Identification of structural protein–protein interactions of herpes simplex virus type 1
Abstract In this study we have defined protein–protein interactions between the structural proteins of herpes simplex virus type 1 (HSV-1) using a LexA yeast two-hybrid system. The majority of the capsid, tegument and envelope proteins of HSV-1 were screened in a matrix approach. A total of 40 binar...
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| Veröffentlicht in: | Virology (New York, N.Y.) N.Y.), 2008-09, Vol.378 (2), p.347-354 |
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| creator | Lee, Jin H Vittone, Valerio Diefenbach, Eve Cunningham, Anthony L Diefenbach, Russell J |
| description | Abstract In this study we have defined protein–protein interactions between the structural proteins of herpes simplex virus type 1 (HSV-1) using a LexA yeast two-hybrid system. The majority of the capsid, tegument and envelope proteins of HSV-1 were screened in a matrix approach. A total of 40 binary interactions were detected including 9 out of 10 previously identified tegument–tegument interactions (Vittone, V., Diefenbach, E., Triffett, D., Douglas, M.W., Cunningham, A.L., and Diefenbach, R.J., 2005. Determination of interactions between tegument proteins of herpes simplex virus type 1. J. Virol. 79, 9566–9571). A total of 12 interactions involving the capsid protein pUL35 (VP26) and 11 interactions involving the tegument protein pUL46 (VP11/12) were identified. The most significant novel interactions detected in this study, which are likely to play a role in viral assembly, include pUL35–pUL37 (capsid–tegument), pUL46–pUL37 (tegument–tegument) and pUL49 (VP22)–pUS9 (tegument–envelope). This information will provide further insights into the pathways of HSV-1 assembly and the identified interactions are potential targets for new antiviral drugs. |
| doi_str_mv | 10.1016/j.virol.2008.05.035 |
| format | Article |
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The majority of the capsid, tegument and envelope proteins of HSV-1 were screened in a matrix approach. A total of 40 binary interactions were detected including 9 out of 10 previously identified tegument–tegument interactions (Vittone, V., Diefenbach, E., Triffett, D., Douglas, M.W., Cunningham, A.L., and Diefenbach, R.J., 2005. Determination of interactions between tegument proteins of herpes simplex virus type 1. J. Virol. 79, 9566–9571). A total of 12 interactions involving the capsid protein pUL35 (VP26) and 11 interactions involving the tegument protein pUL46 (VP11/12) were identified. The most significant novel interactions detected in this study, which are likely to play a role in viral assembly, include pUL35–pUL37 (capsid–tegument), pUL46–pUL37 (tegument–tegument) and pUL49 (VP22)–pUS9 (tegument–envelope). This information will provide further insights into the pathways of HSV-1 assembly and the identified interactions are potential targets for new antiviral drugs.</description><identifier>ISSN: 0042-6822</identifier><identifier>EISSN: 1096-0341</identifier><identifier>DOI: 10.1016/j.virol.2008.05.035</identifier><identifier>PMID: 18602131</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Electrophoresis, Polyacrylamide Gel ; Herpes simplex virus ; Herpes simplex virus 1 ; Herpesvirus 1, Human - physiology ; Infectious Disease ; Protein Binding ; Protein Interaction Mapping ; Protein–protein interactions ; Two-Hybrid System Techniques ; Viral Structural Proteins - metabolism ; Virus assembly ; Yeast two-hybrid assay</subject><ispartof>Virology (New York, N.Y.), 2008-09, Vol.378 (2), p.347-354</ispartof><rights>Elsevier Inc.</rights><rights>2008 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c554t-9694c2863fdd287bba970f74033344c8c547781440aee5515c876d5a500419c43</citedby><cites>FETCH-LOGICAL-c554t-9694c2863fdd287bba970f74033344c8c547781440aee5515c876d5a500419c43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0042682208003905$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18602131$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lee, Jin H</creatorcontrib><creatorcontrib>Vittone, Valerio</creatorcontrib><creatorcontrib>Diefenbach, Eve</creatorcontrib><creatorcontrib>Cunningham, Anthony L</creatorcontrib><creatorcontrib>Diefenbach, Russell J</creatorcontrib><title>Identification of structural protein–protein interactions of herpes simplex virus type 1</title><title>Virology (New York, N.Y.)</title><addtitle>Virology</addtitle><description>Abstract In this study we have defined protein–protein interactions between the structural proteins of herpes simplex virus type 1 (HSV-1) using a LexA yeast two-hybrid system. The majority of the capsid, tegument and envelope proteins of HSV-1 were screened in a matrix approach. A total of 40 binary interactions were detected including 9 out of 10 previously identified tegument–tegument interactions (Vittone, V., Diefenbach, E., Triffett, D., Douglas, M.W., Cunningham, A.L., and Diefenbach, R.J., 2005. Determination of interactions between tegument proteins of herpes simplex virus type 1. J. Virol. 