Multiple Plasmodium vivax proteins of Pv-fam-a family interact with human erythrocyte receptor Band 3 and have a role in red cell invasion

Alam, Mohd Shoeb; Zeeshan, Mohammad; Rathore, Sumit; Sharma, Yagya D.

doi:10.1016/j.bbrc.2016.08.096

Cited by 14 publications

(14 citation statements)

References 28 publications

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“…In the current study, tryptophanrich antigen (Pv-fam-a: PVX_112675) expression in Saimiri infection is 37-fold higher than that of Aotus infection. This protein has been shown to bind to erythrocyte receptor, which is chymotrypsinsensitive (47), and it was later identified to be band 3 protein in the erythrocytes (52). Furthermore, of the six tryptophan-rich genes expressed higher in Saimiri than Aotus, five were shown to bind erythrocytes (46)(47)(48) and PVX_090265 was shown to be highly expressed in clinical isolates (53).…”

Section: Differential Expression Of Different Family Members In P Vivaxmentioning

confidence: 99%

Transcriptome profiling ofPlasmodium vivaxinSaimirimonkeys identifies potential ligands for invasion

Gunalan

Sá

Barros

et al. 2019

Proc. Natl. Acad. Sci. U.S.A.

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Unlike the case in Asia and Latin America,Plasmodium vivaxinfections are rare in sub-Saharan Africa due to the absence of the Duffy blood group antigen (Duffy antigen), the only known erythrocyte receptor for theP. vivaxmerozoite invasion ligand, Duffy binding protein 1 (DBP1). However,P. vivaxinfections have been documented in Duffy-negative individuals throughout Africa, suggesting thatP. vivaxmay use ligands other than DBP1 to invade Duffy-negative erythrocytes through other receptors. To identify potentialP. vivaxligands, we compared parasite gene expression inSaimiriandAotusmonkey erythrocytes infected withP. vivaxSalvador I (Sal I). DBP1 bindsAotusbut does not bind toSaimirierythrocytes; thus,P. vivaxSal I must invadeSaimirierythrocytes independent of DBP1. Comparing RNA sequencing (RNAseq) data for late-stage infections inSaimiriandAotuserythrocytes when invasion ligands are expressed, we identified genes that belong to tryptophan-rich antigen and merozoite surface protein 3 (MSP3) families that were more abundantly expressed inSaimiriinfections compared withAotusinfections. These genes may encode potential ligands responsible forP. vivaxinfections of Duffy-negative Africans.

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Section: Differential Expression Of Different Family Members In P Vivaxmentioning

confidence: 99%

Transcriptome profiling ofPlasmodium vivaxinSaimirimonkeys identifies potential ligands for invasion

Gunalan

Sá

Barros

et al. 2019

Proc. Natl. Acad. Sci. U.S.A.

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“…falciparum merozoite surface protein 1 (MSP1) and band 3 is also bound by multiple P . vivax merozoite proteins 15 , 36 , 37 . Although the regions of band 3 involved in the interaction with merozoite proteins are located on extracellular loops different from loop 4 36 , 37 , E658 may modulate RBC invasion by (de)stabilizing the GPA-band 3 complex.…”

Section: Resultsmentioning

confidence: 99%

“…vivax merozoite proteins 15 , 36 , 37 . Although the regions of band 3 involved in the interaction with merozoite proteins are located on extracellular loops different from loop 4 36 , 37 , E658 may modulate RBC invasion by (de)stabilizing the GPA-band 3 complex. In this respect it is worth noting that mouse models genetically deficient for band 3, and consequently lacking the GPA-band 3-protein 4.2 complex, are fully resistant to P .…”

Section: Resultsmentioning

confidence: 99%

Genetic conflicts with Plasmodium parasites and functional constraints shape the evolution of erythrocyte cytoskeletal proteins

