title: Strongyloides stercoralis excretory/secretory protein strongylastacin specifically recognized by IgE antibodies in infected human sera.
abstract: The infective, microscopic Strongyloides stercoralis larvae in contaminated soil can penetrate human skin with the help of excretory/secretory proteases. These proteases play a critical role in infection and transmigration of the parasite to the intestines. Strongylastacin is similar to astacin (from the digestive gland of the crayfish Astacus astacus), a multi-domain protein with a signal peptide, a pro-enzyme, a catalytic domain containing the zinc binding consensus astacin family signature sequence HEXXHXXGFXHEXXRXDR, and a second conserved zinc binding motif SIMHY at N- terminal region. An EGF-1 like domain and a CUB domain are located at the COOH- terminal. In this study, the excretory/secretory Strongylastacin gene from S. stercoralis infective larval stage was cloned and expressed as a 45 kDa in Escherichia coli. Immunoblot analysis showed the presence of natural IgG antibodies against strongylastacin in six infected and six non-endemic normal sera. These findings were confirmed in an ELISA of 32 S. stercoralis infected and 32 presumed normal human sera; all contained natural anti-strongylastacin IgG antibodies. By contrast, IgE antibodies specific to strongylastacin were present in sera from individuals infected with S. stercoralis but not in uninfected control sera. Moreover, recombinant strongylastacin did not cross-react with IgE antibodies either from patients infected with filaria or patients with tropical pulmonary eosinophilic (TPE) who had increased IgE antibodies. The present authors conclude that strongylastacin, an excretory/secretory antigen, elicits specific IgE antibodies in S. stercoralis infected humans. Non-specific IgG antibodies to strongylastacin are present in both infected and normal humans. Further investigation is needed to understand the role of the host protective response against strongylastacin.
authors.affiliation: Laboratory of Parasitic Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA. rvaratha@gwu.edu
authors.forename: Ravi
authors.initials: R
authors.lastname: Varatharajalu
authors.forename: Vijayalakshmi
authors.initials: V
authors.lastname: Parandaman
authors.forename: Momar
authors.initials: M
authors.lastname: Ndao
authors.forename: John F
authors.initials: JF
authors.lastname: Andersen
authors.forename: Franklin A
authors.initials: FA
authors.lastname: Neva
mesh_terms: D000818:Animals; D000909:Antibodies, Helminth / Q000276:immunology*; D005110:Extracellular Space / Q000201:enzymology* / Q000235:genetics / Q000276:immunology / Q000378:metabolism; D015801:Helminth Proteins / Q000235:genetics / Q000276:immunology* / Q000378:metabolism; D006801:Humans; D007073:Immunoglobulin E / Q000276:immunology*; D045726:Metalloproteases / Q000235:genetics / Q000276:immunology* / Q000378:metabolism; D021381:Protein Transport; D017171:Strongyloides stercoralis / Q000201:enzymology* / Q000235:genetics / Q000276:immunology; D013322:Strongyloidiasis / Q000276:immunology* / Q000469:parasitology
chemical_list: D000909:Antibodies, Helminth; D015801:Helminth Proteins; D007073:Immunoglobulin E; D045726:Metalloproteases