Immunoglobulin response to the low polymorphic Pf113 antigen in children from Lastoursville, South-East of Gabon

Imboumy-Limoukou, Roméo Karl; Maghendi-Nzondo, Sidney; Kouna, Charlene Lady; Bounaadja, Lotfi; Mbang, Sophie; Biteghe, Jean Claude; Eboumbou, Carole; Prugnolle, Franck; Florent, Isabelle; Lékana-Douki, Jean-Bernard

doi:10.1016/j.actatropica.2016.08.014

Cited by 3 publications

(3 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Using antibodies against P113, we could show that it is expressed in early and late-stage schizonts and on the surface of free merozoites by co-staining with the established merozoite surface markers MSP9 ( Fig. 2d ) and MSP1 ( Supplementary Fig.1a ), findings that are consistent with an independent study 30 . Antibodies to P113, unlike those to a marker of the inner membrane complex (MTIP), stained both permeabilized and unpermeabilized merozoites demonstrating P113 is surface localized ( Supplementary Fig.1b ).…”

Section: Resultssupporting

confidence: 89%

P113 is a merozoite surface protein that binds the N terminus of Plasmodium falciparum RH5

et al. 2017

View full text Add to dashboard Cite

Invasion of erythrocytes by Plasmodium falciparum merozoites is necessary for malaria pathogenesis and is therefore a primary target for vaccine development. RH5 is a leading subunit vaccine candidate because anti-RH5 antibodies inhibit parasite growth and the interaction with its erythrocyte receptor basigin is essential for invasion. RH5 is secreted, complexes with other parasite proteins including CyRPA and RIPR, and contains a conserved N-terminal region (RH5Nt) of unknown function that is cleaved from the native protein. Here, we identify P113 as a merozoite surface protein that directly interacts with RH5Nt. Using recombinant proteins and a sensitive protein interaction assay, we establish the binding interdependencies of all the other known RH5 complex components and conclude that the RH5Nt-P113 interaction provides a releasable mechanism for anchoring RH5 to the merozoite surface. We exploit these findings to design a chemically synthesized peptide corresponding to RH5Nt, which could contribute to a cost-effective malaria vaccine.

show abstract

Section: Resultssupporting

confidence: 89%

P113 is a merozoite surface protein that binds the N terminus of Plasmodium falciparum RH5

et al. 2017

View full text Add to dashboard Cite

show abstract

“…The observed dominance by cytophilic IgG sub-classes for all the antigens studied here is also in agreement with most previous studies of humoral immunity to P . falciparum asexual blood-stage antigens following natural exposure [ 19 , 20 , 23 ].…”

Section: Resultsmentioning

confidence: 99%

Kinetics of antibody responses to PfRH5-complex antigens in Ghanaian children with Plasmodium falciparum malaria

et al. 2018

View full text Add to dashboard Cite

Plasmodium falciparum PfRH5 protein binds Ripr, CyRPA and Pf113 to form a complex that is essential for merozoite invasion of erythrocytes. The inter-genomic conservation of the PfRH5 complex proteins makes them attractive blood stage vaccine candidates. However, little is known about how antibodies to PfRH5, CyRPA and Pf113 are acquired and maintained in naturally exposed populations, and the role of PfRH5 complex proteins in naturally acquired immunity. To provide such data, we studied 206 Ghanaian children between the ages of 1–12 years, who were symptomatic, asymptomatic or aparasitemic and healthy. Plasma levels of antigen-specific IgG and IgG subclasses were measured by ELISA at several time points during acute disease and convalescence. On the day of admission with acute P. falciparum malaria, the prevalence of antibodies to PfRH5-complex proteins was low compared to other merozoite antigens (EBA175, GLURP-R0 and GLURP-R2). At convalescence, the levels of RH5-complex-specific IgG were reduced, with the decay of PfRH5-specific IgG being slower than the decay of IgG specific for CyRPA and Pf113. No correlation between IgG levels and protection against P. falciparum malaria was observed for any of the PfRH5 complex proteins. From this we conclude that specific IgG was induced against proteins from the PfRH5-complex during acute P. falciparum malaria, but the prevalence was low and the IgG levels decayed rapidly after treatment. These data indicate that the levels of IgG specific for PfRH5-complex proteins in natural infections in Ghanaian children were markers of recent exposure only.

show abstract

“…Al ser una proteína que carece de un dominio transmembranal y de anclaje Glucosilfosfatidilinositol (GPI) (46), se ha demostrado por estudios de criomicroscopía electrónica (CryoEM) que PfRH5 se une al GR a través de un complejo conformado por el antígeno protector rico en cisteína (CyRPA) y la proteína de interacción con PfRH5 (Ripr) que lo ayudan a anclar a la membrana del GR (Figura 3B) ( 14); por otro lado, la proteína P113 ayuda a PfRH5 a anclarse a la membrana del Mrz a través de una interacción con 19 residuos en el N-terminal (49)(50)(51)(52).…”

Section: Proteína Homologa De Unión a Reticulocito 1 (Pfrh5)unclassified

Proteínas homólogas de unión a reticulocitos de Plasmodium falciparum involucradas en el proceso de invasión al eritrocito: Revisión de la literatura

Royero-Bermeo

Santofimio

Rojas

et al. 2020

Revista Investig. Salud Univ. Boyacá

View full text Add to dashboard Cite

Introducción. La malaria es uno de los mayores retos de salud pública a nivel mundial, es causada principalmente por los parásitos Plasmodium falciparum y Plasmodium vivax. Durante el proceso de invasión, se encuentran involucradas las proteínas homólogas de unión a reticulocitos de Plasmodium falciparum PfRH1, PfRH2a, PfRH2b, PfRH4 y PfRH5, que tras su unión a receptores específicos de membrana permiten la invasión del merozoíto al eritrocito. Objetivo. Compilar y resumir las características moleculares y estructurales de las interacciones entre las proteínas pertenecientes a la familia de proteínas homólogas de unión a reticulocitos de Plasmodium falciparum y los receptores expresados en la célula del hospedero. Método. Revisión descriptiva sobre las proteínas homólogas de unión a reticulocitos de Plasmodium falciparum involucradas en el proceso de invasión al eritrocito. Esta revisión, incluye literatura publicada hasta el año 2020 en bases de datos electrónicas especializadas en investigación biomédica. Se encontraron 105 documentos, de los cuales se seleccionaron 70 y se excluyeron 11 por no presentar los criterios de inclusión, analizando un total de 59 referencias. Conclusión. La invasión del merozoíto es mediada por interacciones específicas de los ligandos de las familias EBL y PfRH. La unión de las proteínas PfRH1 y PfRH2b a sus receptores en el eritrocito, dan lugar a la liberación de la proteína EBL-175, que junto con PfRH4 median la formación de una unión estrecha entre el parásito y los glóbulos rojos, permitiendo así, la unión de la proteína PfRH5 a basigina y la entrada del parásito a la célula del hospedero.

show abstract

Immunoglobulin response to the low polymorphic Pf113 antigen in children from Lastoursville, South-East of Gabon

Cited by 3 publications

References 27 publications

P113 is a merozoite surface protein that binds the N terminus of Plasmodium falciparum RH5

P113 is a merozoite surface protein that binds the N terminus of Plasmodium falciparum RH5

Kinetics of antibody responses to PfRH5-complex antigens in Ghanaian children with Plasmodium falciparum malaria

Proteínas homólogas de unión a reticulocitos de Plasmodium falciparum involucradas en el proceso de invasión al eritrocito: Revisión de la literatura

Contact Info

Product

Resources

About