Developmentally regulated expression, alternative splicing and distinct sub-groupings in members of the Schistosoma mansoni venom allergen-like (SmVAL) gene family.
BACKGROUND
The Sperm-coating protein/Tpx-1/Ag5/PR-1/Sc7 (SCP/TAPS) domain is found across phyla and is a major structural feature of insect allergens, mammalian sperm proteins and parasitic nematode secreted molecules. Proteins containing this domain are implicated in diverse biological activities and may be important for chronic host/parasite interactions.


RESULTS
We report the first description of an SCP/TAPS gene family (Schistosoma mansoni venom allergen-like (SmVALs)) in the medically important Platyhelminthes (class Trematoda) and describe individual members' phylogenetic relationships, genomic organization and life cycle expression profiles. Twenty-eight SmVALs with complete SCP/TAPS domains were identified and comparison of their predicted protein features and gene structures indicated the presence of two distinct sub-families (group 1 & group 2). Phylogenetic analysis demonstrated that this group 1/group 2 split is zoologically widespread as it exists across the metazoan sub-kingdom. Chromosomal localisation and PCR analysis, coupled to inspection of the current S. mansoni genomic assembly, revealed that many of the SmVAL genes are spatially linked throughout the genome. Quantitative lifecycle expression profiling demonstrated distinct SmVAL expression patterns, including transcripts specifically associated with lifestages involved in definitive host invasion, transcripts restricted to lifestages involved in the invasion of the intermediate host and transcripts ubiquitously expressed. Analysis of SmVAL6 transcript diversity demonstrated statistically significant, developmentally regulated, alternative splicing.


CONCLUSIONS
Our results highlight the existence of two distinct SCP/TAPS protein types within the Platyhelminthes and across taxa. The extensive lifecycle expression analysis indicates several SmVAL transcripts are upregulated in infective stages of the parasite, suggesting that these particular protein products may be linked to the establishment of chronic host/parasite interactions.
Chalmers
Iain W
IW
Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QP, UK. iwc21@cam.ac.uk
McArdle
Andrew J
AJ
Coulson
Richard Mr
RM
Wagner
Marissa A
MA
Schmid
Ralf
R
Hirai
Hirohisa
H
Hoffmann
Karl F
KF
D000485:Allergens / Q000235:genetics*; D017398:Alternative Splicing / Q000235:genetics*; D000595:Amino Acid Sequence; D000818:Animals; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics; D019143:Evolution, Molecular; D005091:Exons / Q000235:genetics; D018507:Gene Expression Regulation, Developmental / Q000235:genetics*; D017238:Genes, Helminth / Q000235:genetics*; D015801:Helminth Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D007438:Introns / Q000235:genetics; D005810:Multigene Family; D010802:Phylogeny; D012550:Schistosoma mansoni / Q000235:genetics* / Q000276:immunology*; D020539:Sequence Analysis, Protein; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity; D014688:Venoms / Q000235:genetics* / Q000276:immunology* / Q000378:metabolism
D000485:Allergens; D018076:DNA, Complementary; D015801:Helminth Proteins; D014688:Venoms