Sterile α Motif Domain Containing 9 Is a Novel Cellular Interacting Partner to Low-Risk Type Human Papillomavirus E6 Proteins
Low-risk type human papillomavirus (HPV) 6 and 11 infection causes recurrent respiratory papillomatosis (RRP) and genital warts. RRP is the most common benign tumor of the larynx in children with frequent relapses. Repeated surgeries are often needed to improve vocal function and prevent life-threat...
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| creator | Wang, Jia Dupuis, Crystal Tyring, Stephen K Underbrink, Michael P |
| description | Low-risk type human papillomavirus (HPV) 6 and 11 infection causes recurrent respiratory papillomatosis (RRP) and genital warts. RRP is the most common benign tumor of the larynx in children with frequent relapses. Repeated surgeries are often needed to improve vocal function and prevent life-threatening respiratory obstruction. Currently, there are no effective treatments available to completely eliminate these diseases, largely due to limited knowledge regarding their viral molecular pathogenesis. HPV E6 proteins contribute to cell immortalization by interacting with a variety of cellular proteins, which have been well studied for the high-risk type HPVs related to cancer progression. However, the functions of low-risk HPV E6 proteins are largely unknown. In this study, we report GST-pulldown coupled mass spectrometry analysis with low-risk HPV E6 proteins that identified sterile alpha motif domain containing 9 (SAMD9) as a novel interacting partner. We then confirmed the interaction between HPV-E6 and SAMD9 using co-immunoprecipitation, proximity ligation assay, and confocal immunofluorescence staining. The SAMD9 gene is down-regulated in a variety of neoplasms and deleteriously mutated in normophosphatemic familial tumoral calcinosis. Interestingly, SAMD9 also has antiviral functions against poxvirus. Our study adds to the limited knowledge of the molecular properties of low-risk HPVs and describes new potential functions for the low-risk HPV E6 protein. |
| doi_str_mv | 10.1371/journal.pone.0149859 |
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RRP is the most common benign tumor of the larynx in children with frequent relapses. Repeated surgeries are often needed to improve vocal function and prevent life-threatening respiratory obstruction. Currently, there are no effective treatments available to completely eliminate these diseases, largely due to limited knowledge regarding their viral molecular pathogenesis. HPV E6 proteins contribute to cell immortalization by interacting with a variety of cellular proteins, which have been well studied for the high-risk type HPVs related to cancer progression. However, the functions of low-risk HPV E6 proteins are largely unknown. In this study, we report GST-pulldown coupled mass spectrometry analysis with low-risk HPV E6 proteins that identified sterile alpha motif domain containing 9 (SAMD9) as a novel interacting partner. We then confirmed the interaction between HPV-E6 and SAMD9 using co-immunoprecipitation, proximity ligation assay, and confocal immunofluorescence staining. The SAMD9 gene is down-regulated in a variety of neoplasms and deleteriously mutated in normophosphatemic familial tumoral calcinosis. Interestingly, SAMD9 also has antiviral functions against poxvirus. Our study adds to the limited knowledge of the molecular properties of low-risk HPVs and describes new potential functions for the low-risk HPV E6 protein.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0149859</identifier><identifier>PMID: 26901061</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Biology and life sciences ; Calcinosis ; Cancer ; Cell immortalization ; Children ; Condyloma acuminatum ; Dermatology ; DNA-Binding Proteins - chemistry ; DNA-Binding Proteins - metabolism ; E6 protein ; Health risks ; HEK293 Cells ; Human papillomavirus ; Human papillomavirus 6 - metabolism ; Humans ; Immortalization ; Immunofluorescence ; Immunology ; Immunoprecipitation ; Infections ; Larynx ; Mass spectrometry ; Mass spectroscopy ; Medical research ; Medical treatment ; Medicine and Health Sciences ; Neoplasms ; Oncogene Proteins, Viral - chemistry ; Oncogene Proteins, Viral - metabolism ; Otolaryngology ; Papilloma ; Pathogenesis ; Penicillin ; Plasmids ; Protein Structure, Secondary ; Proteins ; Recurrent infection ; Repressor Proteins - chemistry ; Repressor Proteins - metabolism ; Risk analysis ; Tumors ; Virology ; Warts</subject><ispartof>PloS one, 2016-02, Vol.11 (2), p.e0149859-e0149859</ispartof><rights>2016 Wang et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2016 Wang et al 2016 Wang et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4419-7f540b9b57149365417ad0b5b81f99cd8e84af7ef2aaeadc6ac7f6b20d9fef853</citedby><cites>FETCH-LOGICAL-c4419-7f540b9b57149365417ad0b5b81f99cd8e84af7ef2aaeadc6ac7f6b20d9fef853</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4764768/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4764768/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,2096,2915,23845,27901,27902,53766,53768,79342,79343</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26901061$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, Jia</creatorcontrib><creatorcontrib>Dupuis, Crystal</creatorcontrib><creatorcontrib>Tyring, Stephen K</creatorcontrib><creatorcontrib>Underbrink, Michael P</creatorcontrib><title>Sterile α Motif Domain Containing 9 Is a Novel Cellular Interacting Partner to Low-Risk Type Human Papillomavirus E6 Proteins</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Low-risk type human papillomavirus (HPV) 6 and 11 