A mysterious family of calcium-binding proteins from parasitic worms

Charlotte M. Thomas, David J. Timson

Research output: Contribution to journalArticle

Abstract

There is a family of proteins from parasitic worms which combine N-terminal EF-hand domains with C-terminal dynein light chain-like domains. Data are accumulating on the biochemistry and cell biology of these proteins. However, little is known about their functions in vivo. Schistosoma mansoni expresses 13 family members (SmTAL1-SmTAL13). Three of these (SmTAL1, SmTAL2 and SmTAL3) have been subjected to biochemical analysis which demonstrated that they have different molecular properties. Although their overall folds are predicted to be similar, small changes in the EF-hand domains result in differences in their ion binding properties. Whereas SmTAL1 and SmTAL2 are able to bind calcium (and some other) ions, SmTAL3 appears to be unable to bind any divalent cations. Similar biochemical diversity has been seen in the CaBP proteins from Fasciola hepatica. Four family members are known (FhCaBP1-4). All of these bind to calcium ions. However, FhCaBP4 dimerizes in the presence of calcium ions, FhCaBP3 dimerizes in the absence of calcium ions and FhCaBP2 dimerizes regardless of the prevailing calcium ion concentration. In both the SmTAL and FhCaBP families, the proteins also differ in their ability to bind calmodulin antagonists and related drugs. Interestingly, SmTAL1 interacts with praziquantel (the drug of choice for treating schistosomiasis). The pharmacological significance (if any) of this finding is unknown.

Original languageEnglish
Pages (from-to)1005-1010
Number of pages6
JournalBiochemical Society Transactions
Volume44
Issue number4
DOIs
Publication statusPublished - 15 Aug 2016

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Calcium-Binding Proteins
Helminths
Ions
Calcium
EF Hand Motifs
Proteins
Cytology
Praziquantel
Dyneins
Fasciola hepatica
Biochemistry
Aptitude
Schistosoma mansoni
Schistosomiasis
Divalent Cations
Calmodulin
Pharmaceutical Preparations
Cell Biology
Pharmacology

Bibliographical note

This is not the final peer-reviewed Version of Record. The Version of Record can be found at http://www.biochemsoctrans.org/content/44/4/1005

Keywords

  • Calcium signalling
  • Dynein light chain
  • EF-hand
  • Fasciola hepatica
  • Praziquantel
  • Schistosoma mansoni

Cite this

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title = "A mysterious family of calcium-binding proteins from parasitic worms",
abstract = "There is a family of proteins from parasitic worms which combine N-terminal EF-hand domains with C-terminal dynein light chain-like domains. Data are accumulating on the biochemistry and cell biology of these proteins. However, little is known about their functions in vivo. Schistosoma mansoni expresses 13 family members (SmTAL1-SmTAL13). Three of these (SmTAL1, SmTAL2 and SmTAL3) have been subjected to biochemical analysis which demonstrated that they have different molecular properties. Although their overall folds are predicted to be similar, small changes in the EF-hand domains result in differences in their ion binding properties. Whereas SmTAL1 and SmTAL2 are able to bind calcium (and some other) ions, SmTAL3 appears to be unable to bind any divalent cations. Similar biochemical diversity has been seen in the CaBP proteins from Fasciola hepatica. Four family members are known (FhCaBP1-4). All of these bind to calcium ions. However, FhCaBP4 dimerizes in the presence of calcium ions, FhCaBP3 dimerizes in the absence of calcium ions and FhCaBP2 dimerizes regardless of the prevailing calcium ion concentration. In both the SmTAL and FhCaBP families, the proteins also differ in their ability to bind calmodulin antagonists and related drugs. Interestingly, SmTAL1 interacts with praziquantel (the drug of choice for treating schistosomiasis). The pharmacological significance (if any) of this finding is unknown.",
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A mysterious family of calcium-binding proteins from parasitic worms. / Thomas, Charlotte M.; Timson, David J.

In: Biochemical Society Transactions, Vol. 44, No. 4, 15.08.2016, p. 1005-1010.

Research output: Contribution to journalArticle

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AU - Thomas, Charlotte M.

AU - Timson, David J.

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