{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,30]],"date-time":"2026-04-30T04:21:42Z","timestamp":1777522902559,"version":"3.51.4"},"reference-count":44,"publisher":"American Veterinary Medical Association (AVMA)","issue":"8","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["ajvr"],"published-print":{"date-parts":[[2001,8,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n\t\t\t\t<jats:p>\n\t\t\t\t\t<jats:bold>Objective<\/jats:bold>\u2014To identify the <jats:italic>Moraxella bovis<\/jats:italic> cytotoxin\ngene.<\/jats:p>\n\t\t\t\t<jats:p>\n\t\t\t\t\t<jats:bold>Procedure<\/jats:bold>\u2014Hemolytic and nonhemolytic strains of\n<jats:italic>M bovis<\/jats:italic> were compared by use of western blotting to\nidentify proteins unique to hemolytic strains.\nOligonucleotide primers, designed on the basis of\namino acid sequences of 2 tryptic peptides derived\nfrom 1 such protein and conserved regions of the <jats:italic>C<\/jats:italic>\nand <jats:italic>B<\/jats:italic> genes from members of the repeats in the\nstructural toxin (RTX) family of bacterial toxins, were\nused to amplify cytotoxin-specific genes from <jats:italic>M\nbovis<\/jats:italic> genomic DNA. Recombinant proteins were\nexpressed, and antisera against these proteins were\nproduced in rabbits.<\/jats:p>\n\t\t\t\t<jats:p>\n\t\t\t\t\t<jats:bold>Results<\/jats:bold>\u2014Several proteins ranging in molecular mass\nfrom 55 to 75 kd were unique to the hemolytic strain.\nAn open reading frame encoding a 927-amino acid protein\nwith a predicted molecular mass of 98.8 kd was\namplified from <jats:italic>M bovis<\/jats:italic> genomic DNA. The deduced\namino acid sequence encoded by this open reading\nframe was homologous to RTX toxins. Antisera against\nthe recombinant carboxy terminus encoded by this\nopen reading frame neutralized hemolytic and cytolytic\nactivities of native <jats:italic>M bovis<\/jats:italic> cytotoxin.<\/jats:p>\n\t\t\t\t<jats:p>\n\t\t\t\t\t<jats:bold>Conclusions and Clinical Relevance<\/jats:bold>\u2014A gene was\nidentified in <jats:italic>M bovis<\/jats:italic> that encodes a protein with\nsequence homology to other RTX toxins. Results of\ncytotoxin neutralization assays support the hypothesis\nthat <jats:italic>M bovis<\/jats:italic> cytotoxin is encoded by this gene and\nbelongs in the RTX family of bacterial exoproteins.\nIdentification of this gene and expression of recombinant\ncytotoxin could facilitate the development of\nimproved vaccines against infectious bovine keratoconjunctivitis.\n(<jats:italic>Am J Vet Res<\/jats:italic> 2001;62:1222\u20131228)<\/jats:p>","DOI":"10.2460\/ajvr.2001.62.1222","type":"journal-article","created":{"date-parts":[[2005,12,6]],"date-time":"2005-12-06T17:24:23Z","timestamp":1133889863000},"page":"1222-1228","source":"Crossref","is-referenced-by-count":35,"title":["Cloning and characterization of a Moraxella bovis cytotoxin gene"],"prefix":"10.2460","volume":"62","author":[{"given":"John A.","family":"Angelos","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"John F.","family":"Hess","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lisle W.","family":"George","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1272","reference":[{"key":"p_1_208","first-page":"761","author":"Henson JB","year":"1960","journal-title":"Etiology. 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