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Article: Intact sphingomyelin biosynthetic pathway is essential for intracellular transport of influenza virus glycoproteins

TitleIntact sphingomyelin biosynthetic pathway is essential for intracellular transport of influenza virus glycoproteins
Authors
Issue Date2013
PublisherNational Academy of Sciences. The Journal's web site is located at http://www.pnas.org
Citation
Proceedings Of The National Academy Of Sciences Of The United States Of America, 2013, v. 110 n. 16, p. 6406-6411 How to Cite?
AbstractCells genetically deficient in sphingomyelin synthase-1 (SGMS1) or blocked in their synthesis pharmacologically through exposure to a serine palmitoyltransferase inhibitor (myriocin) show strongly reduced surface display of influenza virus glycoproteins hemag-glutinin (HA) and neuraminidase (NA). The transport of HA to the cell surface was assessed by accessibility of HA on intact cells to exogenously added trypsin and to HA-specific antibodies. Rates of de novo synthesis of viral proteins in wild-type and SGMS1-deficient cells were equivalent, and HA negotiated the intracellular trafficking pathway through the Golgi normally. We engineered a strain of influenza virus to allow site-specific labeling of HA and NA using sortase. Accessibility of both HA and NA to sortase was blocked in SGMS1-deficient cells and in cells exposed to myriocin, with a corresponding inhibition of the release of virus particles from infected cells. Generation of influenza virus particles thus critically relies on a functional sphingomyelin biosynthetic pathway, required to drive influenza viral glycoproteins into lipid domains of a composition compatible with virus budding and release.
Persistent Identifierhttp://hdl.handle.net/10722/188686
ISSN
2015 Impact Factor: 9.423
2015 SCImago Journal Rankings: 6.883
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorTafesse, FGen_US
dc.contributor.authorSanyal, Sen_US
dc.contributor.authorAshour, Jen_US
dc.contributor.authorGuimaraes, CPen_US
dc.contributor.authorHermansson, Men_US
dc.contributor.authorSomerharju, Pen_US
dc.contributor.authorPloegh, HLen_US
dc.date.accessioned2013-09-03T04:12:46Z-
dc.date.available2013-09-03T04:12:46Z-
dc.date.issued2013en_US
dc.identifier.citationProceedings Of The National Academy Of Sciences Of The United States Of America, 2013, v. 110 n. 16, p. 6406-6411en_US
dc.identifier.issn0027-8424en_US
dc.identifier.urihttp://hdl.handle.net/10722/188686-
dc.description.abstractCells genetically deficient in sphingomyelin synthase-1 (SGMS1) or blocked in their synthesis pharmacologically through exposure to a serine palmitoyltransferase inhibitor (myriocin) show strongly reduced surface display of influenza virus glycoproteins hemag-glutinin (HA) and neuraminidase (NA). The transport of HA to the cell surface was assessed by accessibility of HA on intact cells to exogenously added trypsin and to HA-specific antibodies. Rates of de novo synthesis of viral proteins in wild-type and SGMS1-deficient cells were equivalent, and HA negotiated the intracellular trafficking pathway through the Golgi normally. We engineered a strain of influenza virus to allow site-specific labeling of HA and NA using sortase. Accessibility of both HA and NA to sortase was blocked in SGMS1-deficient cells and in cells exposed to myriocin, with a corresponding inhibition of the release of virus particles from infected cells. Generation of influenza virus particles thus critically relies on a functional sphingomyelin biosynthetic pathway, required to drive influenza viral glycoproteins into lipid domains of a composition compatible with virus budding and release.en_US
dc.languageengen_US
dc.publisherNational Academy of Sciences. The Journal's web site is located at http://www.pnas.orgen_US
dc.relation.ispartofProceedings of the National Academy of Sciences of the United States of Americaen_US
dc.subject.meshAnimalsen_US
dc.subject.meshBiological Transport - Physiologyen_US
dc.subject.meshBiosynthetic Pathways - Physiologyen_US
dc.subject.meshDogsen_US
dc.subject.meshFatty Acids, Monounsaturated - Pharmacologyen_US
dc.subject.meshFluorescent Antibody Techniqueen_US
dc.subject.meshHemagglutinin Glycoproteins, Influenza Virus - Metabolism - Physiologyen_US
dc.subject.meshHost-Pathogen Interactionsen_US
dc.subject.meshMadin Darby Canine Kidney Cellsen_US
dc.subject.meshPolyethylene Glycolsen_US
dc.subject.meshSerine C-Palmitoyltransferase - Antagonists & Inhibitorsen_US
dc.subject.meshSphingomyelins - Biosynthesisen_US
dc.subject.meshTransferases (Other Substituted Phosphate Groups) - Deficiencyen_US
dc.subject.meshTrypsinen_US
dc.titleIntact sphingomyelin biosynthetic pathway is essential for intracellular transport of influenza virus glycoproteinsen_US
dc.typeArticleen_US
dc.identifier.emailSanyal, S: sumana@wi.mit.eduen_US
dc.identifier.authoritySanyal, S=rp01794en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1073/pnas.1219909110en_US
dc.identifier.pmid23576732-
dc.identifier.scopuseid_2-s2.0-84876276496en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-84876276496&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume110en_US
dc.identifier.issue16en_US
dc.identifier.spage6406en_US
dc.identifier.epage6411en_US
dc.identifier.isiWOS:000318041500043-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridTafesse, FG=14832089000en_US
dc.identifier.scopusauthoridSanyal, S=16069600000en_US
dc.identifier.scopusauthoridAshour, J=8586250900en_US
dc.identifier.scopusauthoridGuimaraes, CP=30967477400en_US
dc.identifier.scopusauthoridHermansson, M=9241690600en_US
dc.identifier.scopusauthoridSomerharju, P=7005452736en_US
dc.identifier.scopusauthoridPloegh, HL=35433834100en_US

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