Ítem
Solo Metadatos
Functional, structural, and immunological compartmentalisation of malaria invasive proteins
Título de la revista
Autores
Reyes, Claudia
Patarroyo, Manuel Elkin
Vargas, Luis Eduardo
Rodríguez, Luis Eduardo
Patarroyo, Manuel A.
Fecha
2007-03-09
Directores
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Editor
Elsevier
Citations
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Resumen
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 ?-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.
Palabras clave
Keywords
Malaria , Invasive proteins , Compartmentalisation , Structure
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