{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,23]],"date-time":"2026-09-23T04:33:33Z","timestamp":1790138013774,"version":"4.0.1"},"reference-count":30,"publisher":"National Academy of Sciences","issue":"24","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[1996,11,26]]},"abstract":"<jats:p>\n                    Many animal\u2013bacteria cooperative associations occur in highly\n modified host organs that create a unique environment for housing and\n maintaining the symbionts. It has been assumed that these specialized\n organs develop through a program of symbiosis-specific or -enhanced\n gene expression in one or both partners, but a clear example of this\n process has been lacking. In this study, we provide evidence for the\n enhanced production of an enzyme in the symbiotic organ of the squid\n                    <jats:italic>Euprymna scolopes<\/jats:italic>\n                    , which harbors a culture of the\n luminous bacterium\n                    <jats:italic>Vibrio fischeri<\/jats:italic>\n                    . Our data show that\n this enzyme has a striking biochemical similarity to mammalian\n myeloperoxidase (MPO; EC 1.11.17), an antimicrobial dianisidine\n peroxidase that occurs in neutrophils. MPO and the squid peroxidase\n catalyze the same reaction, have similar apparent subunit molecular\n masses, and a polyclonal antibody to native human MPO specifically\n localized a peroxidase-like protein to the bacteria-containing regions\n of the symbiotic organ. We also provide evidence that a previously\n described squid cDNA encodes the protein (LO4) that is responsible for\n the observed dianisidine peroxidase activity. An antibody made against\n a fragment of LO4 immunoprecipitated dianisidine peroxidase activity\n from extracts of the symbiotic organ, and reacted against these\n extracts and human MPO in Western blot analysis. These data suggest\n that related biochemical mechanisms for the control of bacterial number\n and growth operate in associations that are as functionally diverse as\n pathogenesis and mutualism, and as phylogenetically distant as molluscs\n and mammals.\n                  <\/jats:p>","DOI":"10.1073\/pnas.93.24.13683","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T10:34:16Z","timestamp":1027679656000},"page":"13683-13688","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":66,"title":["A peroxidase related to the mammalian antimicrobial protein myeloperoxidase in the\n                    <i>Euprymna\u2013Vibrio<\/i>\n                    \u2009mutualism"],"prefix":"10.1073","volume":"93","author":[{"given":"Virginia\u2009M.","family":"Weis","sequence":"first","affiliation":[{"name":"Pacific Biomedical Research Center, University of Hawaii, 41 Ahui\r Street, Honolulu, HI 96813, and Department of Biological Sciences,\r University of Southern California, Los Angeles, CA 90089-0371"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrea\u2009L.","family":"Small","sequence":"additional","affiliation":[{"name":"Pacific Biomedical Research Center, University of Hawaii, 41 Ahui\r Street, Honolulu, HI 96813, and Department of Biological Sciences,\r University of Southern California, Los Angeles, CA 90089-0371"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Margaret\u2009J.","family":"McFall-Ngai","sequence":"additional","affiliation":[{"name":"Pacific Biomedical Research Center, University of Hawaii, 41 Ahui\r Street, Honolulu, HI 96813, and Department of Biological Sciences,\r University of Southern California, Los Angeles, CA 90089-0371"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[1996,11,26]]},"reference":[{"key":"e_1_3_2_1_2","volume-title":"The Biology of Symbiosis","author":"Smith D 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C Chou J Chin Agric Soc 28, 59\u201368 (1990).","journal-title":"J Chin Agric Soc"},{"key":"e_1_3_2_25_2","doi-asserted-by":"publisher","DOI":"10.2331\/suisan.58.2373"},{"key":"e_1_3_2_26_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.76.9.4350"},{"key":"e_1_3_2_27_2","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(94)90544-4"},{"key":"e_1_3_2_28_2","doi-asserted-by":"publisher","DOI":"10.1007\/978-3-642-78624-2_7"},{"key":"e_1_3_2_29_2","unstructured":"Boettcher K.\u2009J. 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