The opdB Locus Encodes the Trypsin-Like Peptidase Activity of Treponema denticola

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Published in:	Infection and Immunity Vol. 69; no. 10; pp. 6193 - 6200
Main Authors:	Fenno, J C, Lee, S Y, Bayer, C H, Ning, Y
Format:	Journal Article
Language:	English
Published:	Washington, DC American Society for Microbiology 01-10-2001
Subjects:	Alleles Amino Acid Sequence Bacterial Proteins Bacteriology Bacteroides forsythus Base Sequence Benzoylarginine-2-Naphthylamide - metabolism Biological and medical sciences DNA, Bacterial Fundamental and applied biological sciences. Psychology Genes, Bacterial Genetics Metabolism. Enzymes Microbiology Molecular Pathogenesis Molecular Sequence Data Mutagenesis opdB gene Porphyromonas gingivalis Serine Endopeptidases - genetics Serine Endopeptidases - metabolism Treponema - enzymology Treponema - genetics Treponema - growth & development Treponema denticola Disease Bacteroidaceae Association Arginine Gene Bacteria Locus Ability Facilitation Porphyromonas gingivalis Treponema denticola Serine endopeptidases Spirochaetales Enzyme Stomatology Dental disease Dental plaque Bacteroides Peptidases Periodontal disease Trypsin Aminoacid Hydrolases Microorganism Treponemataceae Severe
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Abstract	Classifications Services IAI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue IAI About IAI Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy Connect to IAI IAI RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0019-9567 Online ISSN: 1098-5522 Copyright © 2014 by the American Society for Microbiology. For an alternate route to IAI .asm.org, visit: IAI
AbstractList	High levels of Treponema denticola in subgingival dental plaque are associated with severe periodontal disease. T. denticola , along with Porphyromonas gingivalis and Bacteroides forsythus , are the only cultivatable oral microorganisms that produce significant amounts of “trypsin-like” peptidase activity. The ability of subgingival plaque to hydrolyze N -α-benzoyl- dl -arginine-2-naphthylamide (BANA) is associated with high levels of one or more of these organisms. The purpose of this study was to identify the gene encoding trypsin-like activity in T. denticola and thus facilitate molecular-level studies of its potential role in disease. Using published peptide sequences of a T. denticola surface-associated oligopeptidase with BANA-hydrolyzing activity, we identified the gene, designated opdB , in an apparently noncoding region of the T. denticola genome unannotated contigs (11/2000; http://www.tigr.org ). The opdB gene begins with a TTG start codon and encodes a 685-residue peptide with high homology to the oligopeptidase B family in prokaryotes and eukaryotes. An isogenic T. denticola opdB mutant was constructed by allelic replacement mutagenesis using an ermF/AM gene cassette. The mutant lacked BANA-hydrolyzing activity and had a slightly slower growth rate than the parent strain. This mutant will be used in future studies of interactions of T. denticola with host cells and tissue. High levels of Treponema denticola in subgingival dental plaque are associated with severe periodontal disease. T. denticola, along with Porphyromonas gingivalis and Bacteroides forsythus, are the only cultivatable oral microorganisms that produce significant amounts of "trypsin-like" peptidase activity. The ability of subgingival plaque to hydrolyze N-alpha-benzoyl-DL-arginine-2-naphthylamide (BANA) is associated with high levels of one or more of these organisms. The purpose of this study was to identify the gene encoding trypsin-like activity in T. denticola and thus facilitate molecular-level studies of its potential role in disease. Using published peptide sequences of a T. denticola surface-associated oligopeptidase with BANA-hydrolyzing activity, we identified the gene, designated opdB, in an apparently noncoding region of the T. denticola genome unannotated contigs (11/2000; http://www.tigr.org). The opdB gene begins with a TTG start codon and encodes a 685-residue peptide with high homology to the oligopeptidase B family in prokaryotes and eukaryotes. An isogenic T. denticola opdB mutant was constructed by allelic replacement mutagenesis using an ermF/AM gene cassette. The mutant lacked BANA-hydrolyzing activity and had a slightly slower growth rate than the parent strain. This mutant will be used in future studies of interactions of T. denticola with host cells and tissue. ABSTRACT High levels of Treponema denticola in subgingival dental plaque are associated with severe periodontal disease. T. denticola , along with Porphyromonas gingivalis and Bacteroides forsythus , are the only cultivatable oral microorganisms that produce significant amounts of “trypsin-like” peptidase activity. The ability of subgingival plaque to hydrolyze N -α-benzoyl- dl -arginine-2-naphthylamide (BANA) is associated with high levels of one or more of these organisms. The purpose of this study was to