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Proximity labeling of host factor ANXA3 in HCV infection reveals a novel LARP1 function in viral entry

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Proximity labeling of host factor ANXA3 in HCV infection reveals a novel LARP1 function in viral entry. / Bley, Hanna; Krisp, Christoph; Schöbel, Anja; Hehner, Julia; Schneider, Laura; Becker, Miriam; Stegmann, Cora; Heidenfels, Elisa; Nguyen-Dinh, Van; Schlüter, Hartmut; Gerold, Gisa; Herker, Eva.

In: J BIOL CHEM, Vol. 300, No. 5, 05.2024, p. 107286.

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

Harvard

Bley, H, Krisp, C, Schöbel, A, Hehner, J, Schneider, L, Becker, M, Stegmann, C, Heidenfels, E, Nguyen-Dinh, V, Schlüter, H, Gerold, G & Herker, E 2024, 'Proximity labeling of host factor ANXA3 in HCV infection reveals a novel LARP1 function in viral entry', J BIOL CHEM, vol. 300, no. 5, pp. 107286. https://doi.org/10.1016/j.jbc.2024.107286

APA

Bley, H., Krisp, C., Schöbel, A., Hehner, J., Schneider, L., Becker, M., Stegmann, C., Heidenfels, E., Nguyen-Dinh, V., Schlüter, H., Gerold, G., & Herker, E. (2024). Proximity labeling of host factor ANXA3 in HCV infection reveals a novel LARP1 function in viral entry. J BIOL CHEM, 300(5), 107286. https://doi.org/10.1016/j.jbc.2024.107286

Vancouver

Bley H, Krisp C, Schöbel A, Hehner J, Schneider L, Becker M et al. Proximity labeling of host factor ANXA3 in HCV infection reveals a novel LARP1 function in viral entry. J BIOL CHEM. 2024 May;300(5):107286. https://doi.org/10.1016/j.jbc.2024.107286

Bibtex

@article{19e2a8d82607420187a88910770da694,
title = "Proximity labeling of host factor ANXA3 in HCV infection reveals a novel LARP1 function in viral entry",
abstract = "Hepatitis C virus (HCV) infection is tightly connected to the lipid metabolism with lipid droplets (LDs) serving as assembly sites for progeny virions. A previous LD proteome analysis identified annexin A3 (ANXA3) as an important HCV host factor that is enriched at LDs in infected cells and required for HCV morphogenesis. To further characterize ANXA3 function in HCV, we performed proximity labeling using ANXA3-BioID2 as bait in HCV-infected cells. Two of the top proteins identified proximal to ANXA3 during HCV infection were the La-related protein 1 (LARP1) and the ADP ribosylation factor-like protein 8B (ARL8B), both of which have been previously described to act in HCV particle production. In follow-up experiments, ARL8B functioned as a pro-viral HCV host factor without localizing to LDs and thus likely independent of ANXA3. In contrast, LARP1 interacts with HCV core protein in an RNA-dependent manner and is translocated to LDs by core protein. Knockdown of LARP1 decreased HCV spreading without altering HCV RNA replication or viral titers. Unexpectedly, entry of HCV particles and E1/E2-pseudotyped lentiviral particles was reduced by LARP1 depletion, whereas particle production was not altered. Using a recombinant vesicular stomatitis virus (VSV)ΔG entry assay, we showed that LARP1 depletion also decreased entry of VSV with VSV, MERS, and CHIKV glycoproteins. Therefore, our data expand the role of LARP1 as an HCV host factor that is most prominently involved in the early steps of infection, likely contributing to endocytosis of viral particles through the pleiotropic effect LARP1 has on the cellular translatome.",
keywords = "Humans, Annexin A3/metabolism, Autoantigens/metabolism, HEK293 Cells, Hepacivirus/metabolism, Hepatitis C/metabolism, Host-Pathogen Interactions, Lipid Droplets/metabolism, Ribonucleoproteins/metabolism, SS-B Antigen, Viral Core Proteins/metabolism, Viral Envelope Proteins/metabolism, Virus Internalization",
author = "Hanna Bley and Christoph Krisp and Anja Sch{\"o}bel and Julia Hehner and Laura Schneider and Miriam Becker and Cora Stegmann and Elisa Heidenfels and Van Nguyen-Dinh and Hartmut Schl{\"u}ter and Gisa Gerold and Eva Herker",
note = "Copyright {\textcopyright} 2024 The Authors. Published by Elsevier Inc. All rights reserved.",
year = "2024",
month = may,
doi = "10.1016/j.jbc.2024.107286",
language = "English",
volume = "300",
pages = "107286",
journal = "J BIOL CHEM",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "5",

}

RIS

TY - JOUR

T1 - Proximity labeling of host factor ANXA3 in HCV infection reveals a novel LARP1 function in viral entry

AU - Bley, Hanna

AU - Krisp, Christoph

AU - Schöbel, Anja

AU - Hehner, Julia

AU - Schneider, Laura

AU - Becker, Miriam

AU - Stegmann, Cora

AU - Heidenfels, Elisa

AU - Nguyen-Dinh, Van

AU - Schlüter, Hartmut

AU - Gerold, Gisa

AU - Herker, Eva

N1 - Copyright © 2024 The Authors. Published by Elsevier Inc. All rights reserved.

