A 95 kDa protein of <i>Plasmodium vivax</i> and <i>P. cynomolgi</i> visualized by three‐dimensional tomography in the caveola–vesicle complexes (Schüffner's dots) of infected erythrocytes is a member of the PHIST family

Akinyi, Sheila; Hanssen, Eric; Meyer, Esmeralda; Jiang, Jianlin; Korir, Cindy C.; Singh, Balwan; Lapp, Stacey A.; Barnwell, John W.; Tilley, Leann; Galinski, Mary R.

doi:10.1111/j.1365-2958.2012.08060.x

Cited by 65 publications

(82 citation statements)

References 54 publications

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“…Recently, a member of the plasmodium helical interspersed subtelomeric (PHIST) superfamily, which is named PHIST/CVC-81 95 , was identified as a 95-kDa CVC protein and localized on the cytoplasmic side of the CVC tubular extensions. This protein may be essential for the survival of vivax malaria parasites (22). In the current study, we observed that five PvTRAg proteins were partially merged with PvPHIST/CVC-81 95 , indicating the CVC-associated localization of these proteins.…”

Section: Discussionmentioning

confidence: 59%

“…The purity of each recombinant protein was confirmed by SDS-PAGE and Western blot analysis according to protocols described previously (21). We also expressed the helical N terminus of P. vivax, interspersed with the subtelomeric/caveola-vesicle complexes-81 95 (PHIST/ CVC-81 95 ) protein (PVX_093680), which was used as a control caveolavesicle complex (CVC) marker (22), using a pGEX-4T-2 (GE Healthcare) expression vector with a GST tag (data not shown). Protein microarrays.…”

Section: Methodsmentioning

confidence: 99%

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Immunoprofiling of the Tryptophan-Rich Antigen Family in Plasmodium vivax

Wang

Cheng

et al. 2015

Infect Immun

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h Tryptophan-rich antigens (TRAgs) are an antigen family that has been identified in human and rodent malaria parasites. TRAgs have been proposed as candidate antigens for potential vaccines. The Plasmodium vivax TRAg (PvTRAg) family includes 36 members. Each PvTRAg contains a tryptophan-rich (TR) domain in the C-terminal region. In this study, we recombinantly expressed all 36 PvTRAgs using a cell-free expression system, and, for the first time, profiled the IgG antibody responses against all PvTRAgs in the sera from 96 vivax malaria patients and 40 healthy individuals using protein microarray technology. The mean seropositive rate for all PvTRAgs was 60.3%. Among them, nine PvTRAgs were newly identified in this study and showed a seropositive rate of >50%. Five of them, PvTRAg_13, PvTRAg_15, PvTRAg_16, PvTRAg_26, and PvTRAg_29, produced higher levels of IgG antibody, even in low-endemicity countries. In addition, the results of an immunofluorescence analysis suggest that PvTRAgs are, at least in part, associated with caveola-vesicle complexes, a unique structure of P. vivax-infected erythrocytes. The mechanism of formation and the function of these abundant membrane structures are not known. Further investigation aimed at determining the functions of these proteins would lead to a better understanding of the blood-stage biology of P. vivax.

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Section: Discussionmentioning

confidence: 59%

Section: Methodsmentioning

confidence: 99%

Immunoprofiling of the Tryptophan-Rich Antigen Family in Plasmodium vivax

Wang

Cheng

et al. 2015

Infect Immun

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“…Caveola-vesicle complexes (CVCs) are parasite-induced indentations in P. vivax-infected erythrocyte cell membranes. The exact structure, protein composition, and function are not yet fully understood, but CVC-81 95 is exported, is a predominant protein in these CVCs, and is found on tubular extensions going inwards from the CVC (75,76). Its orthologue in P. cynomolgi shows a similar localization (75).…”

Section: Pvx_093680 (Cvc-81 95 )mentioning

confidence: 92%

“…The exact structure, protein composition, and function are not yet fully understood, but CVC-81 95 is exported, is a predominant protein in these CVCs, and is found on tubular extensions going inwards from the CVC (75,76). Its orthologue in P. cynomolgi shows a similar localization (75). CVC-81 95 was found by Acharya et al (77) in P. vivax-infected peripheral blood, and another study showed that over 80% of patient sera reacted positively with CVC-81 95 (78).…”

Section: Pvx_093680 (Cvc-81 95 )mentioning

confidence: 99%

Plasmodium Helical Interspersed Subtelomeric (PHIST) Proteins, at the Center of Host Cell Remodeling

