{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T00:56:35Z","timestamp":1787014595619,"version":"build-2736575974"},"reference-count":48,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2011,3,17]],"date-time":"2011-03-17T00:00:00Z","timestamp":1300320000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Veterinary Dermatology"],"published-print":{"date-parts":[[2011,8]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    Staphylococcal exfoliative toxins are known to digest desmoglein (Dsg) 1, a desmosomal cell\u2013cell adhesion molecule, thus causing intraepidermal splitting in human bullous impetigo, staphylococcal scalded skin syndrome and swine exudative epidermitis. Recently, a novel exfoliative toxin gene (\n                    <jats:italic>exi<\/jats:italic>\n                    ), whose sequence shares significant homology with previously identified exfoliative toxins, was isolated from\n                    <jats:italic>Staphylococcus pseudintermedius<\/jats:italic>\n                    . Little is known about the pathogenic involvement of this toxin in canine pustular diseases such as impetigo. The aim of this study was to determine whether EXI, the product of the\n                    <jats:italic>exi<\/jats:italic>\n                    gene, digests canine Dsg1 and causes intraepidermal splitting in canine skin. An\n                    <jats:italic>exi<\/jats:italic>\n                    gene was isolated from chromosomal DNA of an\n                    <jats:italic>S.\u2003pseudintermedius<\/jats:italic>\n                    strain obtained from a pustule of a dog with impetigo, and was used to produce a recombinant EXI by\n                    <jats:italic>Escherichia coli<\/jats:italic>\n                    expression. When purified recombinant EXI was injected intradermally into normal dogs, it caused the development of vesicles or erosions with superficial epidermal splitting. In addition, the EXI abolished immunofluorescence for Dsg1, but not for Dsg3, at the injection sites. Moreover, the EXI directly degraded baculovirus\u2010secreted recombinant extracellular domains of canine Dsg1, but not that of canine Dsg3,\n                    <jats:italic>in vitro<\/jats:italic>\n                    . The EXI also degraded mouse Dsg1\u03b1 and swine Dsg1, but not human Dsg1, mouse Dsg1\u03b2 and Dsg1\u03b3. Conversely, recombinant SIET, previously designated as\n                    <jats:italic>S.\u2003intermedius<\/jats:italic>\n                    exfoliative toxin, did not cause intraepidermal splitting or degradation of any Dsgs. These findings indicate that EXI has a proteolytic activity that digests canine Dsg1, and this characteristic might be involved in the pathogenesis of intraepidermal splitting in canine impetigo.\n                  <\/jats:p>","DOI":"10.1111\/j.1365-3164.2011.00952.x","type":"journal-article","created":{"date-parts":[[2011,3,17]],"date-time":"2011-03-17T06:44:34Z","timestamp":1300344274000},"page":"319-326","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":42,"title":["<i>Staphylococcus pseudintermedius<\/i>\n                    exfoliative toxin EXI selectively digests canine desmoglein 1 and causes subcorneal clefts in canine 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