{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,12]],"date-time":"2026-05-12T23:19:17Z","timestamp":1778627957182,"version":"3.51.4"},"reference-count":40,"publisher":"Wiley","issue":"12","license":[{"start":{"date-parts":[[2004,12,2]],"date-time":"2004-12-02T00:00:00Z","timestamp":1101945600000},"content-version":"vor","delay-in-days":1,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Fish Diseases"],"published-print":{"date-parts":[[2004,12]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>In order to identify genes encoding the outer membrane proteins (OMPs) of the myxobacter<jats:italic>Flavobacterium columnare<\/jats:italic>G<jats:sub>4<\/jats:sub>, the expression library of the bacterium was screened by using rabbit antisera developed against its OMPs. Positive colonies of<jats:italic>Escherichia coli<\/jats:italic>M15 containing fragments encoding the bacterial OMPs were selected for cloning the relevant genes by genomic walking methods. Two genes encoding a membrane\u2010associated zinc metalloprotease and prolyl oligopeptidase are reported in this paper. The membrane\u2010associated zinc metalloprotease gene (<jats:italic>map<\/jats:italic>) is 1800\u2003bp in length, coding for 449 amino acids (aa). Despite the presence of a conserved motif HEXXH for all metalloproteases, the special HEXXH\u2003\u223c\u200332 aa\u2003\u223c\u2003E motif of the<jats:italic>F. columnare<\/jats:italic>G<jats:sub>4<\/jats:sub>Map and its low level of identity with other reported zinc\u2010containing metalloproteases may imply that the membrane\u2010associated zinc metalloprotease of<jats:italic>F. columnare<\/jats:italic>G<jats:sub>4<\/jats:sub>represents a new family of zincins. The gene encoding prolyl oligopeptidase (Pop), a serine proteinase, is 2352\u2003bp in length, coding for 649 aa. Sequence homology analysis revealed that the Pop is also novel as it has &lt;50% identity with other reported prolyl oligopeptidase family proteins. The present study represents the first to employ anti\u2010fish bacterial OMP sera to screen genes of membrane\u2010associated proteases of fish pathogenic bacteria, and to provide necessary information for the examination of the role of the two genes in the infection and pathogenesis of<jats:italic>F. columnare<\/jats:italic>.<\/jats:p>","DOI":"10.1111\/j.1365-2761.2004.00596.x","type":"journal-article","created":{"date-parts":[[2004,12,2]],"date-time":"2004-12-02T09:47:42Z","timestamp":1101980862000},"page":"719-729","source":"Crossref","is-referenced-by-count":27,"title":["Characterization of two membrane\u2010associated protease genes obtained from screening out\u2010membrane protein genes of<i>Flavobacterium columnare<\/i>G<sub>4<\/sub>"],"prefix":"10.1111","volume":"27","author":[{"given":"H X","family":"Xie","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"P","family":"Nie","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"B J","family":"Sun","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2004,12,2]]},"reference":[{"key":"e_1_2_15_2_1","doi-asserted-by":"publisher","DOI":"10.1007\/s001090050215"},{"key":"e_1_2_15_3_1","doi-asserted-by":"publisher","DOI":"10.1515\/bchm3.1992.373.2.353"},{"key":"e_1_2_15_4_1","doi-asserted-by":"crossref","first-page":"8192","DOI":"10.1016\/S0021-9258(18)42426-X","article-title":"Characterization of a prolyl endopeptidase from Flavobacterium meningosepticum","volume":"267","author":"Chevallier S.","year":"1992","journal-title":"Journal of Biological Chemistry"},{"key":"e_1_2_15_5_1","doi-asserted-by":"publisher","DOI":"10.1093\/protein\/10.6.673"},{"key":"e_1_2_15_6_1","doi-asserted-by":"publisher","DOI":"10.1128\/JCM.35.1.322-324.1997"},{"key":"e_1_2_15_7_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0378-1135(98)00196-5"},{"key":"e_1_2_15_8_1","first-page":"1","article-title":"Influence of water quality and temperature on adhesion of high and low virulence Flavobacterium columnare strains to isolated gill arches","volume":"21","author":"Decostere A.","year":"1998","journal-title":"Journal of Fish Diseases"},{"key":"e_1_2_15_9_1","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2761.1999.00198.x"},{"key":"e_1_2_15_10_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0378-1135(99)00050-4"},{"key":"e_1_2_15_11_1","doi-asserted-by":"publisher","DOI":"10.1007\/BF00170434"},{"key":"e_1_2_15_12_1","volume-title":"Columnaris Disease: a Bacterial Infection Caused by Flavobacterium columnare","author":"Durborow R.M.","year":"1998"},{"key":"e_1_2_15_13_1","doi-asserted-by":"publisher","DOI":"10.1006\/fsim.1994.1004"},{"key":"e_1_2_15_14_1","doi-asserted-by":"publisher","DOI":"10.1006\/abbi.1998.0836"},{"key":"e_1_2_15_15_1","doi-asserted-by":"crossref","first-page":"790","DOI":"10.1093\/oxfordjournals.jbchem.a124120","article-title":"Prolyl endopeptidase from Aeromonas hydrophila: cloning, sequencing, and expression of the enzyme gene, and characterization of the expressed enzyme","volume":"113","author":"Kanatani A.","year":"1993","journal-title":"Journal of Biochemistry"},{"key":"e_1_2_15_16_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1574-6968.1989.tb03565.x"},{"key":"e_1_2_15_17_1","first-page":"315","article-title":"Studies on the gill diseases of the grass carp (Ctenopharyngodon idellus) I. 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