Characterization of a novel merozoite surface protein of Plasmodium vivax, Pv41

Cheng, Yang; Lu, Feng; Tsuboi, Takafumi; Han, Eun‐Taek

doi:10.1016/j.actatropica.2013.03.002

Cited by 24 publications

(21 citation statements)

References 27 publications

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“…The expression and subcellular localization profiles for Pv41 are similar to the P. falciparum orthologue, however the apical localization in the merozoite was not reported (Angel et al, 2008; Chen et al, 2010; Cheng et al, 2013). Positive balancing selection was suggested for Pv41, particularly in the C-terminus of parasites from the China-Myanmar border (Wang et al, 2014).…”

Section: 6-cys Proteins In Asexual Erythrocytic Stagesmentioning

confidence: 77%

“…Alternatively, low genetic diversity was found for Pv41 in parasites from Colombia with a few substitutions in the C-terminus under positive selection (Forero-Rodriguez et al, 2014). Pv41 is also recognized by sera from naturally infected individuals and a strong association for protection is reported for Pv41 antibodies in a Papua New Guinean cohort (Chen et al, 2010; Cheng et al, 2013; Franca et al, 2016). …”

Section: 6-cys Proteins In Asexual Erythrocytic Stagesmentioning

confidence: 94%

“…Pv12, the Pf12 orthologue in P. vivax , was shown to be transcribed in schizonts and localized to the surface and rhoptries of merozoites by immunofluorescence (Li et al, 2012; Cheng et al, 2013; Moreno-Perez et al, 2013). The interaction of Pv12 and Pv41 has recently been reported in addition to a novel interaction with PVX_110945 (Hostetler et al, 2015).…”

Section: 6-cys Proteins In Asexual Erythrocytic Stagesmentioning

confidence: 99%

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The s48/45 six-cysteine proteins: mediators of interaction throughout the Plasmodium life cycle

Arredondo

Kappe

2017

International Journal for Parasitology

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During their life cycle Plasmodium parasites rely upon an arsenal of proteins that establish key interactions with the host or vector, and between the parasite sexual stages, with the purpose of ensuring infection, reproduction and proliferation. Among these is a group of secreted or membrane-anchored proteins known as the six-cysteine (6-cys) family. This is a small but important family with only 14 members thus far identified, each stage-specifically expressed during the parasite life cycle. 6-cys proteins often localize at the parasite surface or interface with the host and are conserved in different Plasmodium species. The unifying feature of the family is the s48/45 domain, presumably involved in adhesion and structurally related to Ephrins, the ligands of Eph receptors. The most prominent s48/45 members are currently under functional investigation and are being pursued as vaccine candidates. In this review, we examine what is known about the 6-cys family, their structure and function, and discuss future research directions.

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Section: 6-cys Proteins In Asexual Erythrocytic Stagesmentioning

confidence: 77%

Section: 6-cys Proteins In Asexual Erythrocytic Stagesmentioning

confidence: 94%

Section: 6-cys Proteins In Asexual Erythrocytic Stagesmentioning

confidence: 99%

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The s48/45 six-cysteine proteins: mediators of interaction throughout the Plasmodium life cycle

Arredondo

Kappe

2017

International Journal for Parasitology

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“…In some individuals, IgG levels were equivalent to the immune control plasma pool made from PNG adults, whilst in others no protein-specific IgG was detected. Ten of 11 P. vivax proteins tested are expressed during the blood-stage of the parasite’s lifecycle, and it is likely their proposed location on the surface of merozoites makes them immunogenic targets [14, 32, 33]. PVX_081550 is an exception, as the P. falciparum orthologue of this protein locates to the parasitophorous vacuole, although there is some evidence it may be transferred into the apical organelles of merozoites [34].…”

Section: Discussionmentioning

confidence: 99%

Asymptomatic Plasmodium vivax infections induce robust IgG responses to multiple blood-stage proteins in a low-transmission region of western Thailand

