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

Adriana Janneth Bermudez Quintero; Carlos Giovanni Pinzón; Hernando Curtidor Castellanos; Martha Forero; Magnolia Vanegas Murcia; Jorge Rodríguez; Manuel Elkin Patarroyo

doi:10.1016/j.vaccine.2007.11.086

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

Adriana Janneth Bermudez Quintero, Carlos Giovanni Pinzón, Hernando Curtidor Castellanos, Martha Forero, Magnolia Vanegas Murcia, Jorge Rodríguez, Manuel Elkin Patarroyo

School of Medicine and Health Sciences

Research output: Contribution to journal › Research Article › peer-review

19 Scopus citations

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

Original language	English (US)
Pages (from-to)	853-862
Number of pages	10
Journal	Vaccine
Volume	26
Issue number	6
DOIs	https://doi.org/10.1016/j.vaccine.2007.11.086
State	Published - Feb 6 2008

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@article{849841a5d0204c0eb5c206870f0eb245,

title = "Studies of Plasmodium falciparum rhoptry-associated membrane antigen (RAMA) protein peptides specifically binding to human RBC",

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",

author = "{Bermudez Quintero}, {Adriana Janneth} and Pinz{\'o}n, {Carlos Giovanni} and {Curtidor Castellanos}, Hernando and Martha Forero and {Vanegas Murcia}, Magnolia and Jorge Rodr{\'i}guez and Patarroyo, {Manuel Elkin}",

year = "2008",

month = feb,

day = "6",

doi = "10.1016/j.vaccine.2007.11.086",

language = "English (US)",

volume = "26",

pages = "853--862",

journal = "Vaccine",

issn = "0264-410X",

publisher = "Elsevier BV",

number = "6",

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TY - JOUR

T1 - Studies of Plasmodium falciparum rhoptry-associated membrane antigen (RAMA) protein peptides specifically binding to human RBC

AU - Bermudez Quintero, Adriana Janneth

AU - Pinzón, Carlos Giovanni

AU - Curtidor Castellanos, Hernando

AU - Forero, Martha

AU - Vanegas Murcia, Magnolia

AU - Rodríguez, Jorge

AU - Patarroyo, Manuel Elkin

PY - 2008/2/6

Y1 - 2008/2/6

N2 - 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

AB - 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

UR - http://www.sciencedirect.com/science/article/pii/S0264410X07013072?via%3Dihub

U2 - 10.1016/j.vaccine.2007.11.086

DO - 10.1016/j.vaccine.2007.11.086

M3 - Research Article

SN - 0264-410X

VL - 26

SP - 853

EP - 862

JO - Vaccine

JF - Vaccine

IS - 6

ER -

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

Abstract

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