Functional, structural, and immunological compartmentalisation of malaria invasive proteins

Claudia Reyes, Manuel Elkin Patarroyo, Luis Eduardo Vargas, Luis Eduardo Rodríguez, Manuel Alfonso Patarroyo

Research output: Contribution to journalArticlepeer-review

21 Scopus citations

Abstract

Conserved Plasmodium falciparum merozoite high activity binding peptides (HABPs) involved in red blood cell (RBC) invasion which are present in merozoite surface proteins (MSPs) involved in attachment, rolling over RBC, those derived from soluble proteins loosely bound to the membrane, and those present in microneme and rhoptry organelles have an α-helical structure and bind with high affinity to HLA-DR52 molecules. On the contrary, conserved HABPs belonging to molecules anchored to the membrane by a GPI tail, or a transmembranal region, or those molecules presenting PEXEL motifs have a strand, turn or unordered configuration and bind with high affinity to HLA-DR53 molecules. Such functional, cellular, structural, and immunological compartmentalisation has tremendous implications in subunit-based, multi-epitope, synthetic, anti-malarial vaccine development. © 2006 Elsevier Inc. All rights reserved.
Original languageEnglish (US)
Pages (from-to)363-371
Number of pages9
JournalBiochemical and Biophysical Research Communications
DOIs
StatePublished - Mar 9 2007
Externally publishedYes

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