Molecular cloning, sequencing, and expression analysis of presenilin cDNA from Schistosoma mansoni.
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Data
2009
Autores
Magalhães, Lizandra Guidi
Borges, William de Castro
Gomes, Matheus de Souza
Cota, Renata Guerra de Sá
Rodrigues, Vanderlei
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Resumo
Presenilins (PS) are integral membrane proteins
involved, among other functions, in regulated intramembrane
proteolysis. In this study, we report the identification and
characterization of a complementary DNA from Schistosoma
mansoni exhibiting a significant homology to human and
nonvertebrate presinilins. S. mansoni contained a 1,485 bp
open reading frame encoding a predicted protein of 494
amino acids. Alignment of predicted amino acid sequence of
S. mansoni with PS (SmPS) from other species revealed up
to 40% similarity shared among the investigated organisms.
In addition, phylogenetic analyses demonstrated SmPS being
closely related to its orthologues found in Schistosoma
japonicum and Caenorhabditis elegans. Expression analysis
of SmPS using quantitative real-time PCR revealed that the
transcript is up-regulated in the egg stage. We hypothesize
that the high level of SmPS in the S. mansoni embryo
correlates to an important role during cellular signaling
associated to larval development. To our knowledge, this
study represents the first attempt to investigate the existence
and abundance of PS from a helminth parasite.
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MAGALHÃES, L. G. et al. Molecular cloning, sequencing, and expression analysis of presenilin cDNA from Schistosoma mansoni. Parasitology Research, v. 106, p. 07-13, 2009. Disponível em: <https://link.springer.com/article/10.1007%2Fs00436-009-1620-9>. Acesso em: 23 fev. 2017.