Differential assembly of Hepatitis B Virus core protein on single- and double-stranded nucleic acid suggest the dsDNA-filled core is spring-loaded
Abstract Hepatitis B Virus (HBV) cores assemble on viral RNA, which is reverse transcribed within the core to the partially dsDNA genome of mature HBV. However, constraining dsDNA, a stiff polymer, within a core necessarily requires far greater capsid stability than constraining ssRNA. We hypothesiz...
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| Veröffentlicht in: | Virology (New York, N.Y.) N.Y.), 2012-08, Vol.430 (1), p.20-29 |
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| creator | Dhason, Mary S Wang, Joseph C.-Y Hagan, Michael F Zlotnick, Adam |
| description | Abstract Hepatitis B Virus (HBV) cores assemble on viral RNA, which is reverse transcribed within the core to the partially dsDNA genome of mature HBV. However, constraining dsDNA, a stiff polymer, within a core necessarily requires far greater capsid stability than constraining ssRNA. We hypothesized that, unlike ssRNA, dsDNA would be a poor substrate for assembly. We examined titrations of ssDNA and dsDNA with purified HBV core protein, Cp183, by EMSA, EM, DLS, and etheno-DNA fluorescence. Cp183 bound ssDNA with high affinity to form virus-like capsids. However, Cp183 bound dsDNA poorly, forming a mixture of irregular complexes. Nonetheless, we observed some normal cores in dsDNA assembly reactions, indicating that the energy required to bend DNA could be similar to the protein–protein association energy. This similarity of energies suggests that dsDNA stresses mature HBV cores, in agreement with calculation, which may be the basis for the virus maturation signal and DNA release. |
| doi_str_mv | 10.1016/j.virol.2012.04.012 |
| format | Article |
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However, constraining dsDNA, a stiff polymer, within a core necessarily requires far greater capsid stability than constraining ssRNA. We hypothesized that, unlike ssRNA, dsDNA would be a poor substrate for assembly. We examined titrations of ssDNA and dsDNA with purified HBV core protein, Cp183, by EMSA, EM, DLS, and etheno-DNA fluorescence. Cp183 bound ssDNA with high affinity to form virus-like capsids. However, Cp183 bound dsDNA poorly, forming a mixture of irregular complexes. Nonetheless, we observed some normal cores in dsDNA assembly reactions, indicating that the energy required to bend DNA could be similar to the protein–protein association energy. This similarity of energies suggests that dsDNA stresses mature HBV cores, in agreement with calculation, which may be the basis for the virus maturation signal and DNA release.</description><identifier>ISSN: 0042-6822</identifier><identifier>EISSN: 1096-0341</identifier><identifier>DOI: 10.1016/j.virol.2012.04.012</identifier><identifier>PMID: 22595445</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Biophysics ; Capsid assembly ; DNA - metabolism ; DNA, Single-Stranded - metabolism ; DNA, Viral - metabolism ; DNA-binding ; Hepadnavirus ; Hepatitis B Core Antigens - metabolism ; Hepatitis B virus - genetics ; Hepatitis B virus - physiology ; Humans ; Infectious Disease ; RNA, Viral - metabolism ; RNA-binding ; Self-assembly ; Spumavirus ; Virus Assembly</subject><ispartof>Virology (New York, N.Y.), 2012-08, Vol.430 (1), p.20-29</ispartof><rights>Elsevier Inc.</rights><rights>2012 Elsevier Inc.</rights><rights>Copyright © 2012 Elsevier Inc. All rights reserved.</rights><rights>2012 Elsevier Inc. All rights reserved. 2012</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c514t-ff3598654e4a47975798b1b3cbefb3fb50d1a3a4f5441c7c07908684d5a9427d3</citedby><cites>FETCH-LOGICAL-c514t-ff3598654e4a47975798b1b3cbefb3fb50d1a3a4f5441c7c07908684d5a9427d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.virol.2012.04.012$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,780,784,885,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22595445$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Dhason, Mary S</creatorcontrib><creatorcontrib>Wang, Joseph C.-Y</creatorcontrib><creatorcontrib>Hagan, Michael F</creatorcontrib><creatorcontrib>Zlotnick, Adam</creatorcontrib><title>Differential assembly of Hepatitis B Virus core protein on single- and double-stranded nucleic acid suggest the dsDNA-filled core is spring-loaded</title><title>Virology (New York, N.Y.)</title><addtitle>Virology</addtitle><description>Abstract Hepatitis B Virus (HBV) cores assemble on viral RNA, which is reverse transcribed within the core to the partially dsDNA genome of mature HBV. However, constraining dsDNA, a stiff polymer, within a core necessarily requires far greater capsid stability than constraining ssRNA. We hypothesized that, unlike ssRNA, dsDNA would be a poor substrate for assembly. We examined titrations of ssDNA and dsDNA with purified HBV core protein, Cp183, by EMSA, EM, DLS, and etheno-DNA fluorescence. Cp183 bound ssDNA with high affinity to form virus-like capsids. However, Cp183 bound dsDNA poorly, forming a mixture of irregular complexes. Nonetheless, we observed some normal cores in dsDNA assembly reactions, indicating that the energy required to bend DNA could be similar to the protein–protein association energy. This similarity of energies suggests that dsDNA stresses mature HBV cores, in agreement with calculation, which may be the basis for the virus maturation signal and DNA release.