Human Serum Albumin Enhances the Hemolytic Activity of Vibrio vulnificus
Vibrio vulnificus hemolysin (VvhA) is inactivated in the late growth phase by its oligomerization. Albumin is known to affect the activities of many bacterial toxins. In this study, we investigated the effects of human or bovine serum albumin (HSA or BSA) on the production and activity of VvhA. HSA...
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| Veröffentlicht in: | Biological & pharmaceutical bulletin 2006, Vol.29(1), pp.180-182 |
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| creator | Choi, Mi-Hwa Sun, Hui-Yu Park, Ra-Young Bai, Young-Hoon Chung, Yoon-Young Kim, Choon-Mee Shin, Sung-Heui |
| description | Vibrio vulnificus hemolysin (VvhA) is inactivated in the late growth phase by its oligomerization. Albumin is known to affect the activities of many bacterial toxins. In this study, we investigated the effects of human or bovine serum albumin (HSA or BSA) on the production and activity of VvhA. HSA did not affect V. vulnificus growth and vvhA transcription. However, VvhA hemolytic activity in culture supernatants was significantly higher in the presence of HSA than in the absence of HSA. By Western blot analysis, the oligomerization of VvhA was inhibited and the remaining active VvhA monomer was increased in culture supernatants containing HSA. BSA produced similar results. These findings indicate that both HSA and BSA stabilize VvhA and delay VvhA inactivation by oligomerization, and thus enhance VvhA activity. |
| doi_str_mv | 10.1248/bpb.29.180 |
| format | Article |
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Albumin is known to affect the activities of many bacterial toxins. In this study, we investigated the effects of human or bovine serum albumin (HSA or BSA) on the production and activity of VvhA. HSA did not affect V. vulnificus growth and vvhA transcription. However, VvhA hemolytic activity in culture supernatants was significantly higher in the presence of HSA than in the absence of HSA. By Western blot analysis, the oligomerization of VvhA was inhibited and the remaining active VvhA monomer was increased in culture supernatants containing HSA. BSA produced similar results. These findings indicate that both HSA and BSA stabilize VvhA and delay VvhA inactivation by oligomerization, and thus enhance VvhA activity.</description><identifier>ISSN: 0918-6158</identifier><identifier>EISSN: 1347-5215</identifier><identifier>DOI: 10.1248/bpb.29.180</identifier><identifier>PMID: 16394536</identifier><language>eng</language><publisher>Japan: The Pharmaceutical Society of Japan</publisher><subject>Animals ; Bacterial Proteins - pharmacology ; beta-Galactosidase - blood ; Blotting, Western ; bovine serum albumin ; Cattle ; Drug Synergism ; Electrophoresis, Polyacrylamide Gel ; hemolysin ; Hemolysin Proteins ; Hemolysis - drug effects ; human serum albumin ; Humans ; In Vitro Techniques ; Serum Albumin - pharmacology ; Serum Albumin, Bovine - pharmacology ; Vibrio vulnificus ; Vibrio vulnificus - chemistry</subject><ispartof>Biological and Pharmaceutical Bulletin, 2006, Vol.29(1), pp.180-182</ispartof><rights>2006 The Pharmaceutical Society of Japan</rights><rights>Copyright Japan Science and Technology Agency 2006</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c552t-a7f476d8d3e15c94cf7e6c22cf129dc9711fda6f547bc748d9d363979c21a57e3</citedby><cites>FETCH-LOGICAL-c552t-a7f476d8d3e15c94cf7e6c22cf129dc9711fda6f547bc748d9d363979c21a57e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,1877,4010,27900,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16394536$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Choi, Mi-Hwa</creatorcontrib><creatorcontrib>Sun, Hui-Yu</creatorcontrib><creatorcontrib>Park, Ra-Young</creatorcontrib><creatorcontrib>Bai, Young-Hoon</creatorcontrib><creatorcontrib>Chung, Yoon-Young</creatorcontrib><creatorcontrib>Kim, Choon-Mee</creatorcontrib><creatorcontrib>Shin, Sung-Heui</creatorcontrib><title>Human Serum Albumin Enhances the Hemolytic Activity of Vibrio vulnificus</title><title>Biological & pharmaceutical bulletin</title><addtitle>Biol Pharm Bull</addtitle><description>Vibrio vulnificus hemolysin (VvhA) is inactivated in the late growth phase by its oligomerization. Albumin is known to affect the activities of many bacterial toxins. In this study, we investigated the effects of human or bovine serum albumin (HSA or BSA) on the production and activity of VvhA. HSA did not affect V. vulnificus growth and vvhA transcription. However, VvhA hemolytic activity in culture supernatants was significantly higher in the presence of HSA than in the absence of HSA. By Western blot analysis, the oligomerization of VvhA was inhibited and the remaining active VvhA monomer was increased in culture supernatants containing HSA. BSA produced similar results. These findings indicate that both HSA and BSA stabilize VvhA and delay VvhA inactivation by oligomerization, and thus enhance VvhA activity.