Longley

França

White

et al. 2017

Malar J

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BackgroundThailand is aiming to eliminate malaria by the year 2024. Plasmodium vivax has now become the dominant species causing malaria within the country, and a high proportion of infections are asymptomatic. A better understanding of antibody dynamics to P. vivax antigens in a low-transmission setting, where acquired immune responses are poorly characterized, will be pivotal for developing new strategies for elimination, such as improved surveillance methods and vaccines. The objective of this study was to characterize total IgG antibody levels to 11 key P. vivax proteins in a village of western Thailand.MethodsPlasma samples from 546 volunteers enrolled in a cross-sectional survey conducted in 2012 in Kanchanaburi Province were utilized. Total IgG levels to 11 different proteins known or predicted to be involved in reticulocyte binding or invasion (ARP, GAMA, P41, P12, PVX_081550, and five members of the PvRBP family), as well as the leading pre-erythrocytic vaccine candidate (CSP) were measured using a multiplexed bead-based assay. Associations between IgG levels and infection status, age, and spatial location were explored.ResultsIndividuals from a low-transmission region of western Thailand reacted to all 11 P. vivax recombinant proteins. Significantly greater IgG levels were observed in the presence of a current P. vivax infection, despite all infected individuals being asymptomatic. IgG levels were also higher in adults (18 years and older) than in children. For most of the proteins, higher IgG levels were observed in individuals living closer to the Myanmar border and further away from local health services.ConclusionsRobust IgG responses were observed to most proteins and IgG levels correlated with surrogates of exposure, suggesting these antigens may serve as potential biomarkers of exposure, immunity, or both.Electronic supplementary materialThe online version of this article (doi:10.1186/s12936-017-1826-8) contains supplementary material, which is available to authorized users.

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“…vivax surface proteins have been identified based on their orthologues in P . falciparum [9, 10, 15, 17], and the antibody responses to them have been investigated [18–20]. …”

Section: Introductionmentioning

confidence: 99%

Identification of a novel merozoite surface antigen of Plasmodium vivax, PvMSA180

Muh¹,

Han²,

Nyunt³

et al. 2017

Malar J

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BackgroundAlthough a number of Plasmodium vivax proteins have been identified, few have been investigated as potential vaccine candidates. This study characterized the Plasmodium vivax merozoite surface antigen 180 (PvMSA180, PVX_094920), a novel P. vivax antigenic protein.MethodsThe target gene was amplified as four overlapping domains (D1, D2, D3 and D4) to enable expression of the recombinant protein using cell-free and bacterial expression systems. The recombinant PvMSA180 proteins were used in protein microarrays to evaluate the humoral immune response of 72 vivax-infected patients and 24 vivax-naïve individuals. Antibodies produced in mice against the PvMSA180-D1 and -D4 domains were used to assess the subcellular localization of schizont-stage parasites with immunofluorescence assays. A total of 51 pvmsa180 sequences from 12 countries (41 sequences from PlasmoDB and 6 generated in this study) were used to determine the genetic diversity and genealogical relationships with DNAsp and NETWORK software packages, respectively.ResultsPvMSA180 consists of 1603 amino acids with a predicted molecular mass of 182 kDa, and has a signal peptide at the amino-terminus. A total of 70.8% of patients (51/72) showed a specific antibody response to at least one of the PvMSA180 domains, and 20.8% (15/72) exhibited a robust antibody response to at least three of the domains. These findings suggest that PvMSA180 is targeted by the humoral immune response during natural infection with P. vivax. Immunofluorescence analysis demonstrated that PvMSA180 is localized on the merozoite surface of schizont-stage parasites, and pvmsa180 sequences originating from various geographic regions worldwide showed low genetic diversity. Twenty-two haplotypes were found, and haplotype 6 (Hap_6, 77%) of pvmsa180 was detected in isolates from six countries.ConclusionsA novel P. vivax surface protein, PvMSA180, was characterized in this study. Most of P. vivax-infected patients had specific antibodies against particular antigenic domains, indicating that this protein is immunogenic in naturally exposed populations. Genetic analysis of worldwide isolates showed that pvmsa180 is less polymorphic than other well-known candidates and that some haplotypes are common to several countries. However, additional studies with a larger sample size are necessary to evaluate the antibody responses in geographically separated populations, and to identify the function of PvMSA180 during parasite invasion.Electronic supplementary materialThe online version of this article (doi:10.1186/s12936-017-1760-9) contains supplementary material, which is available to authorized users.

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Characterization of a novel merozoite surface protein of Plasmodium vivax, Pv41

Cited by 24 publications

References 27 publications

The s48/45 six-cysteine proteins: mediators of interaction throughout the Plasmodium life cycle

The s48/45 six-cysteine proteins: mediators of interaction throughout the Plasmodium life cycle

Asymptomatic Plasmodium vivax infections induce robust IgG responses to multiple blood-stage proteins in a low-transmission region of western Thailand

Identification of a novel merozoite surface antigen of Plasmodium vivax, PvMSA180

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