Functional, structural, and immunological compartmentalisation of malaria invasive proteins

Reyes, Claudia; Patarroyo, Manuel Elkin; Vargas, Luis Eduardo; Rodríguez, Luis Eduardo; Patarroyo, Manuel A.

doi:https://doi.org/10.1016/j.bbrc.2006.12.220

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Functional, structural, and immunological compartmentalisation of malaria invasive proteins

https://repository.urosario.edu.co/handle/10336/25937
https://doi.org/10.1016/j.bbrc.2006.12.220

Autores

Reyes, Claudia

Patarroyo, Manuel Elkin

Vargas, Luis Eduardo

Rodríguez, Luis Eduardo

Patarroyo, Manuel A.

Fecha

2007-03-09

Editor

Elsevier

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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.