The bovine salivary proteins BSP30a and BSP30b are independently expressed BPI-like proteins with anti- Pseudomonas activity
The family of BPI-like proteins are thought to play a role in innate immunity of the airways and oral cavity. They have similarities with bactericidal/permeability-increasing protein (BPI), an important host defence molecule in mammals, in the nucleotide sequence of their mRNAs, organisation of exon...
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| Veröffentlicht in: | Molecular immunology 2008-04, Vol.45 (7), p.1944-1951 |
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| container_end_page | 1951 |
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| container_issue | 7 |
| container_start_page | 1944 |
| container_title | Molecular immunology |
| container_volume | 45 |
| creator | Haigh, B. Hood, K. Broadhurst, M. Medele, S. Callaghan, M. Smolenski, G. Dines, M. Wheeler, T. |
| description | The family of BPI-like proteins are thought to play a role in innate immunity of the airways and oral cavity. They have similarities with bactericidal/permeability-increasing protein (BPI), an important host defence molecule in mammals, in the nucleotide sequence of their mRNAs, organisation of exons and their predicted protein structure. We compared the expression and function of 2 of the 13 known bovine BPI-like proteins, BSP30a and b, which together constitute 30% of the total protein in bovine saliva. Despite their recent divergence, we found that the two proteins have unique expression patterns, considerable inter- and intra-animal variation in abundance and differ in their glycosylation status. Recombinant and native BSP30a and b exhibited growth suppression activity against
Pseudomonas aeruginosa and
Streptococcus pneumoniae. Native BSP30a and b had no significant lipopolysaccharide-binding activity. These data provide functional evidence supporting a role for the BPI-like proteins in host defence and suggest that BSP30a and b contribute to the growth suppression function of bovine saliva through a mechanism independent of LPS opsonisation. |
| doi_str_mv | 10.1016/j.molimm.2007.10.032 |
| format | Article |
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Pseudomonas aeruginosa and
Streptococcus pneumoniae. Native BSP30a and b had no significant lipopolysaccharide-binding activity. These data provide functional evidence supporting a role for the BPI-like proteins in host defence and suggest that BSP30a and b contribute to the growth suppression function of bovine saliva through a mechanism independent of LPS opsonisation.</description><identifier>ISSN: 0161-5890</identifier><identifier>EISSN: 1872-9142</identifier><identifier>DOI: 10.1016/j.molimm.2007.10.032</identifier><identifier>PMID: 18055015</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Animals ; Anti-Bacterial Agents - metabolism ; Anti-Bacterial Agents - pharmacology ; Antibody Specificity - drug effects ; Antimicrobial Cationic Peptides - metabolism ; Blood Proteins - metabolism ; BPI-like protein ; BSP30 ; Cattle ; Glycosylation - drug effects ; Innate immunity ; Lipopolysaccharides - metabolism ; Membrane Proteins - metabolism ; Microbial Sensitivity Tests ; Pseudomonas aeruginosa ; Pseudomonas aeruginosa - drug effects ; Pseudomonas aeruginosa - growth & development ; Recombinant Proteins - isolation & purification ; Recombinant Proteins - pharmacology ; Saliva ; Saliva - chemistry ; Saliva - drug effects ; Salivary Glands - drug effects ; Salivary Glands - metabolism ; Salivary Proteins and Peptides - isolation & purification ; Salivary Proteins and Peptides - metabolism ; Salivary Proteins and Peptides - pharmacology ; Streptococcus pneumoniae</subject><ispartof>Molecular immunology, 2008-04, Vol.45 (7), p.1944-1951</ispartof><rights>2007 Elsevier Ltd</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c423t-23c2357157097b70f976930d0e7ab0f3a5f55c0fc29fb5eedadcf6351ac6a0133</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.molimm.2007.10.032$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18055015$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Haigh, B.</creatorcontrib><creatorcontrib>Hood, K.</creatorcontrib><creatorcontrib>Broadhurst, M.</creatorcontrib><creatorcontrib>Medele, S.</creatorcontrib><creatorcontrib>Callaghan, M.</creatorcontrib><creatorcontrib>Smolenski, G.</creatorcontrib><creatorcontrib>Dines, M.</creatorcontrib><creatorcontrib>Wheeler, T.