Da'dara A, Tsai M H, Tao L F, Marx K A, Shoemaker C B, Harn D A, Skelly P J
Department of Immunology and Infectious Diseases, Harvard School of Public Health, 665 Huntington Avenue, Boston, MA 02115, U.S.A.
Exp Parasitol. 2001 Aug;98(4):215-22. doi: 10.1006/expr.2001.4637.
A cDNA encoding a Ca-ATPase homologue, designated SMA3, was isolated from an adult cDNA library of Schistosoma mansoni. The full-length cloned DNA contains a 3105-bp open reading frame that potentially encodes a 1035-amino-acid protein with a M(r) of 113,729 and a pl of 6.48. Homology searches for SMA3 reveal high sequence identity with a variety of Ca-ATPases from evolutionarily diverse organisms. SMA3 is predicted to contain 10 transmembrane regions typical of this protein family as well as other conserved domains, such as the phosphorylation site and FITC binding domain. The greatest sequence identity (40-50%) is found to those Ca-ATPases belonging to the secretory pathway subclass. Identification of the 5' end of the SMA3 cDNA by RACE analysis reveals the presence of a 36-base spliced leader RNA, suggesting that the SMA3 pre-mRNA is processed by trans-splicing. Northern analysis reveals a single dominant transcript of 5 kb in adult RNA preparations. Antibodies raised against an amino terminal peptide detect the protein in the adult tegument, suggesting that SMA3 functions to help control Ca homeostasis within the tegument and may play a role in signal transduction at the host parasite interface.