Sironi

Forni

Clerici

et al. 2018

Sci Rep

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Plasmodium parasites exerted a strong selective pressure on primate genomes and mutations in genes encoding erythrocyte cytoskeleton proteins (ECP) determine protective effects against Plasmodium infection/pathogenesis. We thus hypothesized that ECP-encoding genes have evolved in response to Plasmodium-driven selection. We analyzed the evolutionary history of 15 ECP-encoding genes in primates, as well as of their Plasmodium-encoded ligands (KAHRP, MESA and EMP3). Results indicated that EPB42, SLC4A1, and SPTA1 evolved under pervasive positive selection and that episodes of positive selection tended to occur more frequently in primate species that host a larger number of Plasmodium parasites. Conversely, several genes, including ANK1 and SPTB, displayed extensive signatures of purifying selection in primate phylogenies, Homininae lineages, and human populations, suggesting strong functional constraints. Analysis of Plasmodium genes indicated adaptive evolution in MESA and KAHRP; in the latter, different positively selected sites were located in the spectrin-binding domains. Because most of the positively selected sites in alpha-spectrin localized to the domains involved in the interaction with KAHRP, we suggest that the two proteins are engaged in an arms-race scenario. This observation is relevant because KAHRP is essential for the formation of “knobs”, which represent a major virulence determinant for P. falciparum.

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“…Some spots exclusively recognized by autoantibodies from anemic vivax patients were identified as band 3 protein, an anion transporter that mediates cell flexibility and shape maintenance 22 . In Plasmodium infections, band 3 acts as a host receptor for interaction with different merozoite proteins such as MSP-1 23 , MSP-9 24 , and tryptophan-rich antigens 25 , 26 . In endemic areas where P. falciparum is the prevalent species, band 3 antibodies seem to be protective because children with higher levels of these antibodies had lower parasitemia than nonimmune ones 27 , 28 .…”

Section: Discussionmentioning

confidence: 99%

Anti-band 3 and anti-spectrin antibodies are increased in Plasmodium vivax infection and are associated with anemia

Mourão

Baptista

Almeida

et al. 2018

Sci Rep

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Clearance of non-infected red blood cells (nRBCs) is one of the main components of anemia associated with Plasmodium vivax malaria. Recently, we have shown that anemic patients with P. vivax infection had elevated levels of anti-RBCs antibodies, which could enhance in vitro phagocytosis of nRBCs and decrease their deformability. Using immunoproteomics, here we characterized erythrocytic antigens that are differentially recognized by autoantibodies from anemic and non-anemic patients with acute vivax malaria. Protein spots exclusively recognized by anemic P. vivax-infected patients were identified by mass spectrometry revealing band 3 and spectrin as the main targets. To confirm this finding, antibody responses against these specific proteins were assessed by ELISA. In addition, an inverse association between hemoglobin and anti-band 3 or anti-spectrin antibodies levels was found. Anemic patients had higher levels of IgG against both band 3 and spectrin than the non-anemic ones. To determine if these autoantibodies were elicited because of molecular mimicry, we used in silico analysis and identified P. vivax proteins that share homology with human RBC proteins such as spectrin, suggesting that infection drives autoimmune responses. These findings suggest that band 3 and spectrin are potential targets of autoantibodies that may be relevant for P. vivax malaria-associated anemia.

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Multiple Plasmodium vivax proteins of Pv-fam-a family interact with human erythrocyte receptor Band 3 and have a role in red cell invasion

Cited by 14 publications

References 28 publications

Transcriptome profiling ofPlasmodium vivaxinSaimirimonkeys identifies potential ligands for invasion

Transcriptome profiling ofPlasmodium vivaxinSaimirimonkeys identifies potential ligands for invasion

Genetic conflicts with Plasmodium parasites and functional constraints shape the evolution of erythrocyte cytoskeletal proteins

Anti-band 3 and anti-spectrin antibodies are increased in Plasmodium vivax infection and are associated with anemia

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