A Proteomic approach to discover and compare interacting partners of Papillomavirus E2 proteins from diverse phylogenetic groups
Identifieur interne : 000106 ( Pmc/Corpus ); précédent : 000105; suivant : 000107A Proteomic approach to discover and compare interacting partners of Papillomavirus E2 proteins from diverse phylogenetic groups
Auteurs : Moon Kyoo Jang ; D. Eric Anderson ; Koenraad Van Doorslaer ; Alison A. McbrideSource :
- Proteomics [ 1615-9853 ] ; 2015.
Abstract
Papillomaviruses are a very successful group of viruses that replicate persistently in localized regions of the stratified epithelium of their specific host. Infection results in pathologies ranging from asymptomatic infection, benign warts, to malignant carcinomas. Despite this diversity, papillomavirus genomes are small (7-8 kbp) and contain at most eight genes. To sustain the complex papillomaviral life cycle, each viral protein has multiple functions and interacts with and manipulates a plethora of cellular proteins. In this study, we use tandem affinity purification and mass spectrometry to identify host factors that interact with eleven different papillomavirus E2 proteins from diverse phylogenetic groups. The E2 proteins function in viral transcription and replication and correspondingly interact with host proteins involved in transcription, chromatin remodeling and modification, replication and RNA processing.
Url:
DOI: 10.1002/pmic.201400613
PubMed: 25758368
PubMed Central: 4535189
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Eric Anderson</name><affiliation><nlm:aff id="A2">Advanced Mass Spectrometry Core, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892</nlm:aff></affiliation></author><author><name sortKey="Van Doorslaer, Koenraad" sort="Van Doorslaer, Koenraad" uniqKey="Van Doorslaer K" first="Koenraad" last="Van Doorslaer">Koenraad Van Doorslaer</name><affiliation><nlm:aff id="A1">Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892</nlm:aff></affiliation></author><author><name sortKey="Mcbride, Alison A" sort="Mcbride, Alison A" uniqKey="Mcbride A" first="Alison A." last="Mcbride">Alison A. Mcbride</name><affiliation><nlm:aff id="A1">Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">25758368</idno><idno type="pmc">4535189</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4535189</idno><idno type="RBID">PMC:4535189</idno><idno type="doi">10.1002/pmic.201400613</idno><date when="2015">2015</date><idno type="wicri:Area/Pmc/Corpus">000106</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000106</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">A Proteomic approach to discover and compare interacting partners of Papillomavirus E2 proteins from diverse phylogenetic groups</title><author><name sortKey="Jang, Moon Kyoo" sort="Jang, Moon Kyoo" uniqKey="Jang M" first="Moon Kyoo" last="Jang">Moon Kyoo Jang</name><affiliation><nlm:aff id="A1">Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892</nlm:aff></affiliation></author><author><name sortKey="Anderson, D Eric" sort="Anderson, D Eric" uniqKey="Anderson D" first="D. Eric" last="Anderson">D. Eric Anderson</name><affiliation><nlm:aff id="A2">Advanced Mass Spectrometry Core, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892</nlm:aff></affiliation></author><author><name sortKey="Van Doorslaer, Koenraad" sort="Van Doorslaer, Koenraad" uniqKey="Van Doorslaer K" first="Koenraad" last="Van Doorslaer">Koenraad Van Doorslaer</name><affiliation><nlm:aff id="A1">Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892</nlm:aff></affiliation></author><author><name sortKey="Mcbride, Alison A" sort="Mcbride, Alison A" uniqKey="Mcbride A" first="Alison A." last="Mcbride">Alison A. Mcbride</name><affiliation><nlm:aff id="A1">Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892</nlm:aff></affiliation></author></analytic><series><title level="j">Proteomics</title><idno type="ISSN">1615-9853</idno><idno type="eISSN">1615-9861</idno><imprint><date when="2015">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p id="P1">Papillomaviruses are a very successful group of viruses that replicate persistently in localized regions of the stratified epithelium of their specific host. Infection results in pathologies ranging from asymptomatic infection, benign warts, to malignant carcinomas. Despite