PY - 2024/5

Y1 - 2024/5

N2 - Hepatitis C virus (HCV) infection is tightly connected to the lipid metabolism with lipid droplets (LDs) serving as assembly sites for progeny virions. A previous LD proteome analysis identified annexin A3 (ANXA3) as an important HCV host factor that is enriched at LDs in infected cells and required for HCV morphogenesis. To further characterize ANXA3 function in HCV, we performed proximity labeling using ANXA3-BioID2 as bait in HCV-infected cells. Two of the top proteins identified proximal to ANXA3 during HCV infection were the La-related protein 1 (LARP1) and the ADP ribosylation factor-like protein 8B (ARL8B), both of which have been previously described to act in HCV particle production. In follow-up experiments, ARL8B functioned as a pro-viral HCV host factor without localizing to LDs and thus likely independent of ANXA3. In contrast, LARP1 interacts with HCV core protein in an RNA-dependent manner and is translocated to LDs by core protein. Knockdown of LARP1 decreased HCV spreading without altering HCV RNA replication or viral titers. Unexpectedly, entry of HCV particles and E1/E2-pseudotyped lentiviral particles was reduced by LARP1 depletion, whereas particle production was not altered. Using a recombinant vesicular stomatitis virus (VSV)ΔG entry assay, we showed that LARP1 depletion also decreased entry of VSV with VSV, MERS, and CHIKV glycoproteins. Therefore, our data expand the role of LARP1 as an HCV host factor that is most prominently involved in the early steps of infection, likely contributing to endocytosis of viral particles through the pleiotropic effect LARP1 has on the cellular translatome.

AB - Hepatitis C virus (HCV) infection is tightly connected to the lipid metabolism with lipid droplets (LDs) serving as assembly sites for progeny virions. A previous LD proteome analysis identified annexin A3 (ANXA3) as an important HCV host factor that is enriched at LDs in infected cells and required for HCV morphogenesis. To further characterize ANXA3 function in HCV, we performed proximity labeling using ANXA3-BioID2 as bait in HCV-infected cells. Two of the top proteins identified proximal to ANXA3 during HCV infection were the La-related protein 1 (LARP1) and the ADP ribosylation factor-like protein 8B (ARL8B), both of which have been previously described to act in HCV particle production. In follow-up experiments, ARL8B functioned as a pro-viral HCV host factor without localizing to LDs and thus likely independent of ANXA3. In contrast, LARP1 interacts with HCV core protein in an RNA-dependent manner and is translocated to LDs by core protein. Knockdown of LARP1 decreased HCV spreading without altering HCV RNA replication or viral titers. Unexpectedly, entry of HCV particles and E1/E2-pseudotyped lentiviral particles was reduced by LARP1 depletion, whereas particle production was not altered. Using a recombinant vesicular stomatitis virus (VSV)ΔG entry assay, we showed that LARP1 depletion also decreased entry of VSV with VSV, MERS, and CHIKV glycoproteins. Therefore, our data expand the role of LARP1 as an HCV host factor that is most prominently involved in the early steps of infection, likely contributing to endocytosis of viral particles through the pleiotropic effect LARP1 has on the cellular translatome.

KW - Humans

KW - Annexin A3/metabolism

KW - Autoantigens/metabolism

KW - HEK293 Cells

KW - Hepacivirus/metabolism

KW - Hepatitis C/metabolism

KW - Host-Pathogen Interactions

KW - Lipid Droplets/metabolism

KW - Ribonucleoproteins/metabolism

KW - SS-B Antigen

KW - Viral Core Proteins/metabolism

KW - Viral Envelope Proteins/metabolism

KW - Virus Internalization

U2 - 10.1016/j.jbc.2024.107286

DO - 10.1016/j.jbc.2024.107286

M3 - SCORING: Journal article

C2 - 38636657

VL - 300

SP - 107286

JO - J BIOL CHEM

JF - J BIOL CHEM

SN - 0021-9258

IS - 5

ER -