Plasmodium vivax merozoite surface protein 8 cloning, expression, and characterisation

Pérez-Leal, Oscar; Sierra, Adriana Y.; Barrero, Carlos; Moncada, Camilo; Martínez, Pilar; Cortés, Jimena; López, Yolanda; Torres, Elizabeth Aparecida Ferraz da Silva; Salazar, Luz Mary; Patarroyo, Manuel A.

doi:10.1016/j.bbrc.2004.09.202

Cited by 40 publications

(26 citation statements)

References 21 publications

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“…However, our preliminary findings indicate that rPyMSP-8 does bind to the surface of normocytes, as well as reticulocytes (Shi and Burns, unpublished observations). Perez-Leal et al (47) have also reported that P. vivax blood-stage parasites, which are known to infect only reticulocytes, do express P. vivax MSP-8.…”

Section: Discussionmentioning

confidence: 97%

Alteration in Host Cell Tropism Limits the Efficacy of Immunization with a Surface Protein of Malaria Merozoites

et al. 2005

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Immunization with Plasmodium yoelii merozoite surface protein-8 (PyMSP-8) has been shown to protect mice against lethal P. yoelii 17XL malaria. Here we demonstrate that PyMSP-8-specific antibodies preferentially suppress P. yoelii 17XL growth in mature erythrocytes compared to growth in reticulocytes and do not suppress the growth of nonlethal P. yoelii 17X, a parasite that primarily replicates in reticulocytes. The protection against normocyte-associated P. yoelii malaria parasites is mediated by antibodies that recognize conformational epitopes of PyMSP-8 that are nonpolymorphic. We examined changes in gene expression in reticulocyterestricted P. yoelii 17XL parasites that escaped neutralization by PyMSP-8-specific antibodies using P. yoelii DNA microarrays. Of interest, Pymsp-8 gene expression decreased, while the expression of msp-1, msp-7, and several rhoptry protein genes increased. Breakthrough parasites also exhibited increases in the expression of a subset of yir and Pyst-a genes that are predicted to encode polymorphic antigens expressed on the surface of infected erythrocytes. These data suggest that changes in the expression of parasite proteins expressed on the merozoite surface, as well as the surface of infected erythrocytes, may alter host cell tropism and contribute to the ability of malaria parasites to evade merozoite-specific, neutralizing antibodies.

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Section: Discussionmentioning

confidence: 97%

Alteration in Host Cell Tropism Limits the Efficacy of Immunization with a Surface Protein of Malaria Merozoites

et al. 2005

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“…PvMSPs with GPI anchors (PvMSP1, PvMSP5, and PvMSP8) are immunogenic in humans in areas where malaria is endemic (14,15,18,27,32). Acquired immune responses to PvMSP1 suggest that antibodies and cellular immune responses to PvMSP1 are strongly induced during vivax malaria (15,38).…”

Section: Discussionmentioning

confidence: 99%

“…Thirty-one putative GPI-APs from the P. vivax genome have been identified, and 30 of them are predicted to be orthologs of GPI-APs in P. falciparum (13). Among them, only eight GPI-APs (PvMSP-1, -4, -5, -8, and -10, Pv12, Pv34, and Pv38) have been identified as possible blood-stage vaccine candidates (14)(15)(16)(17)(18)(19)(20)(21), and the rest remain uncharacterized.…”

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confidence: 99%

The Plasmodium vivax Merozoite Surface Protein 1 Paralog Is a Novel Erythrocyte-Binding Ligand of P. vivax

et al. 2013

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dMerozoite surface protein 1 of Plasmodium vivax (PvMSP1), a glycosylphosphatidylinositol-anchored protein (GPI-AP), is a malaria vaccine candidate for P. vivax. The paralog of PvMSP1, named P. vivax merozoite surface protein 1 paralog (PvMSP1P; PlasmoDB PVX_099975), was recently identified and predicted as a GPI-AP. The similarities in genetic structural characteristics between PvMSP1 and PvMSP1P (e.g., size of open reading frames, two epidermal growth factor-like domains, and GPI anchor motif in the C terminus) led us to study this protein. In the present study, different regions of the PvMSP1P protein, demarcated based on the processed forms of PvMSP1, were expressed successfully as recombinant proteins [i.e., 83 (A, B, and C), 30, 38, 42, 33, and 19 fragments]. We studied the naturally acquired immune response against each fragment of recombinant PvMSP1P and the potential ability of each fragment to bind erythrocytes. The N-terminal fragment (83A) and two C-terminal fragments (33 and 19) reacted strongly with sera from P. vivax-infected patients, with 50 to 68% sensitivity and 95 to 96% specificity, respectively. Due to colocalization of PvMSP1P with PvMSP1, we supposed that PvMSP1P plays a similar role as PvMSP1 during erythrocyte invasion. An in vitro cytoadherence assay showed that PvMSP1P, especially the 19-kDa C-terminal region, could bind to erythrocytes. We also found that human sera from populations naturally exposed to vivax malaria and antisera obtained by immunization using the recombinant molecule PvMSP1P-19 inhibited in vitro binding of human erythrocytes to PvMSP1P-19. These results provide further evidence that the PvMSP1P might be an essential parasite adhesion molecule in the P. vivax merozoite and is a potential vaccine candidate against P. vivax.

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“…5 Merozoite surface proteins have been characterized and are highly immunogenic in natural infection. [6][7][8][9] Among them, several major vaccine candidate antigens (including MSP1, MSP4, MSP5, MSP8, and MSP10) are either known or presumed glycosylphosphatidylinositol (GPI)-anchored membrane proteins. Plasmodium vivax MSP1 is the largest and most abundant protein on the P. vivax merozoite surface.…”

Section: Introductionmentioning

confidence: 99%

Genetic Polymorphism of Plasmodium vivax msp1p, a Paralog of Merozoite Surface Protein 1, from Worldwide Isolates

Wang¹,

Kaneko²,

Sattabongkot³

et al. 2011

The American Society of Tropical Medicine and Hygiene

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Plasmodium vivax msp1p, a paralog of the candidate vaccine antigen P. vivax merozoite surface protein 1, possesses a signal peptide at its N-terminus and two epidermal growth factor–like domains at its C-terminus with a glycosylphosphatidylinositol attachment site. The msp1p gene locus may have originated by a duplication of the msp1 gene locus in a common ancestor of the analyzed Plasmodium species and lost from P. yoelii, P. berghei, and P. falciparum during their evolutionary history. Full-length sequences of the msp1p gene were generally highly conserved; they had a few amino acid substitutions, one highly polymorphic E/Q-rich region, and a single-to-triple hepta-peptide repeat motif. Twenty-one distinguishable allelic types (A1–A21) of the E/Q-rich region were identified from worldwide isolates. Among them, four types were detected in isolates from South Korea. The length polymorphism of the E/Q-rich region might be useful as a genetic marker for population structure studies in malaria-endemic areas.

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Plasmodium vivax merozoite surface protein 8 cloning, expression, and characterisation

Cited by 40 publications

References 21 publications

Alteration in Host Cell Tropism Limits the Efficacy of Immunization with a Surface Protein of Malaria Merozoites

Alteration in Host Cell Tropism Limits the Efficacy of Immunization with a Surface Protein of Malaria Merozoites

The Plasmodium vivax Merozoite Surface Protein 1 Paralog Is a Novel Erythrocyte-Binding Ligand of P. vivax

Genetic Polymorphism of Plasmodium vivax msp1p, a Paralog of Merozoite Surface Protein 1, from Worldwide Isolates

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