Warncke

Vakonakis

Beck

2016

Microbiol Mol Biol Rev

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SUMMARYDuring the asexual cycle,Plasmodium falciparumextensively remodels the human erythrocyte to make it a suitable host cell. A large number of exported proteins facilitate this remodeling process, which causes erythrocytes to become more rigid, cytoadherent, and permeable for nutrients and metabolic products. Among the exported proteins, a family of 89 proteins, called thePlasmodiumhelical interspersed subtelomeric (PHIST) protein family, has been identified. While also found in otherPlasmodiumspecies, the PHIST family is greatly expanded inP. falciparum. Although a decade has passed since their first description, to date, most PHIST proteins remain uncharacterized and are of unknown function and localization within the host cell, and there are few data on their interactions with other host or parasite proteins. However, over the past few years, PHIST proteins have been mentioned in the literature at an increasing rate owing to their presence at various localizations within the infected erythrocyte. Expression of PHIST proteins has been implicated in molecular and cellular processes such as the surface display of PfEMP1, gametocytogenesis, changes in cell rigidity, and also cerebral and pregnancy-associated malaria. Thus, we conclude that PHIST proteins are central to host cell remodeling, but despite their obvious importance in pathology, PHIST proteins seem to be understudied. Here we review current knowledge, shed light on the definition of PHIST proteins, and discuss these proteins with respect to their localization and probable function. We take into consideration interaction studies, microarray analyses, or data from blood samples from naturally infected patients to combine all available information on this protein family.

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“…32,[53][54][55] It is thought that CVCs are involved in the endocytosis of macromolecules vital for the development of P vivax, 32 and the rapid appearance of caveolae at the ring stage and their maintenance to the end of the asexual cycle would seem to support this assertion. Although Barnwell et al and Akinyi et al 53,56 have characterized parasitic proteins associated with the vesicle complexes, little is known about the proteins associated with the actual caveolae opening. Aikawa suggests that, unlike the positively charged vesicles, the negatively charged caveolae opening are largely host-derived.…”

Section: Discussionmentioning

confidence: 99%

Plasmodium vivax: restricted tropism and rapid remodeling of CD71-positive reticulocytes

Malleret

Li²,

Zhang

et al. 2015

Blood

172

209

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Key Points• Plasmodium vivax merozoites preferentially infect a subgroup of reticulocytes generally restricted to the bone marrow.• Accelerated "maturation" of infected reticulocytes.Plasmodium vivax merozoites only invade reticulocytes, a minor though heterogeneous population of red blood cell precursors that can be graded by levels of transferrin receptor (CD71) expression. The development of a protocol that allows sorting reticulocytes into defined developmental stages and a robust ex vivo P vivax invasion assay has made it possible for the first time to investigate the fine-scale invasion preference of P vivax merozoites. Surprisingly, it was the immature reticulocytes (CD71 1) that are generally restricted to the bone marrow that were preferentially invaded, whereas older reticulocytes (CD71 2 ), principally found in the peripheral blood, were rarely invaded. Invasion assays based on the CD71 1 reticulocyte fraction revealed substantial postinvasion modification. Thus, 3 to 6 hours after invasion, the initially biomechanically rigid CD71 1 reticulocytes convert into a highly deformable CD71 2 infected red blood cell devoid of host reticular matter, a process that normally spans 24 hours for uninfected reticulocytes. Concurrent with these changes, clathrin pits disappear by 3 hours postinvasion, replaced by distinctive caveolae nanostructures. These 2 hitherto unsuspected features of P vivax invasion, a narrow preference for immature reticulocytes and a rapid remodeling of the host cell, provide important insights pertinent to the pathobiology of the P vivax infection. (Blood. 2015;125(8):1314-1324

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A 95 kDa protein of Plasmodium vivax and P. cynomolgi visualized by three‐dimensional tomography in the caveola–vesicle complexes (Schüffner's dots) of infected erythrocytes is a member of the PHIST family

Cited by 65 publications

References 54 publications

Immunoprofiling of the Tryptophan-Rich Antigen Family in Plasmodium vivax

Immunoprofiling of the Tryptophan-Rich Antigen Family in Plasmodium vivax

Plasmodium Helical Interspersed Subtelomeric (PHIST) Proteins, at the Center of Host Cell Remodeling

Plasmodium vivax: restricted tropism and rapid remodeling of CD71-positive reticulocytes

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