American Oyster, Crassostrea virginica, Expresses a Potent Antibacterial Histone H2B Protein
An antibacterial protein was purified from acidified gill extract of a bivalve mollusk, the American oyster (Crassostrea virginica). Protein isolation was best accomplished by briefly boiling the tissues in a weak acetic acid solution. Adding protease inhibitors while boiling did not have a major ef...
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| Veröffentlicht in: | Marine biotechnology (New York, N.Y.) N.Y.), 2010-10, Vol.12 (5), p.543-551 |
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| creator | Seo, Jung-Kil Stephenson, Jeana Crawford, J. Myron Stone, Kathryn L Noga, Edward J |
| description | An antibacterial protein was purified from acidified gill extract of a bivalve mollusk, the American oyster (Crassostrea virginica). Protein isolation was best accomplished by briefly boiling the tissues in a weak acetic acid solution. Adding protease inhibitors while boiling did not have a major effect on activity recovery. In contrast, use of only protease inhibitors (without boiling) resulted in virtually no recovery of this activity. The amino acid sequence of this antibacterial protein was identified as a histone H2B and was designated cvH2B. cvH2B had potent activity against gram-negative bacteria, including the human pathogens Vibrio parahaemolyticus and Vibrio vulnificus, which commonly reside in oyster tissues. We estimated that the concentration of this protein was well within the concentration that was inhibitory to these bacterial pathogens in vitro. This is the first report of the antimicrobial function of histone H2B from any mollusk. |
| doi_str_mv | 10.1007/s10126-009-9240-z |
| format | Article |
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We estimated that the concentration of this protein was well within the concentration that was inhibitory to these bacterial pathogens in vitro. This is the first report of the antimicrobial function of histone H2B from any mollusk.</description><identifier>ISSN: 1436-2228</identifier><identifier>EISSN: 1436-2236</identifier><identifier>DOI: 10.1007/s10126-009-9240-z</identifier><identifier>PMID: 19949827</identifier><language>eng</language><publisher>New York: New York : Springer-Verlag</publisher><subject>Acetic acid ; Acidification ; Amino Acid Sequence ; Amino acid sequences ; Amino acids ; Animals ; Anti-Bacterial Agents - chemistry ; Anti-Bacterial Agents - metabolism ; Anti-Bacterial Agents - pharmacology ; Antimicrobial protein ; Bacteria ; Bacteriology ; Biomedical and Life Sciences ; Biotechnology ; Boiling ; Cell Survival - drug effects ; Crassostrea virginica ; DNA ; Engineering ; Freshwater & Marine Ecology ; Gram-negative bacteria ; Histone H2B ; Histones ; Histones - chemistry ; Histones - metabolism ; Histones - pharmacology ; immunity ; In vitro methods and tests ; Inhibitors ; Life Sciences ; Marine biology ; Marine molluscs ; Microbiology ; Molecular Sequence Data ; Mollusks ; Original Article ; Ostreidae - metabolism ; Oysters ; Pathogens ; Protease ; Protease inhibitors ; Proteinase ; Proteinase inhibitors ; Proteins ; Recovery ; Sequencing ; Studies ; Tissue ; United States ; Vibrio - cytology ; Vibrio - drug effects ; Waterborne diseases ; Zoology</subject><ispartof>Marine biotechnology (New York, N.Y.), 2010-10, Vol.12 (5), p.543-551</ispartof><rights>Springer Science+Business Media, LLC 2009</rights><rights>Marine Biotechnology is a copyright of Springer, 2010.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c461t-9d555852d48e00082ba157c57dd25d76640b61d49b0908f12929734d0f1af48a3</citedby><cites>FETCH-LOGICAL-c461t-9d555852d48e00082ba157c57dd25d76640b61d49b0908f12929734d0f1af48a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s10126-009-9240-z$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s10126-009-9240-z$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19949827$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Seo, Jung-Kil</creatorcontrib><creatorcontrib>Stephenson, Jeana</creatorcontrib><creatorcontrib>Crawford, J. Myron</creatorcontrib><creatorcontrib>Stone, Kathryn L</creatorcontrib><creatorcontrib>Noga, Edward J</creatorcontrib><title>American Oyster, Crassostrea virginica, Expresses a Potent Antibacterial Histone H2B Protein</title><title>Marine biotechnology (New York, N.Y.)</title><addtitle>Mar Biotechnol</addtitle><addtitle>Mar Biotechnol (NY)</addtitle><description>An antibacterial protein was purified from acidified gill extract of a bivalve mollusk, the American oyster (Crassostrea virginica). Protein isolation was best accomplished by briefly boiling the tissues in a weak acetic acid solution. Adding protease inhibitors while boiling did not have a major effect on activity recovery. In contrast, use of only protease inhibitors (without boiling) resulted in virtually no recovery of this activity. The amino acid sequence of this antibacterial protein was identified as a histone H2B and was designated cvH2B. cvH2B had potent activity against gram-negative bacteria, including the human pathogens Vibrio parahaemolyticus and Vibrio vulnificus, which commonly reside in oyster tissues. We estimated that the concentration of this protein was well within the concentration that was inhibitory to these bacterial pathogens in vitro. This is the first report of the antimicrobial function of histone H2B from any mollusk.