identify the gene encoding trypsin-like activity in T. denticola and thus facilitate molecular-level studies of its potential role in disease. Using published peptide sequences of a T. denticola surface-associated oligopeptidase with BANA-hydrolyzing activity, we identified the gene, designated opdB , in an apparently noncoding region of the T. denticola genome unannotated contigs (11/2000; http://www.tigr.org ). The opdB gene begins with a TTG start codon and encodes a 685-residue peptide with high homology to the oligopeptidase B family in prokaryotes and eukaryotes. An isogenic T. denticola opdB mutant was constructed by allelic replacement mutagenesis using an ermF/AM gene cassette. The mutant lacked BANA-hydrolyzing activity and had a slightly slower growth rate than the parent strain. This mutant will be used in future studies of interactions of T. denticola with host cells and tissue. Classifications Services IAI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue IAI About IAI Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy Connect to IAI IAI RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0019-9567 Online ISSN: 1098-5522 Copyright © 2014 by the American Society for Microbiology. For an alternate route to IAI .asm.org, visit: IAI High levels of Treponema denticola in subgingival dental plaque are associated with severe periodontal disease. T. denticola, along with Porphyromonas gingivalis and Bacteroides forsythus, are the only cultivatable oral microorganisms that produce significant amounts of "trypsin-like" peptidase activity. The ability of subgingival plaque to hydrolyze N- alpha -benzoyl-DL-arginine-2-naphthylamide (BANA) is associated with high levels of one or more of these organisms. The purpose of this study was to identify the gene encoding trypsin-like activity in T. denticola and thus facilitate molecular-level studies of its potential role in disease. Using published peptide sequences of a T. denticola surface-associated oligopeptidase with BANA-hydrolyzing activity, we identified the gene, designated opdB, in an apparently noncoding region of the T. denticola genome unannotated contigs.
Author	Si Young Lee J. Christopher Fenno Yu Ning Christopher H. Bayer
AuthorAffiliation	Department of Biologic and Materials Sciences, School of Dentistry, University of Michigan, Ann Arbor, Michigan 48109-1078, 1 and Department of Oral Microbiology, College of Dentistry, Kangnung National University, Kangnung, Korea 2
AuthorAffiliation_xml	– name: Department of Biologic and Materials Sciences, School of Dentistry, University of Michigan, Ann Arbor, Michigan 48109-1078, 1 and Department of Oral Microbiology, College of Dentistry, Kangnung National University, Kangnung, Korea 2
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Keywords	Disease Bacteroidaceae Association Arginine Gene Bacteria Locus Ability Facilitation Porphyromonas gingivalis Treponema denticola Serine endopeptidases Spirochaetales Enzyme Stomatology Dental disease Dental plaque Bacteroides Peptidases Periodontal disease Trypsin Aminoacid Hydrolases Microorganism Treponemataceae Severe
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Notes	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Corresponding author. Mailing address: Department of Biologic and Materials Sciences, School of Dentistry, University of Michigan, Ann Arbor, MI 48109-1078. Phone: (734) 763-3331. Fax: (734) 764-2425. E-mail: fenno@umich.edu.
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Snippet	Classifications Services IAI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit... High levels of Treponema denticola in subgingival dental plaque are associated with severe periodontal disease. T. denticola, along with Porphyromonas... ABSTRACT High levels of Treponema denticola in subgingival dental plaque are associated with severe periodontal disease. T. denticola , along with... High levels of Treponema denticola in subgingival dental plaque are associated with severe periodontal disease. T. denticola , along with Porphyromonas...
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StartPage	6193
SubjectTerms	Alleles Amino Acid Sequence Bacterial Proteins Bacteriology Bacteroides forsythus Base Sequence Benzoylarginine-2-Naphthylamide - metabolism Biological and medical sciences DNA, Bacterial Fundamental and applied biological sciences. Psychology Genes, Bacterial Genetics Metabolism. Enzymes Microbiology Molecular Pathogenesis Molecular Sequence Data Mutagenesis opdB gene Porphyromonas gingivalis Serine Endopeptidases - genetics Serine Endopeptidases - metabolism Treponema - enzymology Treponema - genetics Treponema - growth & development Treponema denticola
Title	The opdB Locus Encodes the Trypsin-Like Peptidase Activity of Treponema denticola
URI	http://iai.asm.org/content/69/10/6193.abstract https://www.ncbi.nlm.nih.gov/pubmed/11553560 https://search.proquest.com/docview/17912913 https://pubmed.ncbi.nlm.nih.gov/PMC98751
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