79, 9566–9571). A total of 12 interactions involving the capsid protein pUL35 (VP26) and 11 interactions involving the tegument protein pUL46 (VP11/12) were identified. The most significant novel interactions detected in this study, which are likely to play a role in viral assembly, include pUL35–pUL37 (capsid–tegument), pUL46–pUL37 (tegument–tegument) and pUL49 (VP22)–pUS9 (tegument–envelope). This information will provide further insights into the pathways of HSV-1 assembly and the identified interactions are potential targets for new antiviral drugs.</description><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Herpes simplex virus</subject><subject>Herpes simplex virus 1</subject><subject>Herpesvirus 1, Human - physiology</subject><subject>Infectious Disease</subject><subject>Protein Binding</subject><subject>Protein Interaction Mapping</subject><subject>Protein–protein interactions</subject><subject>Two-Hybrid System Techniques</subject><subject>Viral Structural Proteins - metabolism</subject><subject>Virus assembly</subject><subject>Yeast two-hybrid assay</subject><issn>0042-6822</issn><issn>1096-0341</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc9O3DAQh60KVBbaJ0CqcuKWMP6XOIcioRWlSEg9tFy4WF5nIrzNJqntIPbGO_QNeZI63ZWQuHCyLX0z_s03hJxSKCjQ8nxdPDo_dAUDUAXIArj8QBYU6jIHLugBWQAIlpeKsSNyHMIa0ruq4CM5oqoERjldkPubBvvoWmdNdEOfDW0Wop9snLzpstEPEV3_8vx3f8tcH9EbO7Nhhh_Qjxiy4DZjh09ZSjSFLG5HzOgnctiaLuDn_XlC7r5d_Vp-z29_XN8sL29zK6WIeV3WwjJV8rZpmKpWK1NX0FYCOOdCWGVlCq2oEGAQpaTSqqpspJFpGlpbwU_I2a5vyvhnwhD1xgWLXWd6HKagU38BrKbvggxqEKVQCeQ70PohBI-tHr3bGL_VFPTsXq_1f_d6dq9B6uQ-VX3Zt59WG2xea_ayE_B1B2Cy8ejQ62Ad9hYb59FG3QzunQ8u3tTbzvVpc91v3GJYD5Pvk2hNdWAa9M95_fP2QQHwGiT_BycnrCQ</recordid><startdate>20080901</startdate><enddate>20080901</enddate><creator>Lee, Jin H</creator><creator>Vittone, Valerio</creator><creator>Diefenbach, Eve</creator><creator>Cunningham, Anthony L</creator><creator>Diefenbach, Russell J</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>7U9</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>20080901</creationdate><title>Identification of structural protein–protein interactions of herpes simplex virus type 1</title><author>Lee, Jin H ; Vittone, Valerio ; Diefenbach, Eve ; Cunningham, Anthony L ; Diefenbach, Russell J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c554t-9694c2863fdd287bba970f74033344c8c547781440aee5515c876d5a500419c43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Herpes simplex virus</topic><topic>Herpes simplex virus 1</topic><topic>Herpesvirus 1, Human - physiology</topic><topic>Infectious Disease</topic><topic>Protein Binding</topic><topic>Protein Interaction Mapping</topic><topic>Protein–protein interactions</topic><topic>Two-Hybrid System Techniques</topic><topic>Viral Structural Proteins - metabolism</topic><topic>Virus assembly</topic><topic>Yeast two-hybrid assay</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lee, Jin H</creatorcontrib><creatorcontrib>Vittone, Valerio</creatorcontrib><creatorcontrib>Diefenbach, Eve</creatorcontrib><creatorcontrib>Cunningham, Anthony L</creatorcontrib><creatorcontrib>Diefenbach, Russell J</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>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Virology (New York, N.Y.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lee, Jin H</au><au>Vittone, Valerio</au><au>Diefenbach, Eve</au><au>Cunningham, Anthony L</au><au>Diefenbach, Russell J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of structural protein–protein interactions of herpes simplex virus type 1</atitle><jtitle>Virology (New York, N.Y.)</jtitle><addtitle>Virology</addtitle><date>2008-09-01</date><risdate>2008</risdate><volume>378</volume><issue>2</issue><spage>347</spage><epage>354</epage><pages>347-354</pages><issn>0042-6822</issn><eissn>1096-0341</eissn><abstract>Abstract In this study we have defined protein–protein interactions between the structural proteins of herpes simplex virus type 1 (HSV-1) using a LexA yeast two-hybrid system. 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| source | MEDLINE; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Electrophoresis, Polyacrylamide Gel Herpes simplex virus Herpes simplex virus 1 Herpesvirus 1, Human - physiology Infectious Disease Protein Binding Protein Interaction Mapping Protein–protein interactions Two-Hybrid System Techniques Viral Structural Proteins - metabolism Virus assembly Yeast two-hybrid assay |
| title | Identification of structural protein–protein interactions of herpes simplex virus type 1 |
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