abstract

The tri-dimensional (3D) structure determined by NMR of functionally relevant High Activity Binding Peptides (HABPs) of chemically-synthesized malarial proteins, involved in invasion to target cells, is practically identical, at the atomic level, to their corresponding recombinantly produced proteins, determined by X-ray crystallography. Both recombinant proteins as well as these chemically-synthesized HABPs bind to host-cell receptors through channels or troughs formation, stabilized by hydrogen bonding; most of them are located on distant segments to the highly polymorphic, highly antigenic, strain specific amino acid sequences the parasite uses to evade immune pressure. When these immunologically silent conserved HABPs are specifically modified, they become highly immunogenic and capable of inducing protective immune responses, supporting the specifically modified minimal subunit-based, multiepitopic, chemically-synthesized vaccines concept.

Original languageEnglish (US)
Pages (from-to)38-44
Number of pages7
JournalProgress in Biophysics and Molecular Biology
Volume102
Issue number1
DOIs
StatePublished - Jan 2010

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Molecular Biology

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