Analysis of a calcium-binding EF-hand protein family in Fasciola gigantica

Subpipattana, Pornpimol; Grams, Rudi; Vichasri-Grams, Suksiri

doi:10.1016/j.exppara.2012.02.005

Cited by 27 publications

(25 citation statements)

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“…While many of the proteins have been localised to the tegument of the worm, their in vivo functions have not been elucidated (Fitzsimmons, et al, 2012, Havercroft, et al, 1990, Huang, et al, 2007, Kim, et al, 2012, Lopes, et al, 2009, Mohamed, et al, 1998, Subpipattana, et al, 2012, Xu, et al, 2014, Zhang, et al, 2012. From the available data it is evident that, despite clear sequence similarities, differences exist between the proteins at the biochemical level.…”

Section: Introductionmentioning

confidence: 91%

“…This species expresses 13 family members, some of which have been shown to elicit IgE-mediated immune responses in the host (Fitzsimmons, et al, 2012, Fitzsimmons, et al, 2007, Webster, et al, 1997. Proteins from this family have also been identified and characterised from other species in the genus Schistosoma, from the Chinese liver fluke Clonorchis sinensis (Huang, et al, 2007, Kim, et al, 2012, Senawong, et al, 2012, Subpipattana, et al, 2012, Vichasri-Grams, et al, 2006, the giant liver fluke Fasciola gigantica and the carcinogenic liver fluke, Opisthorchis viverrini (Fitzsimmons, et al, 2004, Li, et al, 2000, Santiago, et al, 1998, Waine, et al, 1994, Xu, et al, 2014, Zhang, et al, 2012.…”

Section: Introductionmentioning

confidence: 99%

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FhCaBP1 (FH22): A Fasciola hepatica calcium-binding protein with EF-hand and dynein light chain domains

Cheung

Thomas

Timson

2016

Experimental Parasitology

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FH22 has been previously identified as a calcium-binding protein from the common liver fluke, Fasciola hepatica. It is part of a family of at least four proteins in this organism which combine an EFhand containing N-terminal domain with a C-terminal dynein light chainlike domain. Here we report further biochemical properties of FH22, which we propose should be renamed FhCaBP1 for consistency with other family members. Molecular modelling predicted that the two domains are linked by a flexible region and that the second EF-hand in the N-terminal domain is most likely the calcium ion binding site. Native gel electrophoresis demonstrated that the protein binds both calcium and manganese ions, but not cadmium, magnesium, strontium, barium, cobalt, copper(II), iron (II), nickel, zinc, lead or potassium ions. Calcium ion binding alters the conformation of the protein and increases its stability towards thermal denaturation. FhCaBP1 is a dimer in solution and calcium ions have no detectable effect on the protein's ability to dimerise. FhCaBP1 binds to the calmodulin antagonists trifluoperazine and chlorpromazine. Overall, the FhCaBP1's biochemical properties are most similar to FhCaBP2 a fact consistent with the close sequence and predicted structural similarity between the two proteins. properties are most similar to FhCaBP2 a fact consistent with the close sequence and predicted structural similarity between the two proteins.

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Section: Introductionmentioning

confidence: 91%

Section: Introductionmentioning

confidence: 99%

FhCaBP1 (FH22): A Fasciola hepatica calcium-binding protein with EF-hand and dynein light chain domains

Cheung

Thomas

Timson

2016

Experimental Parasitology

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“…These molecules are EF-hand proteins (see Figure 1A), one of the biggest groups of molecular allergens (AF007). Other known allergenic helminth EF-hand proteins include Anisakis simplex troponin C (54) and the Fasciola calcium-binding protein, FgCaBP (91). …”

Section: Are All Allergens Proteins With Homologs In Metazoan Parasites?mentioning

confidence: 99%

Helminth Allergens, Parasite-Specific IgE, and Its Protective Role in Human Immunity

