{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T04:38:03Z","timestamp":1790743083023,"version":"4.1.0"},"reference-count":44,"publisher":"Cambridge University Press (CUP)","issue":"5","license":[{"start":{"date-parts":[[2009,4,6]],"date-time":"2009-04-06T00:00:00Z","timestamp":1238976000000},"content-version":"unspecified","delay-in-days":5240,"URL":"https:\/\/www.cambridge.org\/core\/terms"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Parasitology"],"published-print":{"date-parts":[[1994,12]]},"abstract":"<jats:p>When immunoglobulin G (IgG) was incubated with<jats:italic>Spirometra mansoni<\/jats:italic>plerocercoid (sparganum), it was cleaved into Fab and Fc fragments. Fab\/c fragments were also hydrolysed. The digestion was accelerated by dithiothreitol (DTT), indicating that cleavage of IgG heavy chain was due to a cysteine protease secreted into the medium. The responsible enzyme, of<jats:italic>M<\/jats:italic><jats:sub>r<\/jats:sub>27 (\u00b1 0\u00b78) kDa, was purified by a series of thiopropyl affinity, Sephacryl S-300 HR and DEAE-anion exchange chromatographies, either from worm extracts or from excretory\u2013secretory products (ESP). The purified, thiol-dependent protease showed an optimal activity at pH 5\u00b77 with 0\u00b71 M sodium acetate but was active over the pH range 4\u00b75\u20138\u00b70. Its activity was inhibited completely by 10<jats:sup>\u22125<\/jats:sup>M L-trans-epoxysuccinylleucylamido(4-guanidino) butane (E-64) and 1 mM iodoacetamide (IAA), but by only 53% using the specific cathepsin L inhibitor, Z-Phe-Phe-CHN<jats:sub>2<\/jats:sub>(5 \u00d7 10<jats:sup>\u22125<\/jats:sup>M). Partial NH<jats:sub>2<\/jats:sub>-terminal amino acid sequence was Leu-Pro-Asp-Ser-Val-Asn-Trp-Arg-Glu-Gly-Ala-Val-Thr-Ala-Val which showed 80% homology to human cathepsin S. Immunoblot analysis showed that sera from infected patients exhibited IgE antibody reaction. It is proposed that cleavage of immunoglobulin by an excreted\u2013secreted, cathepsin S-like, allergenic protease is a mechanism of immune evasion used by the sparganum.<\/jats:p>","DOI":"10.1017\/s0031182000076496","type":"journal-article","created":{"date-parts":[[2009,6,5]],"date-time":"2009-06-05T13:51:56Z","timestamp":1244209916000},"page":"611-621","source":"Crossref","is-referenced-by-count":62,"title":["Cleavage of immunoglobulin G by excretory\u2013secretory cathepsin S-like protease of<i>Spirometra 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