Identification and characterization of collagen-binding activity in Streptococcus mutans wall-associated protein: A possible implication in dental root caries and endocarditis
Streptococcus mutans is implicated in coronal and dental root decay, and in endocarditis. Comparative study of the amino acid sequence of S. mutans 47 kDa wall-associated protein A (WapA) revealed a collagen-binding domain (CBD) at the N-terminal region. Recombinant AgA (WapA truncated at the carbox...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2006-05, Vol.343 (3), p.787-792 |
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| creator | Han, Thomas K. Zhang, Chi Dao, My Lien |
| description | Streptococcus mutans is implicated in coronal and dental root decay, and in endocarditis. Comparative study of the amino acid sequence of
S. mutans 47
kDa wall-associated protein A (WapA) revealed a collagen-binding domain (CBD) at the N-terminal region. Recombinant AgA (WapA truncated at the carboxyterminal end) was isolated, biotin-labeled, and analyzed by Solid Phase Binding Assay. The results showed that biotin-labeled AgA bound significantly and in a dose-dependent manner to immobilized collagen type I, and to a lesser extent to fibronectin, but not to collagen type IV or laminin. Binding of biotin-labeled
S. mutans cells to collagen-coated surfaces was significantly inhibited by antibody to WapA or AgA (
P
<
0.001). The results obtained confirmed the collagen-binding activity of CBD in AgA and WapA, and suggested that WapA may be used, not only as a vaccine against coronal and dental root caries, but also against
S. mutans-mediated endocarditis. |
| doi_str_mv | 10.1016/j.bbrc.2006.03.025 |
| format | Article |
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S. mutans 47
kDa wall-associated protein A (WapA) revealed a collagen-binding domain (CBD) at the N-terminal region. Recombinant AgA (WapA truncated at the carboxyterminal end) was isolated, biotin-labeled, and analyzed by Solid Phase Binding Assay. The results showed that biotin-labeled AgA bound significantly and in a dose-dependent manner to immobilized collagen type I, and to a lesser extent to fibronectin, but not to collagen type IV or laminin. Binding of biotin-labeled
S. mutans cells to collagen-coated surfaces was significantly inhibited by antibody to WapA or AgA (
P
<
0.001). The results obtained confirmed the collagen-binding activity of CBD in AgA and WapA, and suggested that WapA may be used, not only as a vaccine against coronal and dental root caries, but also against
S. mutans-mediated endocarditis.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2006.03.025</identifier><identifier>PMID: 16563343</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Antibodies, Bacterial - pharmacology ; Antigens, Bacterial - chemistry ; Antigens, Bacterial - immunology ; Antigens, Bacterial - metabolism ; Bacterial Proteins - chemistry ; Bacterial Proteins - immunology ; Bacterial Proteins - metabolism ; Binding Sites ; Collagen Type I - metabolism ; Collagen-binding activity ; Consensus Sequence ; Dental root decay ; Endocarditis ; Endocarditis, Bacterial - microbiology ; Molecular Sequence Data ; Protein Structure, Tertiary ; Root Caries - microbiology ; Sequence Alignment ; Streptococcus mutans ; Streptococcus mutans - immunology ; Streptococcus mutans - pathogenicity ; Wall-associated protein A</subject><ispartof>Biochemical and biophysical research communications, 2006-05, Vol.343 (3), p.787-792</ispartof><rights>2006 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c385t-e8235846ff6eced017fb83174f69f8cc770b7564ed39dfb33e2ecc52391d56173</citedby><cites>FETCH-LOGICAL-c385t-e8235846ff6eced017fb83174f69f8cc770b7564ed39dfb33e2ecc52391d56173</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bbrc.2006.03.025$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16563343$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Han, Thomas K.</creatorcontrib><creatorcontrib>Zhang, Chi</creatorcontrib><creatorcontrib>Dao, My Lien</creatorcontrib><title>Identification and characterization of collagen-binding activity in Streptococcus mutans wall-associated protein: A possible implication in dental root caries and endocarditis</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Streptococcus mutans is implicated in coronal and dental root decay, and in endocarditis. Comparative study of the amino acid sequence of
S. mutans 47
kDa wall-associated protein A (WapA) revealed a collagen-binding domain (CBD) at the N-terminal region. Recombinant AgA (WapA truncated at the carboxyterminal end) was isolated, biotin-labeled, and analyzed by Solid Phase Binding Assay. The results showed that biotin-labeled AgA bound significantly and in a dose-dependent manner to immobilized collagen type I, and to a lesser extent to fibronectin, but not to collagen type IV or laminin. Binding of biotin-labeled
S. mutans cells to collagen-coated surfaces was significantly inhibited by antibody to WapA or AgA (
P
<
0.001). The results obtained confirmed the collagen-binding activity of CBD in AgA and WapA, and suggested that WapA may be used, not only as a vaccine against coronal and dental root caries, but also against