2014

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The Th2 immune response, culminating in eosinophilia and IgE production, is not only characteristic of allergy but also of infection by parasitic worms (helminths). Anti-parasite IgE has been associated with immunity against a range of helminth infections and many believe that IgE and its receptors evolved to help counter metazoan parasites. Allergens (IgE-antigens) are present in only a small minority of protein families and known IgE targets in helminths belong to these same families (e.g., EF-hand proteins, tropomyosin, and PR-1 proteins). During some helminth infection, especially with the well adapted hookworm, the Th2 response is moderated by parasite-expressed molecules. This has been associated with reduced allergy in helminth endemic areas and worm infection or products have been proposed as treatments for allergic conditions. However, some infections (especially Ascaris) are associated with increased allergy and this has been linked to cross-reactivity between worm proteins (e.g., tropomyosins) and highly similar molecules in dust-mites and insects. The overlap between allergy and helminth infection is best illustrated in Anisakis simplex, a nematode that when consumed in under-cooked fish can be both an infective helminth and a food allergen. Nearly 20 molecular allergens have been isolated from this species, including tropomyosin (Ani s 3) and the EF-hand protein, Ani s troponin. In this review, we highlight aspects of the biology and biochemistry of helminths that may have influenced the evolution of the IgE response. We compare dominant IgE-antigens in worms with clinically important environmental allergens and suggest that arrays of such molecules will provide important information on anti-worm immunity as well as allergy.

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“…The corresponding protein in this organism (FgCaBP2) has been described although there is no experimental demonstration that this is a calcium-binding protein (Subpipattana et al 2012). The corresponding protein in this organism (FgCaBP2) has been described although there is no experimental demonstration that this is a calcium-binding protein (Subpipattana et al 2012).…”

Section: Introductionmentioning

confidence: 99%

FhCaBP2: a Fasciola hepatica calcium-binding protein with EF-hand and dynein light chain domains

Thomas

Timson

2015

Parasitology

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FhCaBP2 is a Fasciola hepatica protein which belongs to a family of helminth calcium-binding proteins which combine an N-terminal domain containing two EF-hand motifs and a C-terminal dynein light chain-like (DLC-like) domain. Its predicted structure showed two globular domains joined by a flexible linker. Recombinant FhCaBP2 interacted reversibly with calcium and manganese ions, but not with magnesium, barium, strontium, copper (II), colbalt (II), iron (II), nickel, lead or potassium ions. Cadmium (II) ions appeared to bind non-site-specifically and destabilize the protein. Interaction with either calcium or magnesium ions results in a conformational change in which the protein's surface becomes more hydrophobic. The EF-hand domain alone was able to interact with calcium and manganese ions; the DLC-like domain was not. Alteration of a residue (Asp-58 to Ala) in the second EF-hand motif in this domain abolished ion-binding activity. This suggests that the second EF-hand is the one responsible for ion-binding. FhCaBP2 homodimerizes and the extent of dimerization was not affected by calcium ions or by the aspartate to alanine substitution in the second EF-hand. The isolated EF-hand and DLC-like domains are both capable of homodimerization. FhCaBP2 interacted with the calmodulin antagonists trifluoperazine, chlorpromazine, thiamylal and W7. Interestingly, while chlorpromazine and thiamylal interacted with the EF-hand domain (as expected), trifluoperazine and W7 bound to the DLC-like domain. Overall, FhCaBP2 has distinct biochemical properties compared with other members of this protein family from Fasciola hepatica, a fact which supports the hypothesis that these proteins have different physiological roles.

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Analysis of a calcium-binding EF-hand protein family in Fasciola gigantica

Cited by 27 publications

References 38 publications

FhCaBP1 (FH22): A Fasciola hepatica calcium-binding protein with EF-hand and dynein light chain domains

FhCaBP1 (FH22): A Fasciola hepatica calcium-binding protein with EF-hand and dynein light chain domains

Helminth Allergens, Parasite-Specific IgE, and Its Protective Role in Human Immunity

FhCaBP2: a Fasciola hepatica calcium-binding protein with EF-hand and dynein light chain domains

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