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Logo of bmcgenoBioMed Centralsearchsubmit a manuscriptregisterthis articleBMC Genomics
 
BMC Genomics. 2009; 10: 611.
Published online Dec 16, 2009. doi:  10.1186/1471-2164-10-611
PMCID: PMC2805697
Identification of novel aspartic proteases from Strongyloides ratti and characterisation of their evolutionary relationships, stage-specific expression and molecular structure
Luciane V Mello,corresponding author#1 Helen O'Meara,#1,2 Daniel J Rigden,1 and Steve Paterson1
1School of Biological Sciences, University of Liverpool, Crown Street, Liverpool L69 7ZB, UK
2Department of Pharmacology and Therapeutics, University of Liverpool, Ashton Street, Liverpool, L69 3GE, UK
corresponding authorCorresponding author.
#Contributed equally.
Luciane V Mello: lumello/at/liverpool.ac.uk; Helen O'Meara: hevan/at/liv.ac.uk; Daniel J Rigden: drigden/at/liverpool.ac.uk; Steve Paterson: S.Paterson/at/liverpool.ac.uk
Received April 27, 2009; Accepted December 16, 2009.
Abstract
Background
Aspartic proteases are known to play an important role in the biology of nematode parasitism. This role is best characterised in blood-feeding nematodes, where they digest haemoglobin, but they are also likely to play important roles in the biology of nematode parasites that do not feed on blood. In the present work, we investigate the evolution and expression of aspartic proteases in Strongyloides ratti, which permits a unique comparison between parasitic and free-living adult forms within its life-cycle.
Results
We identified eight transcribed aspartic protease sequences and a further two genomic sequences and compared these to homologues in Caenorhabditis elegans and other nematode species. Phylogenetic analysis demonstrated a complex pattern of gene evolution, such that some S. ratti sequences had a one-to-one correspondence with orthologues of C. elegans but that lineage-specific expansions have occurred for other aspartic proteases in these two nematodes. These gene duplication events may have contributed to the adaptation of the two species to their different lifestyles. Among the set of S. ratti aspartic proteases were two closely-related isoforms that showed differential expression during different life stages: ASP-2A is highly expressed in parasitic females while ASP-2B is predominantly found in free-living adults. Molecular modelling of the ASP-2 isoforms reveals that their substrate specificities are likely to be very similar, but that ASP-2B is more electrostatically negative over its entire molecular surface than ASP-2A. This characteristic may be related to different pH values of the environments in which these two isoforms operate.
Conclusions
We have demonstrated that S. ratti provides a powerful model to explore the genetic adaptations associated with parasitic versus free-living life-styles. We have discovered gene duplication of aspartic protease genes in Strongyloides and identified a pair of paralogues differentially expressed in either the parasitic or the free-living phase of the nematode life-cycle, consistent with an adaptive role for aspartic proteases in the evolution of nematode parasitism.
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