</description><subject>Biophysics</subject><subject>Capsid assembly</subject><subject>DNA - metabolism</subject><subject>DNA, Single-Stranded - metabolism</subject><subject>DNA, Viral - metabolism</subject><subject>DNA-binding</subject><subject>Hepadnavirus</subject><subject>Hepatitis B Core Antigens - metabolism</subject><subject>Hepatitis B virus - genetics</subject><subject>Hepatitis B virus - physiology</subject><subject>Humans</subject><subject>Infectious Disease</subject><subject>RNA, Viral - metabolism</subject><subject>RNA-binding</subject><subject>Self-assembly</subject><subject>Spumavirus</subject><subject>Virus Assembly</subject><issn>0042-6822</issn><issn>1096-0341</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUstuFDEQHCEQ2QS-AAn5yGUGe-x5HYgUEiBIERx4XC2P3d548dqLPbPS_gZfnN7dEAEXTu2Wq6of1UXxgtGKUda-XlVbl6KvasrqiooKw6NiwejQlpQL9rhYUCrqsu3r-qQ4zXlFMe86-rQ4qetmaIRoFsWvK2ctJAiTU56onGE9-h2JllzDRk1ucpm8Jd9dmjPRMQHZpDiBCyQGkl1YeiiJCoaYOI_4zlPCDAwJs_bgNFHaGZLn5RLyRKZbICZffboorfMeUQdFrJA3CbVKHxVynxVPrPIZnt_Hs-Lb-3dfL6_Lm88fPl5e3JS6YWIqreXN0LeNAKFEN3RNN_QjG7kewY7cjg01THElLA7KdKdpN9C-7YVp1CDqzvCz4vyou5nHNRiNO0jKS2xlrdJORuXk3z_B3cpl3EqOW-QtQ4FX9wIp_pxxQLl2WYP3KkCcs0SXhpb1NeMI5UeoTjHnBPahDKN7XCtX8uCm3LspqZAYkPXyzw4fOL_tQ8CbIwBwT1sHSWbtIGgwLoGepInuPwXO_-Fr74LTyv-AHeRVnFNACySTGTnyy_6g9vfEanqYjd8BbdzJcg</recordid><startdate>20120815</startdate><enddate>20120815</enddate><creator>Dhason, Mary S</creator><creator>Wang, Joseph C.-Y</creator><creator>Hagan, Michael F</creator><creator>Zlotnick, Adam</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><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>7X8</scope><scope>5PM</scope></search><sort><creationdate>20120815</creationdate><title>Differential assembly of Hepatitis B Virus core protein on single- and double-stranded nucleic acid suggest the dsDNA-filled core is spring-loaded</title><author>Dhason, Mary S ; Wang, Joseph C.-Y ; Hagan, Michael F ; Zlotnick, Adam</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c514t-ff3598654e4a47975798b1b3cbefb3fb50d1a3a4f5441c7c07908684d5a9427d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Biophysics</topic><topic>Capsid assembly</topic><topic>DNA - metabolism</topic><topic>DNA, Single-Stranded - metabolism</topic><topic>DNA, Viral - metabolism</topic><topic>DNA-binding</topic><topic>Hepadnavirus</topic><topic>Hepatitis B Core Antigens - metabolism</topic><topic>Hepatitis B virus - genetics</topic><topic>Hepatitis B virus - physiology</topic><topic>Humans</topic><topic>Infectious Disease</topic><topic>RNA, Viral - metabolism</topic><topic>RNA-binding</topic><topic>Self-assembly</topic><topic>Spumavirus</topic><topic>Virus Assembly</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dhason, Mary S</creatorcontrib><creatorcontrib>Wang, Joseph C.-Y</creatorcontrib><creatorcontrib>Hagan, Michael F</creatorcontrib><creatorcontrib>Zlotnick, Adam</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Virology (New York, N.Y.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dhason, Mary S</au><au>Wang, Joseph C.-Y</au><au>Hagan, Michael F</au><au>Zlotnick, Adam</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Differential assembly of Hepatitis B Virus core protein on single- and double-stranded nucleic acid suggest the dsDNA-filled core is spring-loaded</atitle><jtitle>Virology (New York, N.Y.)</jtitle><addtitle>Virology</addtitle><date>2012-08-15</date><risdate>2012</risdate><volume>430</volume><issue>1</issue><spage>20</spage><epage>29</epage><pages>20-29</pages><issn>0042-6822</issn><eissn>1096-0341</eissn><abstract>Abstract Hepatitis B Virus (HBV) cores assemble on viral RNA, which is reverse transcribed within the core to the partially dsDNA genome of mature HBV. However, constraining dsDNA, a stiff polymer, within a core necessarily requires far greater capsid stability than constraining ssRNA. We hypothesized that, unlike ssRNA, dsDNA would be a poor substrate for assembly. We examined titrations of ssDNA and dsDNA with purified HBV core protein, Cp183, by EMSA, EM, DLS, and etheno-DNA fluorescence. Cp183 bound ssDNA with high affinity to form virus-like capsids. However, Cp183 bound dsDNA poorly, forming a mixture of irregular complexes. Nonetheless, we observed some normal cores in dsDNA assembly reactions, indicating that the energy required to bend DNA could be similar to the protein–protein association energy. 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| source | MEDLINE; Elsevier ScienceDirect Journals Complete; EZB-FREE-00999 freely available EZB journals |
| subjects | Biophysics Capsid assembly DNA - metabolism DNA, Single-Stranded - metabolism DNA, Viral - metabolism DNA-binding Hepadnavirus Hepatitis B Core Antigens - metabolism Hepatitis B virus - genetics Hepatitis B virus - physiology Humans Infectious Disease RNA, Viral - metabolism RNA-binding Self-assembly Spumavirus Virus Assembly |
| title | Differential assembly of Hepatitis B Virus core protein on single- and double-stranded nucleic acid suggest the dsDNA-filled core is spring-loaded |
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