{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,18]],"date-time":"2026-03-18T05:43:45Z","timestamp":1773812625739,"version":"3.50.1"},"reference-count":28,"publisher":"American Society for Microbiology","issue":"2","license":[{"start":{"date-parts":[[2006,2,1]],"date-time":"2006-02-01T00:00:00Z","timestamp":1138752000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Infect Immun"],"published-print":{"date-parts":[[2006,2]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Infective larvae (L3) of nematodes secrete macromolecules that are critical to infection and establishment of the parasite in the host. The dog hookworm\n            <jats:italic>Ancylostoma caninum<\/jats:italic>\n            secretes an astacin-like metalloprotease,\n            <jats:italic>Ac<\/jats:italic>\n            -MTP-1, upon activation in vitro with host serum. Recombinant\n            <jats:italic>Ac<\/jats:italic>\n            -MTP-1 was expressed in the baculovirus\/insect cell system as a secreted protein and was purified from culture medium by two separate methods, cation-exchange fast-performance liquid chromatography and gelatin-affinity chromatography. Recombinant MTP-1 was catalytically active and digested a range of native and denatured connective tissue substrates, including gelatin, collagen, laminin, and fibronectin. A dog was immunized with recombinant\n            <jats:italic>Ac<\/jats:italic>\n            -MTP-1 formulated with AS03 adjuvant, and the antiserum was used to immunolocalize the anatomic sites of expression within\n            <jats:italic>A. caninum<\/jats:italic>\n            L3 to secretory granules in the glandular esophagus and the channels that connect the esophagus to the L3 surface and to the cuticle. Antiserum inhibited the ability of recombinant MTP-1 to digest collagen by 85% and inhibited larval migration through tissue in vitro by 70 to 75%, in contrast to just 5 to 10% inhibition obtained with preimmunization serum. The metalloprotease inhibitors EDTA and 1,10-phenanthroline also reduced the penetration of L3 through skin in vitro by 43 to 61%. The data strongly suggest that\n            <jats:italic>Ac<\/jats:italic>\n            -MTP-1 is critical for the invasion process of hookworm larvae, and moreover, that antibodies against the enzyme can neutralize its function and inhibit migration.\n          <\/jats:p>","DOI":"10.1128\/iai.74.2.961-967.2006","type":"journal-article","created":{"date-parts":[[2006,1,21]],"date-time":"2006-01-21T01:42:38Z","timestamp":1137807758000},"page":"961-967","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":98,"title":["<i>Ancylostoma caninum<\/i>\n            MTP-1, an Astacin-Like Metalloprotease Secreted by Infective Hookworm Larvae, Is Involved in Tissue Migration"],"prefix":"10.1128","volume":"74","author":[{"given":"Angela L.","family":"Williamson","sequence":"first","affiliation":[{"name":"Department of Microbiology and Tropical Medicine, George Washington University Medical Center, Washington, D.C."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sara","family":"Lustigman","sequence":"additional","affiliation":[{"name":"Lindsley F. 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