Literature DB >> 18191882

Studies of Plasmodium falciparum rhoptry-associated membrane antigen (RAMA) protein peptides specifically binding to human RBC.

Carlos Giovanni Pinzón1, Hernando Curtidor, Adriana Bermúdez, Martha Forero, Magnolia Vanegas, Jorge Rodríguez, Manuel E Patarroyo.   

Abstract

Plasmodium falciparum rhoptry-associated membrane antigen (RAMA) peptides used in normal red blood cell (RBC) binding assays revealed that peptides 33426 (79NINILSSVHRKGRILYDSF97) and 33460 (777HKKREKSISPHSYQKVSTKVQ797) bound with high activity, presenting nanomolar affinity constants. Such high binding activity peptides (HABPs) displayed helicoid and random coil structures as determined by circular dichroism. HABPs inhibited P. falciparumin vitro invasion of normal RBC by up to 61% (depending on concentration), suggesting that some RAMA protein regions could be involved in P. falciparum invasion of RBC. The nature and localisation of receptors on RBC surface responsible for HABP binding were studied using enzyme-treated erythrocytes and structural analysis.

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Year:  2007        PMID: 18191882     DOI: 10.1016/j.vaccine.2007.11.086

Source DB:  PubMed          Journal:  Vaccine        ISSN: 0264-410X            Impact factor:   3.641


  6 in total

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6.  The Plasmodium falciparum rhoptry bulb protein RAMA plays an essential role in rhoptry neck morphogenesis and host red blood cell invasion.

Authors:  Emma S Sherling; Abigail J Perrin; Ellen Knuepfer; Matthew R G Russell; Lucy M Collinson; Louis H Miller; Michael J Blackman
Journal:  PLoS Pathog       Date:  2019-09-06       Impact factor: 6.823

  6 in total

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