Pv12, a 6-Cys antigen of Plasmodium vivax, is localized to the merozoite rhoptry

Li, Jian; Ito, Daisuke; Chen, Jun-Hu; Lu, Feng; Cheng, Yang; Wang, Bo; Ha, Kwon‐Soo; Cao, Jun; Torii, Motomi; Sattabongkot, Jetsumon; Tsuboi, Takafumi; Han, Eun‐Taek

doi:10.1016/j.parint.2012.02.008

Cited by 37 publications

(37 citation statements)

References 37 publications

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“…This observation suggests a potential biological function in that apicomplexan proteins that share similar localization are involved in host cell invasion and the establishment of infection. It is noteworthy that a similar apical localization pattern has also been reported in mature schizonts for Pv12, the P. vivax orthologue (56), and in free merozoites for Pf12 (21).…”

Section: Purifying Selection and Apical Localization Of Pf12 Suggest Ansupporting

confidence: 73%

Structural and Biochemical Characterization of Plasmodium falciparum 12 (Pf12) Reveals a Unique Interdomain Organization and the Potential for an Antiparallel Arrangement with Pf41

Tonkin

Arredondo

Loveless

et al. 2013

Journal of Biological Chemistry

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Background: Pf12 is the archetypal member of the 6-Cys protein family, members of which are important Plasmodium vaccine targets. Results: Purifying selection and apical localization of Pf12, crystal structure of tandem 6-Cys domains, and mass spectrometry of cross-linked Pf12-Pf41 heterodimer are shown. Conclusion: A functionally important role for Pf12 and potential for antiparallel heterodimer is provided. Significance: First full-length 6-Cys protein structure and first details of heterodimer organization are revealed.

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Section: Purifying Selection and Apical Localization Of Pf12 Suggest Ansupporting

confidence: 73%

Structural and Biochemical Characterization of Plasmodium falciparum 12 (Pf12) Reveals a Unique Interdomain Organization and the Potential for an Antiparallel Arrangement with Pf41

Tonkin

Arredondo

Loveless

et al. 2013

Journal of Biological Chemistry

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“…Immunofluorescence assays (IFAs) were performed on acetone-fixed parasites as described previously (19). The following primary antibodies (dilutions) were used: rabbit anti-PvMSP1-19 (1:100) and mouse anti-PvMSP1P-42 (1:20).…”

Section: Methodsmentioning

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.…”

mentioning

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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“…16 Among them, 12 GPI-APs (PvMSP-1, PvMSP-4, PvMSP-5, PvMSP-8, PvMSP-10, Pv12, Pv34, Pv38, Pvs25, Pvs28, PvCSP and PvRAMA) have been characterized and some of them have been considered as potential vaccine candidates. [17][18][19][20][21][22][23][24][25] However, the other P. vivax GPI-APs including a hypothetical conserved (HP-C) protein named Pvx_092425 coded by gene PVX_092425 still remain uncharacterized and their precise role also stay unclear. To find novel vaccine candidates of P. vivax, the identification and characterization of new antigens among GPI-APs of P. vivax are considered to be one of the promising strategies.…”

mentioning

confidence: 99%

“…[24][25][26] MSP8, MSP10 and Pv12 were recently identified, and the recombinant proteins were highly recognized by P. vivax infected patient sera. 24,27,28 In contrast to the apical and peripheral classes of blood-stage antigens, the GPI-APs appear to be essential to blood-stage growth, together with considerable data highlighting their potential as targets of protection antibodies, places the merozoite GPI-APs among the most highly validated blood-stage vaccine targets. 29 This study aims to design epitope-based peptides of HP-C protein Pvx_092425 for the utility of vivax malaria vaccine development.…”

mentioning

confidence: 99%

In silicoanalysis for structure, function and T-cell epitopes of a hypothetical conserved (HP-C) protein coded by PVX_092425 inPlasmodium vivax

2015

Pathogens and Global Health

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Objective: Plasmodium spp. merozoite glycosylphosphatidylinositol-anchored proteins (GPI-APs) considered as protective immunogen in novel vaccines against malaria. To analyze the structure and function of a hypothetical conserved (HP-C) GPI-AP coded by gene PVX_092425 from Plasmodium vivax, and find its potential T-cell epitopes for further vivax malaria vaccine study. Methods: The structure, function and T-cell epitopes of the HP-C protein named Pvx_092425 were analyzed and predicted by online and offline bioinformatics software. Results: The bioinformatics data showed that the Pvx_092425 is an 830 amino acid (AA) long polypeptide encoded by five exons gene PVX_092425.It contains a pectin lyase-like superfamily, an AA repeats region, a cys-rich region and a transmembrane domain (TM) in C-terminal region. The alignment analysis drew it has a unique AA repeats region among Plasmodium spp. It was located in the cytoplasm, secretory system or cellular nucleus of P. vivax merozoite. For the sequence, the fragment of I823-V829 inserts in the interior side of the membrane, and M1--A812 belongs to the cytoplasmic tail. It has seven protein-protein binding sites. The peptides with the best predicted binding affinities were human leucocyte antigen (HLA) HLA-A * 0203, HLA-DRB1 * 0101 and HLA-DRB1 * 0701.Among these predicted peptides, 582FLWDKALFD590 epitope interacted with HLA-DRB1 * 0101 allele showed best binding affinity compared to others. Structural analysis explained that the epitope fits well into the epitope-binding groove of HLA-DRB1 * 0101. Conclusions: It proposes that the Pvx_092425 plays a key role during erythrocyte stage and generates information that is useful for development of blood-stage vaccine to block the merozoites invasion.

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Pv12, a 6-Cys antigen of Plasmodium vivax, is localized to the merozoite rhoptry

Cited by 37 publications

References 37 publications

Structural and Biochemical Characterization of Plasmodium falciparum 12 (Pf12) Reveals a Unique Interdomain Organization and the Potential for an Antiparallel Arrangement with Pf41

Structural and Biochemical Characterization of Plasmodium falciparum 12 (Pf12) Reveals a Unique Interdomain Organization and the Potential for an Antiparallel Arrangement with Pf41

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

In silicoanalysis for structure, function and T-cell epitopes of a hypothetical conserved (HP-C) protein coded by PVX_092425 inPlasmodium vivax

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