</creatorcontrib><title>The bovine salivary proteins BSP30a and BSP30b are independently expressed BPI-like proteins with anti- Pseudomonas activity</title><title>Molecular immunology</title><addtitle>Mol Immunol</addtitle><description>The family of BPI-like proteins are thought to play a role in innate immunity of the airways and oral cavity. They have similarities with bactericidal/permeability-increasing protein (BPI), an important host defence molecule in mammals, in the nucleotide sequence of their mRNAs, organisation of exons and their predicted protein structure. We compared the expression and function of 2 of the 13 known bovine BPI-like proteins, BSP30a and b, which together constitute 30% of the total protein in bovine saliva. Despite their recent divergence, we found that the two proteins have unique expression patterns, considerable inter- and intra-animal variation in abundance and differ in their glycosylation status. Recombinant and native BSP30a and b exhibited growth suppression activity against
Pseudomonas aeruginosa and
Streptococcus pneumoniae. Native BSP30a and b had no significant lipopolysaccharide-binding activity. These data provide functional evidence supporting a role for the BPI-like proteins in host defence and suggest that BSP30a and b contribute to the growth suppression function of bovine saliva through a mechanism independent of LPS opsonisation.</description><subject>Animals</subject><subject>Anti-Bacterial Agents - metabolism</subject><subject>Anti-Bacterial Agents - pharmacology</subject><subject>Antibody Specificity - drug effects</subject><subject>Antimicrobial Cationic Peptides - metabolism</subject><subject>Blood Proteins - metabolism</subject><subject>BPI-like protein</subject><subject>BSP30</subject><subject>Cattle</subject><subject>Glycosylation - drug effects</subject><subject>Innate immunity</subject><subject>Lipopolysaccharides - metabolism</subject><subject>Membrane Proteins - metabolism</subject><subject>Microbial Sensitivity Tests</subject><subject>Pseudomonas aeruginosa</subject><subject>Pseudomonas aeruginosa - drug effects</subject><subject>Pseudomonas aeruginosa - growth & development</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Recombinant Proteins - pharmacology</subject><subject>Saliva</subject><subject>Saliva - chemistry</subject><subject>Saliva - drug effects</subject><subject>Salivary Glands - drug effects</subject><subject>Salivary Glands - metabolism</subject><subject>Salivary Proteins and Peptides - isolation & purification</subject><subject>Salivary Proteins and Peptides - metabolism</subject><subject>Salivary Proteins and Peptides - pharmacology</subject><subject>Streptococcus pneumoniae</subject><issn>0161-5890</issn><issn>1872-9142</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU9vEzEQxS0EomnKN0DIJzhtOrbX690LElQUKlUiUsvZ8tqzqsP-CbYTiMSHx2Ej9dZexqPR772x5hHylsGKAasuN6th6v0wrDiAyqMVCP6CLFiteNGwkr8ki4yxQtYNnJHzGDcAUEElX5MzVoOUwOSC_L1_QNpOez8ijab3exMOdBumhH6M9PPdWoChZnRz21ITkPrR4RZzGVN_oPhnGzBGzMj6puj9T3zU__bpIauTL-g64s5NwzSaSI1Nfu_T4YK86kwf8c3pXZIf11_ur74Vt9-_3lx9ui1syUUquLBcSMWkgka1CrpGVY0AB6hMC50wspPSQmd507US0Rlnu0pIZmxlgAmxJB9m3_yxXzuMSQ8-Wux7M-K0i7quBYiGM5bJ90-SCsTRkD8LsqaCsszGS1LOoA1TjAE7vQ1-yFfWDPQxSL3Rc5D6GORxCv_93538d-2A7lF0Si4DH2cA8-H2HoOO1uNo0fmANmk3-ac3_ANarrEC</recordid><startdate>20080401</startdate><enddate>20080401</enddate><creator>Haigh, B.</creator><creator>Hood, K.</creator><creator>Broadhurst, M.</creator><creator>Medele, S.</creator><creator>Callaghan, M.</creator><creator>Smolenski, G.</creator><creator>Dines, M.</creator><creator>Wheeler, T.</creator><general>Elsevier Ltd</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>7T5</scope><scope>C1K</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>20080401</creationdate><title>The bovine salivary proteins BSP30a and BSP30b are independently expressed BPI-like proteins with anti- Pseudomonas activity</title><author>Haigh, B. ; Hood, K. ; Broadhurst, M. ; Medele, S. ; Callaghan, M. ; Smolenski, G. ; Dines, M. ; Wheeler, T.