this diversity, papillomavirus genomes are small (7-8 kbp) and contain at most eight genes. To sustain the complex papillomaviral life cycle, each viral protein has multiple functions and interacts with and manipulates a plethora of cellular proteins. In this study, we use tandem affinity purification and mass spectrometry to identify host factors that interact with eleven different papillomavirus E2 proteins from diverse phylogenetic groups. The E2 proteins function in viral transcription and replication and correspondingly interact with host proteins involved in transcription, chromatin remodeling and modification, replication and RNA processing.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<pmc-dir>properties manuscript</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-journal-id">101092707</journal-id><journal-id journal-id-type="pubmed-jr-id">22472</journal-id><journal-id journal-id-type="nlm-ta">Proteomics</journal-id><journal-id journal-id-type="iso-abbrev">Proteomics</journal-id><journal-title-group><journal-title>Proteomics</journal-title></journal-title-group><issn pub-type="ppub">1615-9853</issn><issn pub-type="epub">1615-9861</issn></journal-meta><article-meta><article-id pub-id-type="pmid">25758368</article-id><article-id pub-id-type="pmc">4535189</article-id><article-id pub-id-type="doi">10.1002/pmic.201400613</article-id><article-id pub-id-type="manuscript">NIHMS711233</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>A Proteomic approach to discover and compare interacting partners of Papillomavirus E2 proteins from diverse phylogenetic groups</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Jang</surname><given-names>Moon Kyoo</given-names></name><xref ref-type="aff" rid="A1">1</xref></contrib><contrib contrib-type="author"><name><surname>Anderson</surname><given-names>D. Eric</given-names></name><xref ref-type="aff" rid="A2">2</xref></contrib><contrib contrib-type="author"><name><surname>van Doorslaer</surname><given-names>Koenraad</given-names></name><xref ref-type="aff" rid="A1">1</xref></contrib><contrib contrib-type="author"><name><surname>McBride</surname><given-names>Alison A.</given-names></name><xref ref-type="aff" rid="A1">1</xref></contrib></contrib-group><aff id="A1"><label>1</label>Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892</aff><aff id="A2"><label>2</label>Advanced Mass Spectrometry Core, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892</aff><author-notes><corresp id="CR1"><bold>Correspondence: <email>amcbride@nih.gov</email>,</bold> Room 3W20B.4, 33 North Drive, MSC3209, NIH, Bethesda, MD 20892-3209, Tel: 301-496-1370</corresp></author-notes><pub-date pub-type="nihms-submitted"><day>3</day><month>8</month><year>2015</year></pub-date><pub-date pub-type="epub"><day>28</day><month>4</month><year>2015</year></pub-date><pub-date pub-type="ppub"><month>6</month><year>2015</year></pub-date><pub-date pub-type="pmc-release"><day>01</day><month>6</month><year>2016</year></pub-date><volume>15</volume><issue>12</issue><fpage>2038</fpage><lpage>2050</lpage><pmc-comment>elocation-id from pubmed: 10.1002/pmic.201400613</pmc-comment>
<abstract><p id="P1">Papillomaviruses are a very successful group of viruses that replicate persistently in localized regions of the stratified epithelium of their specific host. Infection results in pathologies ranging from asymptomatic infection, benign warts, to malignant carcinomas. Despite this diversity, papillomavirus genomes are small (7-8 kbp) and contain at most eight genes. To sustain the complex papillomaviral life cycle, each viral protein has multiple functions and interacts with and manipulates a plethora of cellular proteins. In this study, we use tandem affinity purification and mass spectrometry to identify host factors that interact with eleven different papillomavirus E2 proteins from diverse phylogenetic groups. The E2 proteins function in viral transcription and replication and correspondingly interact with host proteins involved in transcription, chromatin remodeling and modification, replication and RNA processing.</p></abstract><kwd-group><kwd>E2</kwd><kwd>BRD4</kwd><kwd>HPV</kwd><kwd>papillomavirus</kwd><kwd>virus</kwd></kwd-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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