scholarly journals Cloning and Functional Characterization of Two Calmodulin Genes During Larval Development in the Parasitic Flatworm Schistosoma mansoni

2011 ◽  
Vol 97 (1) ◽  
pp. 72-81 ◽  
Author(s):  
Andrew S. Taft ◽  
Timothy P. Yoshino
2004 ◽  
Vol 279 (40) ◽  
pp. 41650-41657 ◽  
Author(s):  
Kelvin.C. Agboh ◽  
Tania E. Webb ◽  
Richard J. Evans ◽  
Steven J. Ennion

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Kim van Noort ◽  
Dieu‑Linh Nguyen ◽  
Verena Kriechbaumer ◽  
Chris Hawes ◽  
Cornelis H. Hokke ◽  
...  

An amendment to this paper has been published and can be accessed via a link at the top of the paper.


2000 ◽  
Vol 110 (2) ◽  
pp. 373-390 ◽  
Author(s):  
Marcelo R Fantappie ◽  
Ahmed Osman ◽  
Edward G Niles ◽  
Philip T LoVerde

2014 ◽  
Vol 10 (6) ◽  
pp. e1004181 ◽  
Author(s):  
Kevin MacDonald ◽  
Samuel Buxton ◽  
Michael J. Kimber ◽  
Tim A. Day ◽  
Alan P. Robertson ◽  
...  

2018 ◽  
Vol 475 (1) ◽  
pp. 289-303 ◽  
Author(s):  
Xavier Maréchal ◽  
Ricardo De Mendonça ◽  
Roger Miras ◽  
Jean Revilloud ◽  
Patrice Catty

Schistosoma mansoni is a parasite that causes bilharzia, a neglected tropical disease affecting hundreds of millions of people each year worldwide. In 2012, S. mansoni had been identified as the only invertebrate possessing two SERCA-type Ca2+-ATPases, SMA1 and SMA2. However, our analysis of recent genomic data shows that the presence of two SERCA pumps is rather frequent in parasitic flatworms. To understand the reasons of this redundancy in S. mansoni, we compared SMA1 and SMA2 at different levels. In terms of sequence and organization, the genes SMA1 and SMA2 are similar, suggesting that they might be the result of a duplication event. At the protein level, SMA1 and SMA2 only slightly differ in length and in the sequence of the nucleotide-binding domain. To get functional information on SMA1, we produced it in an active form in Saccharomyces cerevisiae, as previously done for SMA2. Using phosphorylation assays from ATP, we demonstrated that like SMA2, SMA1 bound calcium in a cooperative mode with an apparent affinity in the micromolar range. We also showed that SMA1 and SMA2 had close sensitivities to cyclopiazonic acid but different sensitivities to thapsigargin, two specific inhibitors of SERCA pumps. On the basis of transcriptomic data available in GeneDB, we hypothesize that SMA1 is a housekeeping Ca2+-ATPase, whereas SMA2 might be required in particular striated-like muscles like those present the tail of the cercariae, the infecting form of the parasite.


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