Characterisation of Sm20, a 20-kilodalton calcium-binding protein of Schistosoma mansoni

Havercroft, Jane C.; Huggins, Maureen C.; Dunne, David W.; Taylor, David W.

doi:10.1016/0166-6851(90)90024-g

Cited by 28 publications

(27 citation statements)

References 18 publications

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“…It is noteworthy that 85 tegument proteins were only found in mixed-sex adults, which might reflect heterogeneity in protein extraction and peptide detection with the mass spectrometer for different tegumental batch samples. Among the tegument proteins in our preparations, several cytoskeleton and motor proteins (actins, tubulins, paramyosin, tropomyosin, myosin, and dynein light chain 1) [23], 22.6 kDa tegument membrane-associated antigen [26], tegumental antigen Sm20 [27], glutathione-S-transferase [28], nitric oxide synthase 1 (NOS1) [29], leucine aminopeptidase [30], 14–3–3 proteins [31], and SnaK [32], as well as a cathepsin B-like cysteine protease precursor [33] and 21.7 kDa antigen [34] have been characterized previously as tegumental proteins.…”

Section: Resultsmentioning

confidence: 99%

New Perspectives on Host-Parasite Interplay by Comparative Transcriptomic and Proteomic Analyses of Schistosoma japonicum

et al. 2006

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Schistosomiasis remains a serious public health problem with an estimated 200 million people infected in 76 countries. Here we isolated ~ 8,400 potential protein-encoding cDNA contigs from Schistosoma japonicum after sequencing circa 84,000 expressed sequence tags. In tandem, we undertook a high-throughput proteomics approach to characterize the protein expression profiles of a number of developmental stages (cercariae, hepatic schistosomula, female and male adults, eggs, and miracidia) and tissues at the host-parasite interface (eggshell and tegument) by interrogating the protein database deduced from the contigs. Comparative analysis of these transcriptomic and proteomic data, the latter including 3,260 proteins with putative identities, revealed differential expression of genes among the various developmental stages and sexes of S. japonicum and localization of putative secretory and membrane antigens, enzymes, and other gene products on the adult tegument and eggshell, many of which displayed genetic polymorphisms. Numerous S. japonicum genes exhibited high levels of identity with those of their mammalian hosts, whereas many others appeared to be conserved only across the genus Schistosoma or Phylum Platyhelminthes. These findings are expected to provide new insights into the pathophysiology of schistosomiasis and for the development of improved interventions for disease control and will facilitate a more fundamental understanding of schistosome biology, evolution, and the host-parasite interplay.

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Section: Resultsmentioning

confidence: 99%

New Perspectives on Host-Parasite Interplay by Comparative Transcriptomic and Proteomic Analyses of Schistosoma japonicum

et al. 2006

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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%

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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“…We have cloned and characterized a calcium binding protein of 20kDa (Sm20) (Havercroft et al 1990). This is also related to calmodulin as judged by comparison of the predicted amino acid sequence of this protein, deduced from the cDNA sequence, with entries in the protein sequence databases.…”

Section: Introductionmentioning

confidence: 99%

“…However, the membrane fractionation experiments of Siddiqui et al (199 1) indicated that calmodulin is found associated with the apical plasma membrane and envelope. Indirect evidence has suggested that at least a proportion of Sm20 is located in the tegument as antisera raised against either purified tegumental membranes of schistosomula or against material stripped from intact schistosomula by treatment with deoxycholate, both recognised Sm20 (Havercroft et al 1990). However, the cloned portion of the antigen was not exposed on the surface.…”

Section: Introductionmentioning

confidence: 99%

Schistosoma mansoni: immuno‐localization of the calcium binding protein Sm20

Havercroft

Smith

Williams

1991

Parasite Immunology

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The 20 kDa calcium binding protein of Schistosoma mansoni, Sm20, is expressed in all stages of the life cycle from the cercaria to the adult worm and in the egg, with equal levels of Sm20 present in adult male and female worms. Localization of Sm20 by immuno-electron microscopy using Sm20-specific antisera and the protein A gold technique demonstrated that the majority of Sm20 is expressed in muscle but that it may also be expressed at low levels in the tegument. These results suggest that Sm20 plays a role in the calcium mediated regulation of muscle contraction. However, it is not clear whether Sm20 acts as a reservoir for calcium in muscle or is directly involved in the regulatory mechanisms of contraction.

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Characterisation of Sm20, a 20-kilodalton calcium-binding protein of Schistosoma mansoni

Cited by 28 publications

References 18 publications

New Perspectives on Host-Parasite Interplay by Comparative Transcriptomic and Proteomic Analyses of Schistosoma japonicum

New Perspectives on Host-Parasite Interplay by Comparative Transcriptomic and Proteomic Analyses of Schistosoma japonicum

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

Schistosoma mansoni: immuno‐localization of the calcium binding protein Sm20

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