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Quantitative Lipid Droplet Proteome Analysis Identifies Annexin A3 as a Cofactor for HCV Particle Production

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Quantitative Lipid Droplet Proteome Analysis Identifies Annexin A3 as a Cofactor for HCV Particle Production. / Rösch, Kathrin; Kwiatkowski, Marcel; Hofmann, Sarah; Schöbel, Anja; Grüttner, Cordula; Wurlitzer, Marcus; Schlüter, Hartmut; Herker, Eva.

In: CELL REP, Vol. 16, No. 12, 20.09.2016, p. 3219-31.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Rösch, K, Kwiatkowski, M, Hofmann, S, Schöbel, A, Grüttner, C, Wurlitzer, M, Schlüter, H & Herker, E 2016, 'Quantitative Lipid Droplet Proteome Analysis Identifies Annexin A3 as a Cofactor for HCV Particle Production', CELL REP, vol. 16, no. 12, pp. 3219-31. https://doi.org/10.1016/j.celrep.2016.08.052

APA

Rösch, K., Kwiatkowski, M., Hofmann, S., Schöbel, A., Grüttner, C., Wurlitzer, M., Schlüter, H., & Herker, E. (2016). Quantitative Lipid Droplet Proteome Analysis Identifies Annexin A3 as a Cofactor for HCV Particle Production. CELL REP, 16(12), 3219-31. https://doi.org/10.1016/j.celrep.2016.08.052

Vancouver

Rösch K, Kwiatkowski M, Hofmann S, Schöbel A, Grüttner C, Wurlitzer M et al. Quantitative Lipid Droplet Proteome Analysis Identifies Annexin A3 as a Cofactor for HCV Particle Production. CELL REP. 2016 Sep 20;16(12):3219-31. https://doi.org/10.1016/j.celrep.2016.08.052

Bibtex

@article{36ae0d15e63f4841860c6c79202afe32,
title = "Quantitative Lipid Droplet Proteome Analysis Identifies Annexin A3 as a Cofactor for HCV Particle Production",
abstract = "Lipid droplets are vital to hepatitis C virus (HCV) infection as the putative sites of virion assembly, but morphogenesis and egress of virions remain ill defined. We performed quantitative lipid droplet proteome analysis of HCV-infected cells to identify co-factors of that process. Our results demonstrate that HCV disconnects lipid droplets from their metabolic function. Annexin A3 (ANXA3), a protein enriched in lipid droplet fractions, strongly impacted HCV replication and was characterized further: ANXA3 is recruited to lipid-rich fractions in HCV-infected cells by the viral core and NS5A proteins. ANXA3 knockdown does not affect HCV RNA replication but severely impairs virion production with lower specific infectivity and higher density of secreted virions. ANXA3 is essential for the interaction of viral envelope E2 with apolipoprotein E (ApoE) and for trafficking, but not lipidation, of ApoE in HCV-infected cells. Thus, we identified ANXA3 as a regulator of HCV maturation and egress.",
keywords = "Journal Article",
author = "Kathrin R{\"o}sch and Marcel Kwiatkowski and Sarah Hofmann and Anja Sch{\"o}bel and Cordula Gr{\"u}ttner and Marcus Wurlitzer and Hartmut Schl{\"u}ter and Eva Herker",
note = "Copyright {\textcopyright} 2016 The Author(s). Published by Elsevier Inc. All rights reserved.",
year = "2016",
month = sep,
day = "20",
doi = "10.1016/j.celrep.2016.08.052",
language = "English",
volume = "16",
pages = "3219--31",
journal = "CELL REP",
issn = "2211-1247",
publisher = "Elsevier",
number = "12",

}

RIS

TY - JOUR

T1 - Quantitative Lipid Droplet Proteome Analysis Identifies Annexin A3 as a Cofactor for HCV Particle Production

AU - Rösch, Kathrin

AU - Kwiatkowski, Marcel

AU - Hofmann, Sarah

AU - Schöbel, Anja

AU - Grüttner, Cordula

AU - Wurlitzer, Marcus

AU - Schlüter, Hartmut

AU - Herker, Eva

N1 - Copyright © 2016 The Author(s). Published by Elsevier Inc. All rights reserved.

PY - 2016/9/20

Y1 - 2016/9/20

N2 - Lipid droplets are vital to hepatitis C virus (HCV) infection as the putative sites of virion assembly, but morphogenesis and egress of virions remain ill defined. We performed quantitative lipid droplet proteome analysis of HCV-infected cells to identify co-factors of that process. Our results demonstrate that HCV disconnects lipid droplets from their metabolic function. Annexin A3 (ANXA3), a protein enriched in lipid droplet fractions, strongly impacted HCV replication and was characterized further: ANXA3 is recruited to lipid-rich fractions in HCV-infected cells by the viral core and NS5A proteins. ANXA3 knockdown does not affect HCV RNA replication but severely impairs virion production with lower specific infectivity and higher density of secreted virions. ANXA3 is essential for the interaction of viral envelope E2 with apolipoprotein E (ApoE) and for trafficking, but not lipidation, of ApoE in HCV-infected cells. Thus, we identified ANXA3 as a regulator of HCV maturation and egress.

AB - Lipid droplets are vital to hepatitis C virus (HCV) infection as the putative sites of virion assembly, but morphogenesis and egress of virions remain ill defined. We performed quantitative lipid droplet proteome analysis of HCV-infected cells to identify co-factors of that process. Our results demonstrate that HCV disconnects lipid droplets from their metabolic function. Annexin A3 (ANXA3), a protein enriched in lipid droplet fractions, strongly impacted HCV replication and was characterized further: ANXA3 is recruited to lipid-rich fractions in HCV-infected cells by the viral core and NS5A proteins. ANXA3 knockdown does not affect HCV RNA replication but severely impairs virion production with lower specific infectivity and higher density of secreted virions. ANXA3 is essential for the interaction of viral envelope E2 with apolipoprotein E (ApoE) and for trafficking, but not lipidation, of ApoE in HCV-infected cells. Thus, we identified ANXA3 as a regulator of HCV maturation and egress.

KW - Journal Article

U2 - 10.1016/j.celrep.2016.08.052

DO - 10.1016/j.celrep.2016.08.052

M3 - SCORING: Journal article

C2 - 27653686

VL - 16

SP - 3219

EP - 3231

JO - CELL REP

JF - CELL REP

SN - 2211-1247

IS - 12

ER -