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c423t-23c2357157097b70f976930d0e7ab0f3a5f55c0fc29fb5eedadcf6351ac6a0133</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Animals</topic><topic>Anti-Bacterial Agents - metabolism</topic><topic>Anti-Bacterial Agents - pharmacology</topic><topic>Antibody Specificity - drug effects</topic><topic>Antimicrobial Cationic Peptides - metabolism</topic><topic>Blood Proteins - metabolism</topic><topic>BPI-like protein</topic><topic>BSP30</topic><topic>Cattle</topic><topic>Glycosylation - drug effects</topic><topic>Innate immunity</topic><topic>Lipopolysaccharides - metabolism</topic><topic>Membrane Proteins - metabolism</topic><topic>Microbial Sensitivity Tests</topic><topic>Pseudomonas aeruginosa</topic><topic>Pseudomonas aeruginosa - drug effects</topic><topic>Pseudomonas aeruginosa - growth & development</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Recombinant Proteins - pharmacology</topic><topic>Saliva</topic><topic>Saliva - chemistry</topic><topic>Saliva - drug effects</topic><topic>Salivary Glands - drug effects</topic><topic>Salivary Glands - metabolism</topic><topic>Salivary Proteins and Peptides - isolation & purification</topic><topic>Salivary Proteins and Peptides - metabolism</topic><topic>Salivary Proteins and Peptides - pharmacology</topic><topic>Streptococcus pneumoniae</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Haigh, B.</creatorcontrib><creatorcontrib>Hood, K.</creatorcontrib><creatorcontrib>Broadhurst, M.</creatorcontrib><creatorcontrib>Medele, S.</creatorcontrib><creatorcontrib>Callaghan, M.</creatorcontrib><creatorcontrib>Smolenski, G.</creatorcontrib><creatorcontrib>Dines, M.</creatorcontrib><creatorcontrib>Wheeler, T.</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>Immunology Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular immunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Haigh, B.</au><au>Hood, K.</au><au>Broadhurst, M.</au><au>Medele, S.</au><au>Callaghan, M.</au><au>Smolenski, G.</au><au>Dines, M.</au><au>Wheeler, T.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The bovine salivary proteins BSP30a and BSP30b are independently expressed BPI-like proteins with anti- Pseudomonas activity</atitle><jtitle>Molecular immunology</jtitle><addtitle>Mol Immunol</addtitle><date>2008-04-01</date><risdate>2008</risdate><volume>45</volume><issue>7</issue><spage>1944</spage><epage>1951</epage><pages>1944-1951</pages><issn>0161-5890</issn><eissn>1872-9142</eissn><abstract>The family of BPI-like proteins are thought to play a role in innate immunity of the airways and oral cavity. They have similarities with bactericidal/permeability-increasing protein (BPI), an important host defence molecule in mammals, in the nucleotide sequence of their mRNAs, organisation of exons and their predicted protein structure. We compared the expression and function of 2 of the 13 known bovine BPI-like proteins, BSP30a and b, which together constitute 30% of the total protein in bovine saliva. Despite their recent divergence, we found that the two proteins have unique expression patterns, considerable inter- and intra-animal variation in abundance and differ in their glycosylation status. Recombinant and native BSP30a and b exhibited growth suppression activity against
Pseudomonas aeruginosa and
Streptococcus pneumoniae. Native BSP30a and b had no significant lipopolysaccharide-binding activity. These data provide functional evidence supporting a role for the BPI-like proteins in host defence and suggest that BSP30a and b contribute to the growth suppression function of bovine saliva through a mechanism independent of LPS opsonisation.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>18055015</pmid><doi>10.1016/j.molimm.2007.10.032</doi><tpages>8</tpages></addata></record> |
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| ispartof | Molecular immunology, 2008-04, Vol.45 (7), p.1944-1951 |
| issn | 0161-5890 1872-9142 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Animals Anti-Bacterial Agents - metabolism Anti-Bacterial Agents - pharmacology Antibody Specificity - drug effects Antimicrobial Cationic Peptides - metabolism Blood Proteins - metabolism BPI-like protein BSP30 Cattle Glycosylation - drug effects Innate immunity Lipopolysaccharides - metabolism Membrane Proteins - metabolism Microbial Sensitivity Tests Pseudomonas aeruginosa Pseudomonas aeruginosa - drug effects Pseudomonas aeruginosa - growth & development Recombinant Proteins - isolation & purification Recombinant Proteins - pharmacology Saliva Saliva - chemistry Saliva - drug effects Salivary Glands - drug effects Salivary Glands - metabolism Salivary Proteins and Peptides - isolation & purification Salivary Proteins and Peptides - metabolism Salivary Proteins and Peptides - pharmacology Streptococcus pneumoniae |
| title | The bovine salivary proteins BSP30a and BSP30b are independently expressed BPI-like proteins with anti- Pseudomonas activity |
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