{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T14:52:36Z","timestamp":1790866356634,"version":"4.1.0"},"reference-count":58,"publisher":"Microbiology Society","issue":"5","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2008,5,1]]},"abstract":"<jats:p>\n                    The purpose of the present study was to identify 12\n                    <jats:italic>Bacillus<\/jats:italic>\n                    isolates that had been obtained from root canals of teeth requiring endodontic therapy and from periodontal pockets in severe marginal periodontitis, and to determine whether these isolates exhibited extracellular proteolytic activity and, using\n                    <jats:italic>in vitro<\/jats:italic>\n                    assays, whether any such activity could degrade substrates that would be pathophysiologically relevant with regard to the production of endodontic and periodontal lesions. Biochemical and carbohydrate fermentation patterns were used in the identification of all strains, which was confirmed by determination of the16S rRNA gene sequence for strain BJ0055. Screening for production of extracellular proteolytic activity by all strains was done with a general proteinase substrate. All isolates were identified as representing\n                    <jats:italic>Bacillus pumilus<\/jats:italic>\n                    and all exhibited extracellular proteolytic activity. The putative pathophysiological relevance of extracellular proteinase production in strain BJ0055 was assessed using fluorophore-labelled elastin and collagen and several chromogenic peptides. Probable classes of proteinases acting on each substrate were investigated using class-specific inhibitors. Activity\u2013pH profiles were determined in buffers at different pH values. Extracellular activities that were caseinolytic, elastinolytic, collagenolytic, glutamyl endopeptidase-like, and alanyl tripeptidyl peptidase-like were observed. No trypsin-like activities were detected. Serine- and chymotrypsin-like serine proteinase activities were detected, with activity observed at neutral and alkaline, but not acidic, pH.\n                    <jats:italic>B. pumilus<\/jats:italic>\n                    strains isolated from endodontic and periodontal lesions exhibited extracellular activities that degrade elastin, collagen and other substrates. These activities may be virulence factors that contribute to tissue damage in apical periodontitis and severe marginal periodontitis.\n                  <\/jats:p>","DOI":"10.1099\/jmm.0.47754-0","type":"journal-article","created":{"date-parts":[[2008,4,24]],"date-time":"2008-04-24T11:33:33Z","timestamp":1209036813000},"page":"643-651","source":"Crossref","is-referenced-by-count":16,"title":["Extracellular proteolytic activities expressed by Bacillus pumilus isolated from endodontic and periodontal lesions"],"prefix":"10.1099","volume":"57","author":[{"given":"Blair T.","family":"Johnson","sequence":"first","affiliation":[{"name":"Department of Endodontics, School of Dentistry, Louisiana State University Health Sciences Center, New Orleans, LA 70119, USA"},{"name":"Department of Microbiology, Immunology and Parasitology, School of Dentistry, Louisiana State University Health Sciences Center, New Orleans, LA 70119, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lindsey N.","family":"Shaw","sequence":"additional","affiliation":[{"name":"Department of Biology, University of South Florida, Tampa, FL 33620, USA"},{"name":"Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniel C.","family":"Nelson","sequence":"additional","affiliation":[{"name":"University of Maryland Biotechnology Institute, Center for Advanced Research in Biotechnology, Rockville, MD 20850, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John A.","family":"Mayo","sequence":"additional","affiliation":[{"name":"Department of Periodontics, School of Dentistry, Louisiana State University Health Sciences Center, New Orleans, LA 70119, USA"},{"name":"Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA"},{"name":"Department of Microbiology, Immunology and Parasitology, School of Dentistry, Louisiana State University Health Sciences Center, New Orleans, LA 70119, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"345","reference":[{"key":"R1","doi-asserted-by":"crossref","first-page":"390","DOI":"10.1007\/s002530051631","article-title":"Soybean-milk-coagulating activity of Bacillus pumilus derives from a serine protease","volume":"53","author":"Aoyama","year":"2000","journal-title":"Appl Microbiol Biotechnol"},{"key":"R2","first-page":"289","article-title":"Subtilisin","volume-title":"In Handbook of Proteolytic Enzymes","author":"Ballinger","year":"1998"},{"key":"R3","doi-asserted-by":"crossref","first-page":"1769","DOI":"10.1001\/archinte.1988.00380080059017","article-title":"Bacillus infections in patients with cancer","volume":"148","author":"Banerjee","year":"1988","journal-title":"Arch Intern Med"},{"key":"R4","doi-asserted-by":"crossref","first-page":"636","DOI":"10.1378\/chest.108.3.636","article-title":"Machine operator's lung: a hypersensitivity pneumonitis disorder associated with exposure to metalworking fluid aerosols","volume":"108","author":"Bernstein","year":"1995","journal-title":"Chest"},{"key":"R5","first-page":"242","article-title":"Commercially available protease inhibitors. 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