S. mutans-mediated endocarditis.</description><subject>Amino Acid Sequence</subject><subject>Antibodies, Bacterial - pharmacology</subject><subject>Antigens, Bacterial - chemistry</subject><subject>Antigens, Bacterial - immunology</subject><subject>Antigens, Bacterial - metabolism</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - immunology</subject><subject>Bacterial Proteins - metabolism</subject><subject>Binding Sites</subject><subject>Collagen Type I - metabolism</subject><subject>Collagen-binding activity</subject><subject>Consensus Sequence</subject><subject>Dental root decay</subject><subject>Endocarditis</subject><subject>Endocarditis, Bacterial - microbiology</subject><subject>Molecular Sequence Data</subject><subject>Protein Structure, Tertiary</subject><subject>Root Caries - microbiology</subject><subject>Sequence Alignment</subject><subject>Streptococcus mutans</subject><subject>Streptococcus mutans - immunology</subject><subject>Streptococcus mutans - pathogenicity</subject><subject>Wall-associated protein A</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1u1TAQhS0EopfCC7BAXrFLsOPESRCbquKnUiUWgMTOcuxxmavEDrbTqrwUr4gv9yJ2sLJsf3PmzBxCnnNWc8blq309TdHUDWOyZqJmTfeA7DgbWdVw1j4kO1Z-qmbkX8_Ik5T2jHHeyvExOeOyk0K0Ykd-XlnwGR0anTF4qr2l5puO2mSI-OP4GBw1YZ71DfhqQm_R39AC4C3me4qefsoR1hxMMGZLdNmy9one6XmudErBoM5g6RpDBvSv6QVdQ0o4zUBxWec_nYvOwYqeaQwhU6MjQvrtB7wN5WoxY3pKHjk9J3h2Os_Jl3dvP19-qK4_vr-6vLiujBi6XMHQiG5opXMSDFjGezcNgvetk6MbjOl7NvWdbMGK0bpJCGjAmK4RI7ed5L04Jy-PusX29w1SVgsmA2UJHsKWlOyHZuz4-F-Q93wQgxAFbI6giWX8CE6tERcd7xVn6pCn2qtDnuqQp2JClTxL0YuT-jYtYP-WnAIswJsjAGUZtwhRJYPgy8wYwWRlA_5L_xd_UbZ9</recordid><startdate>20060512</startdate><enddate>20060512</enddate><creator>Han, Thomas K.</creator><creator>Zhang, Chi</creator><creator>Dao, My Lien</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>20060512</creationdate><title>Identification and characterization of collagen-binding activity in Streptococcus mutans wall-associated protein: A possible implication in dental root caries and endocarditis</title><author>Han, Thomas K. ; Zhang, Chi ; Dao, My Lien</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c385t-e8235846ff6eced017fb83174f69f8cc770b7564ed39dfb33e2ecc52391d56173</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Amino Acid Sequence</topic><topic>Antibodies, Bacterial - pharmacology</topic><topic>Antigens, Bacterial - chemistry</topic><topic>Antigens, Bacterial - immunology</topic><topic>Antigens, Bacterial - metabolism</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - immunology</topic><topic>Bacterial Proteins - metabolism</topic><topic>Binding Sites</topic><topic>Collagen Type I - metabolism</topic><topic>Collagen-binding activity</topic><topic>Consensus Sequence</topic><topic>Dental root decay</topic><topic>Endocarditis</topic><topic>Endocarditis, Bacterial - microbiology</topic><topic>Molecular Sequence Data</topic><topic>Protein Structure, Tertiary</topic><topic>Root Caries - microbiology</topic><topic>Sequence Alignment</topic><topic>Streptococcus mutans</topic><topic>Streptococcus mutans - immunology</topic><topic>Streptococcus mutans - pathogenicity</topic><topic>Wall-associated protein A</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Han, Thomas K.</creatorcontrib><creatorcontrib>Zhang, Chi</creatorcontrib><creatorcontrib>Dao, My Lien</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Han, Thomas K.</au><au>Zhang, Chi</au><au>Dao, My Lien</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification and characterization of collagen-binding activity in Streptococcus mutans wall-associated protein: A possible implication in dental root caries and endocarditis</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2006-05-12</date><risdate>2006</risdate><volume>343</volume><issue>3</issue><spage>787</spage><epage>792</epage><pages>787-792</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Streptococcus mutans is implicated in coronal and dental root decay, and in endocarditis. Comparative study of the amino acid sequence of
S. mutans 47
kDa wall-associated protein A (WapA) revealed a collagen-binding domain (CBD) at the N-terminal region. Recombinant AgA (WapA truncated at the carboxyterminal end) was isolated, biotin-labeled, and analyzed by Solid Phase Binding Assay. The results showed that biotin-labeled AgA bound significantly and in a dose-dependent manner to immobilized collagen type I, and to a lesser extent to fibronectin, but not to collagen type IV or laminin. Binding of biotin-labeled
S. mutans cells to collagen-coated surfaces was significantly inhibited by antibody to WapA or AgA (
P
<
0.001). The results obtained confirmed the collagen-binding activity of CBD in AgA and WapA, and suggested that WapA may be used, not only as a vaccine against coronal and dental root caries, but also against
S. mutans-mediated endocarditis.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>16563343</pmid><doi>10.1016/j.bbrc.2006.03.025</doi><tpages>6</tpages></addata></record> |
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| subjects | Amino Acid Sequence Antibodies, Bacterial - pharmacology Antigens, Bacterial - chemistry Antigens, Bacterial - immunology Antigens, Bacterial - metabolism Bacterial Proteins - chemistry Bacterial Proteins - immunology Bacterial Proteins - metabolism Binding Sites Collagen Type I - metabolism Collagen-binding activity Consensus Sequence Dental root decay Endocarditis Endocarditis, Bacterial - microbiology Molecular Sequence Data Protein Structure, Tertiary Root Caries - microbiology Sequence Alignment Streptococcus mutans Streptococcus mutans - immunology Streptococcus mutans - pathogenicity Wall-associated protein A |
| title | Identification and characterization of collagen-binding activity in Streptococcus mutans wall-associated protein: A possible implication in dental root caries and endocarditis |
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