</description><subject>Acetic acid</subject><subject>Acidification</subject><subject>Amino Acid Sequence</subject><subject>Amino acid sequences</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Anti-Bacterial Agents - chemistry</subject><subject>Anti-Bacterial Agents - metabolism</subject><subject>Anti-Bacterial Agents - pharmacology</subject><subject>Antimicrobial protein</subject><subject>Bacteria</subject><subject>Bacteriology</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnology</subject><subject>Boiling</subject><subject>Cell Survival - drug effects</subject><subject>Crassostrea virginica</subject><subject>DNA</subject><subject>Engineering</subject><subject>Freshwater & Marine Ecology</subject><subject>Gram-negative bacteria</subject><subject>Histone H2B</subject><subject>Histones</subject><subject>Histones - chemistry</subject><subject>Histones - metabolism</subject><subject>Histones - pharmacology</subject><subject>immunity</subject><subject>In vitro methods and tests</subject><subject>Inhibitors</subject><subject>Life Sciences</subject><subject>Marine biology</subject><subject>Marine molluscs</subject><subject>Microbiology</subject><subject>Molecular Sequence Data</subject><subject>Mollusks</subject><subject>Original Article</subject><subject>Ostreidae - metabolism</subject><subject>Oysters</subject><subject>Pathogens</subject><subject>Protease</subject><subject>Protease inhibitors</subject><subject>Proteinase</subject><subject>Proteinase inhibitors</subject><subject>Proteins</subject><subject>Recovery</subject><subject>Sequencing</subject><subject>Studies</subject><subject>Tissue</subject><subject>United States</subject><subject>Vibrio - cytology</subject><subject>Vibrio - drug effects</subject><subject>Waterborne diseases</subject><subject>Zoology</subject><issn>1436-2228</issn><issn>1436-2236</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNp9kE2LFDEQhoMo7of-AC8a8OBlW6vS6Xwcx2HXERZ2QfcmhHR3esgykx5TPeLurzdDDyoePKWgnvdN8TD2CuE9AugPhIBCVQC2skJC9fiEnaKsVSVErZ7-noU5YWdE91Ayuobn7AStldYIfcq-LbYhx84nfvNAU8gXfJk90UhTDp7_iHkdU1lf8MufuxyIAnHPb8cppIkv0hRb35VU9Bu-ijSNKfCV-MhvcyFiesGeDX5D4eXxPWd3V5dfl6vq-ubT5-XiuuqkwqmyfdM0phG9NKHcaETrsdFdo_teNL1WSkKrsJe2BQtmQGGF1bXsYUA_SOPrc_Zu7t3l8fs-0OS2kbqw2fgUxj053Shz0KAL-fYf8n7c51SOc2iFMlqAEoXCmerySJTD4HY5bn1-cAjuYN7N5l0x7w7m3WPJvD4279tt6P8kjqoLIGaAyiqtQ_7r6_-0vplDgx-dX-dI7u6LAKwBbVGFpv4F71aV_A</recordid><startdate>20101001</startdate><enddate>20101001</enddate><creator>Seo, Jung-Kil</creator><creator>Stephenson, Jeana</creator><creator>Crawford, J. 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Myron</au><au>Stone, Kathryn L</au><au>Noga, Edward J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>American Oyster, Crassostrea virginica, Expresses a Potent Antibacterial Histone H2B Protein</atitle><jtitle>Marine biotechnology (New York, N.Y.)</jtitle><stitle>Mar Biotechnol</stitle><addtitle>Mar Biotechnol (NY)</addtitle><date>2010-10-01</date><risdate>2010</risdate><volume>12</volume><issue>5</issue><spage>543</spage><epage>551</epage><pages>543-551</pages><issn>1436-2228</issn><eissn>1436-2236</eissn><abstract>An antibacterial protein was purified from acidified gill extract of a bivalve mollusk, the American oyster (Crassostrea virginica). Protein isolation was best accomplished by briefly boiling the tissues in a weak acetic acid solution. Adding protease inhibitors while boiling did not have a major effect on activity recovery. In contrast, use of only protease inhibitors (without boiling) resulted in virtually no recovery of this activity. The amino acid sequence of this antibacterial protein was identified as a histone H2B and was designated cvH2B. cvH2B had potent activity against gram-negative bacteria, including the human pathogens Vibrio parahaemolyticus and Vibrio vulnificus, which commonly reside in oyster tissues. We estimated that the concentration of this protein was well within the concentration that was inhibitory to these bacterial pathogens in vitro. This is the first report of the antimicrobial function of histone H2B from any mollusk.</abstract><cop>New York</cop><pub>New York : Springer-Verlag</pub><pmid>19949827</pmid><doi>10.1007/s10126-009-9240-z</doi><tpages>9</tpages></addata></record> |
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| ispartof | Marine biotechnology (New York, N.Y.), 2010-10, Vol.12 (5), p.543-551 |
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| subjects | Acetic acid Acidification Amino Acid Sequence Amino acid sequences Amino acids Animals Anti-Bacterial Agents - chemistry Anti-Bacterial Agents - metabolism Anti-Bacterial Agents - pharmacology Antimicrobial protein Bacteria Bacteriology Biomedical and Life Sciences Biotechnology Boiling Cell Survival - drug effects Crassostrea virginica DNA Engineering Freshwater & Marine Ecology Gram-negative bacteria Histone H2B Histones Histones - chemistry Histones - metabolism Histones - pharmacology immunity In vitro methods and tests Inhibitors Life Sciences Marine biology Marine molluscs Microbiology Molecular Sequence Data Mollusks Original Article Ostreidae - metabolism Oysters Pathogens Protease Protease inhibitors Proteinase Proteinase inhibitors Proteins Recovery Sequencing Studies Tissue United States Vibrio - cytology Vibrio - drug effects Waterborne diseases Zoology |
| title | American Oyster, Crassostrea virginica, Expresses a Potent Antibacterial Histone H2B Protein |
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