Short communicationA novel member of the NK-lysin protein family is developmentally regulated and secreted by Fasciola hepatica☆
Section snippets
Acknowledgements
This work was supported by CIBA Animal Health Limited (Australia) and Agriculture Victoria. MBR was supported by the Department of Agriculture ‘Nancy Millis’ Postgraduate Scholarship.
References (42)
- et al.
Differences in intermediary energy metabolism between juvenile and adult Fasciola hepatica
Mol. Biochem. Parasitol.
(1987) Energy generation in parasitic helminths
Parasitol. Today
(1994)- et al.
Fasciola hepatica: characterization and cloning of the major cathepsin B protease secreted by newly excysted juvenile liver fluke
Exp. Parasitol.
(1998) - et al.
Fasciola hepatica: stage-specific expression of novel gene sequences as identified by differential display
Exp. Parasitol.
(1998) - et al.
An amphipathic helical motif common to tumourolytic polypeptide NK-lysin and pulmonary surfactant polypeptide SP-B
FEBS Lett.
(1995) Ancient weapons: NK-lysin is a mammalian homologue to pore-forming peptides of a protozoan parasite
Cell
(1995)- et al.
Saposin-like proteins (SAPLIP) carry out diverse functions on a common backbone structure
J. Lipid Res.
(1995) - et al.
The pore-forming peptide of Entamoeba histolytica, the protozoan parasite causing human amoebiasis
Toxicology
(1994) - et al.
Molecular characterization of cDNA sequences encoding glutathione S-transferases of Fasciola hepatica
Exp. Parasitol.
(1992) - et al.
Basic local alignment search tool
J. Mol. Biol.
(1990)
Signal sequences. The limits of variation
J. Mol. Biol.
A simple method for displaying the hydropathic character of a protein
J. Mol. Biol.
Saposin-C from bovine spleen; complete amino acid sequence and relation between the structure and its biological activity
Biochim. Biophys. Acta
Structure and evolution of the human prosaposin chromosomal gene
Genomics
Human acid sphingomyelinase. Isolation, nucleotide sequence and expression of the full-length and alternatively spliced cDNAs
J. Biol. Chem.
Isolation and characterisation of the cDNA for pulmonary surfactant-associated protein-B (SP-B) in the rabbit
Biochem. Biophys. Res. Commun.
Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
Gene
Lipid membrane binding of NK-lysin
FEBS Lett.
Immunological approaches for the control of fasciolosis
Int. J. Parasitol.
Tricine–sodium dodecyl sulfate–polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
Anal. Biochem.
Fasciola hepatica: rapid switching of stage-specific antigen expression after infection
Parasite Immunol.
Cited by (25)
Saposin-like proteins in Opisthorchis felineus and related opisthorchids
2020, Infection, Genetics and EvolutionCitation Excerpt :Three transcripts coding for paralogous SAPs were also identified in another large liver fluke Fasciola hepatica: FhSAP-1, FhSAP-2 and FhSAP-3. The corresponding proteins were found in ESP of adult parasites, but only FhSAP-1 was specific for immature worms (Reed et al., 2000; Di Maggio et al., 2016). In functional tests, FhSAP-2 showed lytic activity on human blood cells (Espino and Hillyer, 2003).
Characterization and vaccine potential of Fasciola gigantica saposin-like protein 1 (SAP-1)
2017, Veterinary ParasitologyCitation Excerpt :This suggests that the SAPs are involved in the lysis of host cells for further enzymatic processing and uptake by the parasites. Two SAPs encoding cDNAs from F. hepatica (FhSAP-1, FhSAP-2), and three SAPs encoding cDNA from F. gigantica (FgSAP-1, FgSAP-2, FgSAP-3) were reported (Reed et al., 2000; Espino and Hillyer, 2003; Grams et al., 2001; Cabán-Hernández and Espino, 2013). FgSAP-1 is expressed at NEJ and early stage of F. gigantica, whereas FgSAP-2 and FgSAP-3 are expressed in late juveniles to adult stages but not at metacercaria, NEJ and early juvenile stage (Grams et al., 2001).
Adjuvant-enhanced antibody and cellular responses to inclusion bodies expressing FhSAP2 correlates with protection of mice to Fasciola hepatica
2016, Experimental ParasitologyCitation Excerpt :Fasciola species use these lytic proteins to cause lysis of the hosts' erythrocytes and leuckocytes so that their contents can be digested further for the parasite's nourishment (Espino and Hillyer, 2003). In F. hepatica, there are two isoforms (SAP1 and SAP2) (Espino and Hillyer, 2003; Reed et al., 2000). SAP1 is expressed in immature and adult stages (Reed et al., 2000), whereas SAP2 is highly expressed in newly excysted juvenile, 3-week juvenile up to adult stages and also in non-embryonated eggs (Caban-Hernandez and Espino, 2013; Espino and Hillyer, 2003).
Differential expression and localization of saposin-like protein 2 of Fasciola hepatica
2013, Acta TropicaCitation Excerpt :If FhSAP2 has an amoebapore-like capacity and forms ion channels within lipid bilayer membranes, it may contribute to the lymphotoxic activities attributed to F. hepatica excretory–secretory material (Cervi et al., 2009; Goose, 1978). Reed et al. also suggested a role for FhSAP1 in lipid metabolism, another SAPLIP in F. hepatica, since insufficiency in de novo fatty acid and cholesterol synthesis is a trait of trematodes (Reed et al., 2000). Also, we cannot discount a possible role in parasite tegument formation, as seen for other trematode tegumental proteins (Tran et al., 2010).
The saposin-like proteins 1, 2, and 3 of Fasciola gigantica
2006, Molecular and Biochemical Parasitology
- ☆
Note: Nucleotide sequences data reported in this paper are available in the GenBank™ database under the accession number U58467.
- 1
Present address: The Walter and Eliza Hall Institute of Medical Research, Royal Pde., Parkville, Victoria 3052, Australia.