Atomic fidelity of subunit-based chemically-synthesized antimalarial vaccine components.
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.
Patarroyo
Manuel E
ME
Fundación Instituto de Inmunología de Colombia (FIDIC), Bogotá D.C., Colombia; Universidad Nacional de Colombia, Ciudad Universitaria, Bogotá D.C., Colombia. mepatarr@mail.com <mepatarr@mail.com>
Cifuentes
Gladys
G
Martínez
Nora L
NL
Patarroyo
Manuel A
MA
D000818:Animals; D000962:Antimalarials / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology; D016778:Malaria, Falciparum / Q000188:drug therapy / Q000276:immunology; D010963:Plasmodium falciparum / Q000187:drug effects; D014612:Vaccines / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology
D000962:Antimalarials; D014612:Vaccines