Identification and characterisation of the Plasmodium vivax rhoptry-associated protein 2

Patarroyo, Manuel A.; Pérez-Leal, Oscar; López, Yolanda; Cortés, Jimena; Rojas-Caraballo, José; Gómez, Alexander; Moncada, Camilo; Rosas, Juan M.; Patarroyo, Manuel Elkín

doi:10.1016/j.bbrc.2005.09.120

Cited by 24 publications

(15 citation statements)

References 38 publications

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“…Therefore, extensive research is underway to identify and characterize additional potential vaccine antigens from P. vivax . In recent years, several P. vivax antigens have been identified and characterized, including apical membrane antigen‐1 (PvAMA1), Duffy‐binding protein (PvDBP), circumsporozoite protein (PvCSP), rhoptry‐associated protein 1 (PvRAP‐1), rhoptry‐associated protein 2 (PvRAP‐2), reticulocytes‐binding proteins 1 and 2 (PvRBP‐1 and PvRBP‐2), surface protein 25 (PvS25), merozoite surface protein 1 (PvMSP1), PvMSP3 (α, β and γ), PvMSP8, MSP10, tryptophan‐rich antigens PvTRAg and PvTARAg55 (6–16).…”

Section: Details Of Th1 and Th2 Cytokines Levels In 16 P Vivax‐exposmentioning

confidence: 99%

Cellular immune responses to recombinant Plasmodium vivax tryptophan‐rich antigen (PvTRAg) among individuals exposed to vivax malaria

Alam¹,

Bora²,

Mittra³

et al. 2008

Parasite Immunology

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Plasmodium vivax, the most widespread species of human malaria parasite responsible for 70-80 million cases each year requires a vaccine. In recent years, many potential vaccine candidate antigens have been identified from P. vivax including PvTRAg. We describe here cellular immune response to recombinant PvTRAg expressed in Escherichia coli. The in vitro stimulation of PBMCs derived from P. vivax-exposed individuals (n = 16) showed strong proliferative response (SI > 2.2) to PvTRAg as compared to PBMCs from normal healthy controls (n = 8). Although both Th1 (IFN-gamma, TNF-alpha and IL-12) and Th2 (IL-4 and IL-10) cytokines were secreted by the PBMCs of the P. vivax-exposed individuals in response to PvTRAg, the overall response was more inclined towards Th2. In conclusion, recombinant PvTRAg was found to elicit strong cellular immune response among the P. vivax-exposed individuals.

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Section: Details Of Th1 and Th2 Cytokines Levels In 16 P Vivax‐exposmentioning

confidence: 99%

Cellular immune responses to recombinant Plasmodium vivax tryptophan‐rich antigen (PvTRAg) among individuals exposed to vivax malaria

Alam¹,

Bora²,

Mittra³

et al. 2008

Parasite Immunology

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“…To date, five P. vivax rhoptry proteins (RAP1 (Perez-Leal et al, 2006), RAP 2 (Patarroyo et al, 2005), RhopH3 (Mongui et al, 2007), Pv38 (Mongui et al, 2008), Pv34 (Mongui et al, 2009)) have been described by screening the complete P. vivax genome sequence (Carlton et al, 2008) and using a P. vivax strain adapted to Aotus monkeys as a source for parasite DNA, RNA and proteins (Pico de Coana et al, 2003). The characterized proteins might play an important role in human reticulocyte invasion and some of them have been evaluated as vaccine candidates in the Aotus animal model (Rojas-Caraballo et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

Identifying and characterizing a member of the RhopH1/Clag family in Plasmodium vivax

Moreno-Pérez

Mongui

Soler

et al. 2011

Gene

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“…These include proteins associated with merozoite surface and invasive organelles such as merozoite surface proteins (MSP1 [25], MSP5 [26], MSP7 [27], and MSP8 [28]), apical membrane antigen 1 (AMA1) [29], reticulocyte binding protein [30], rhoptry proteins (RAP1 [31], RAP 2 [32], RhopH2, EXP2, and CLAG), and actinomyosin motors (actin, myosin) [33-35]. The parasite samples also contained gametocytes and several sexual stage proteins were detected, including the P. falciparum orthologs of male fertility protein Pf47 (PVX_083240), Pfs16 (PVX_000930) and transmission-blocking vaccine candidate Pfs230 (PVX_000995) [36-38].…”

Section: Resultsmentioning

confidence: 99%

Determination of the Plasmodium vivax schizont stage proteome

Roobsoong

Roytrakul

Sattabongkot

et al. 2011

Journal of Proteomics

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With the genome of the malaria parasite Plasmodium vivax sequenced, it is important to determine the proteomes of the parasite in order to assist efforts in antigen and drug target discovery. Since a method for continuous culture of P. vivax parasite is not available, we tried to study the proteome of the erythrocytic stages using fresh parasite isolates from patients. In schizont-enriched samples, 316 proteins were confidently identified by tandem mass spectrometry. Almost 50% of the identified proteins were hypothetical, while other major categories include proteins with binding function, protein fate, protein synthesis, metabolism and cellular transport. To identify proteins that are recognized by host humoral immunity, parasite proteins were separated by two-dimensional gel electrophoresis and screened by Western blot using an immune serum from a P. vivax patient. Mass spectrometry analysis of protein spots recognized by the serum identified four potential antigens including PV24. The recombinant protein PV24 was recognized by antibodies from vivax malaria patients even during the convalescent period, indicating that PV24 could elicit long-lasting antibody responses in P. vivax patients.

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Identification and characterisation of the Plasmodium vivax rhoptry-associated protein 2

Cited by 24 publications

References 38 publications

Cellular immune responses to recombinant Plasmodium vivax tryptophan‐rich antigen (PvTRAg) among individuals exposed to vivax malaria

Cellular immune responses to recombinant Plasmodium vivax tryptophan‐rich antigen (PvTRAg) among individuals exposed to vivax malaria

Identifying and characterizing a member of the RhopH1/Clag family in Plasmodium vivax

Determination of the Plasmodium vivax schizont stage proteome

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