infection causes recurrent respiratory papillomatosis (RRP) and genital warts. RRP is the most common benign tumor of the larynx in children with frequent relapses. Repeated surgeries are often needed to improve vocal function and prevent life-threatening respiratory obstruction. Currently, there are no effective treatments available to completely eliminate these diseases, largely due to limited knowledge regarding their viral molecular pathogenesis. HPV E6 proteins contribute to cell immortalization by interacting with a variety of cellular proteins, which have been well studied for the high-risk type HPVs related to cancer progression. However, the functions of low-risk HPV E6 proteins are largely unknown. In this study, we report GST-pulldown coupled mass spectrometry analysis with low-risk HPV E6 proteins that identified sterile alpha motif domain containing 9 (SAMD9) as a novel interacting partner. We then confirmed the interaction between HPV-E6 and SAMD9 using co-immunoprecipitation, proximity ligation assay, and confocal immunofluorescence staining. The SAMD9 gene is down-regulated in a variety of neoplasms and deleteriously mutated in normophosphatemic familial tumoral calcinosis. Interestingly, SAMD9 also has antiviral functions against poxvirus. Our study adds to the limited knowledge of the molecular properties of low-risk HPVs and describes new potential functions for the low-risk HPV E6 protein.</description><subject>Biology and life sciences</subject><subject>Calcinosis</subject><subject>Cancer</subject><subject>Cell immortalization</subject><subject>Children</subject><subject>Condyloma acuminatum</subject><subject>Dermatology</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>E6 protein</subject><subject>Health risks</subject><subject>HEK293 Cells</subject><subject>Human papillomavirus</subject><subject>Human papillomavirus 6 - metabolism</subject><subject>Humans</subject><subject>Immortalization</subject><subject>Immunofluorescence</subject><subject>Immunology</subject><subject>Immunoprecipitation</subject><subject>Infections</subject><subject>Larynx</subject><subject>Mass spectrometry</subject><subject>Mass spectroscopy</subject><subject>Medical research</subject><subject>Medical treatment</subject><subject>Medicine and Health Sciences</subject><subject>Neoplasms</subject><subject>Oncogene Proteins, Viral - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, Jia</au><au>Dupuis, Crystal</au><au>Tyring, Stephen K</au><au>Underbrink, Michael P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Sterile α Motif Domain Containing 9 Is a Novel Cellular Interacting Partner to Low-Risk Type Human Papillomavirus E6 Proteins</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2016-02-01</date><risdate>2016</risdate><volume>11</volume><issue>2</issue><spage>e0149859</spage><epage>e0149859</epage><pages>e0149859-e0149859</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Low-risk type human papillomavirus (HPV) 6 and 11 infection causes recurrent respiratory papillomatosis (RRP) and genital warts. RRP is the most common benign tumor of the larynx in children with frequent relapses. Repeated surgeries are often needed to improve vocal function and prevent life-threatening respiratory obstruction. Currently, there are no effective treatments available to completely eliminate these diseases, largely due to limited knowledge regarding their viral molecular pathogenesis. HPV E6 proteins contribute to cell immortalization by interacting with a variety of cellular proteins, which have been well studied for the high-risk type HPVs related to cancer progression. However, the functions of low-risk HPV E6 proteins are largely unknown. In this study, we report GST-pulldown coupled mass spectrometry analysis with low-risk HPV E6 proteins that identified sterile alpha motif domain containing 9 (SAMD9) as a novel interacting partner. We then confirmed the interaction between HPV-E6 and SAMD9 using co-immunoprecipitation, proximity ligation assay, and confocal immunofluorescence staining. The SAMD9 gene is down-regulated in a variety of neoplasms and deleteriously mutated in normophosphatemic familial tumoral calcinosis. Interestingly, SAMD9 also has antiviral functions against poxvirus. Our study adds to the limited knowledge of the molecular properties of low-risk HPVs and describes new potential functions for the low-risk HPV E6 protein.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>26901061</pmid><doi>10.1371/journal.pone.0149859</doi><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; DOAJ Directory of Open Access Journals; EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry; Public Library of Science (PLoS) |
| subjects | Biology and life sciences Calcinosis Cancer Cell immortalization Children Condyloma acuminatum Dermatology DNA-Binding Proteins - chemistry DNA-Binding Proteins - metabolism E6 protein Health risks HEK293 Cells Human papillomavirus Human papillomavirus 6 - metabolism Humans Immortalization Immunofluorescence Immunology Immunoprecipitation Infections Larynx Mass spectrometry Mass spectroscopy Medical research Medical treatment Medicine and Health Sciences Neoplasms Oncogene Proteins, Viral - chemistry Oncogene Proteins, Viral - metabolism Otolaryngology Papilloma Pathogenesis Penicillin Plasmids Protein Structure, Secondary Proteins Recurrent infection Repressor Proteins - chemistry Repressor Proteins - metabolism Risk analysis Tumors Virology Warts |
| title | Sterile α Motif Domain Containing 9 Is a Novel Cellular Interacting Partner to Low-Risk Type Human Papillomavirus E6 Proteins |
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