</description><subject>Animals</subject><subject>Bacterial Proteins - pharmacology</subject><subject>beta-Galactosidase - blood</subject><subject>Blotting, Western</subject><subject>bovine serum albumin</subject><subject>Cattle</subject><subject>Drug Synergism</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>hemolysin</subject><subject>Hemolysin Proteins</subject><subject>Hemolysis - drug effects</subject><subject>human serum albumin</subject><subject>Humans</subject><subject>In Vitro Techniques</subject><subject>Serum Albumin - pharmacology</subject><subject>Serum Albumin, Bovine - pharmacology</subject><subject>Vibrio vulnificus</subject><subject>Vibrio vulnificus - chemistry</subject><issn>0918-6158</issn><issn>1347-5215</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkMtKAzEUQIMotlY3foAE3AlTJ6_JZCWlVEcouPCxDZlMYlPmUZOZQv_eyJS6yV3kcO7lAHCL0jnCNH8sd-UciznK0zMwRYTyhGHEzsE0FShPMsTyCbgKYZumKU8xuQQTlBFBGcmmoCiGRrXw3fihgYu6HBrXwlW7Ua02AfYbAwvTdPWhdxoudO_2rj_AzsIvV3rXwf1Qt846PYRrcGFVHczNcc7A5_PqY1kk67eX1-VinWjGcJ8obinPqrwiBjEtqLbcZBpjbREWlRYcIVupzDLKS81pXomKxGO50Bgpxg2ZgfvRu_Pdz2BCL7fd4Nu4UiJKBWEC5yhSDyOlfReCN1buvGuUP0iUyr9oMkaTWMgYLcJ3R-VQNqb6R4-VIvA0AtvQq29zApSPWWpzco1PVJ5-9EZ5aVryCyQ6fgc</recordid><startdate>2006</startdate><enddate>2006</enddate><creator>Choi, Mi-Hwa</creator><creator>Sun, Hui-Yu</creator><creator>Park, Ra-Young</creator><creator>Bai, Young-Hoon</creator><creator>Chung, Yoon-Young</creator><creator>Kim, Choon-Mee</creator><creator>Shin, Sung-Heui</creator><general>The Pharmaceutical Society of Japan</general><general>Japan Science and Technology Agency</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>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7U9</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope></search><sort><creationdate>2006</creationdate><title>Human Serum Albumin Enhances the Hemolytic Activity of Vibrio vulnificus</title><author>Choi, Mi-Hwa ; Sun, Hui-Yu ; Park, Ra-Young ; Bai, Young-Hoon ; Chung, Yoon-Young ; Kim, Choon-Mee ; Shin, Sung-Heui</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c552t-a7f476d8d3e15c94cf7e6c22cf129dc9711fda6f547bc748d9d363979c21a57e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Animals</topic><topic>Bacterial Proteins - pharmacology</topic><topic>beta-Galactosidase - blood</topic><topic>Blotting, Western</topic><topic>bovine serum albumin</topic><topic>Cattle</topic><topic>Drug Synergism</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>hemolysin</topic><topic>Hemolysin Proteins</topic><topic>Hemolysis - drug effects</topic><topic>human serum albumin</topic><topic>Humans</topic><topic>In Vitro Techniques</topic><topic>Serum Albumin - pharmacology</topic><topic>Serum Albumin, Bovine - pharmacology</topic><topic>Vibrio vulnificus</topic><topic>Vibrio vulnificus - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Choi, Mi-Hwa</creatorcontrib><creatorcontrib>Sun, Hui-Yu</creatorcontrib><creatorcontrib>Park, Ra-Young</creatorcontrib><creatorcontrib>Bai, Young-Hoon</creatorcontrib><creatorcontrib>Chung, Yoon-Young</creatorcontrib><creatorcontrib>Kim, Choon-Mee</creatorcontrib><creatorcontrib>Shin, Sung-Heui</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Biological & pharmaceutical bulletin</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Choi, Mi-Hwa</au><au>Sun, Hui-Yu</au><au>Park, Ra-Young</au><au>Bai, Young-Hoon</au><au>Chung, Yoon-Young</au><au>Kim, Choon-Mee</au><au>Shin, Sung-Heui</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Human Serum Albumin Enhances the Hemolytic Activity of Vibrio vulnificus</atitle><jtitle>Biological & pharmaceutical bulletin</jtitle><addtitle>Biol Pharm Bull</addtitle><date>2006</date><risdate>2006</risdate><volume>29</volume><issue>1</issue><spage>180</spage><epage>182</epage><pages>180-182</pages><issn>0918-6158</issn><eissn>1347-5215</eissn><abstract>Vibrio vulnificus hemolysin (VvhA) is inactivated in the late growth phase by its oligomerization. Albumin is known to affect the activities of many bacterial toxins. In this study, we investigated the effects of human or bovine serum albumin (HSA or BSA) on the production and activity of VvhA. HSA did not affect V. vulnificus growth and vvhA transcription. However, VvhA hemolytic activity in culture supernatants was significantly higher in the presence of HSA than in the absence of HSA. By Western blot analysis, the oligomerization of VvhA was inhibited and the remaining active VvhA monomer was increased in culture supernatants containing HSA. BSA produced similar results. These findings indicate that both HSA and BSA stabilize VvhA and delay VvhA inactivation by oligomerization, and thus enhance VvhA activity.</abstract><cop>Japan</cop><pub>The Pharmaceutical Society of Japan</pub><pmid>16394536</pmid><doi>10.1248/bpb.29.180</doi><tpages>3</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Bacterial Proteins - pharmacology beta-Galactosidase - blood Blotting, Western bovine serum albumin Cattle Drug Synergism Electrophoresis, Polyacrylamide Gel hemolysin Hemolysin Proteins Hemolysis - drug effects human serum albumin Humans In Vitro Techniques Serum Albumin - pharmacology Serum Albumin, Bovine - pharmacology Vibrio vulnificus Vibrio vulnificus - chemistry |
| title | Human Serum Albumin Enhances the Hemolytic Activity of Vibrio vulnificus |
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