ER intrabody-mediated inhibition of interferon α secretion by mouse macrophages and dendritic cells.


Journal

PloS one
ISSN: 1932-6203
Titre abrégé: PLoS One
Pays: United States
ID NLM: 101285081

Informations de publication

Date de publication:
2019
Historique:
received: 02 10 2018
accepted: 26 03 2019
entrez: 17 4 2019
pubmed: 17 4 2019
medline: 28 12 2019
Statut: epublish

Résumé

Interferon α (IFNα) counteracts viral infections by activating various IFNα-stimulated genes (ISGs). These genes encode proteins that block viral transport into the host cell and inhibit viral replication, gene transcription and translation. Due to the existence of 14 different, highly homologous isoforms of mouse IFNα, an IFNα knockout mouse has not yet been established by genetic knockout strategies. An scFv intrabody for holding back IFNα isoforms in the endoplasmic reticulum (ER) and thus counteracting IFNα secretion is reported. The intrabody was constructed from the variable domains of the anti-mouse IFNα rat monoclonal antibody 4EA1 recognizing the 5 isoforms IFNα1, IFNα2, IFNα4, IFNα5, IFNα6. A soluble form of the intrabody had a KD of 39 nM to IFNα4. It could be demonstrated that the anti-IFNα intrabody inhibits clearly recombinant IFNα4 secretion by HEK293T cells. In addition, the secretion of IFNα4 was effectively inhibited in stably transfected intrabody expressing RAW 264.7 macrophages and dendritic D1 cells. Colocalization of the intrabody with IFNα4 and the ER marker calnexin in HEK293T cells indicated complex formation of intrabody and IFNα4 inside the ER. Intracellular binding of intrabody and antigen was confirmed by co-immunoprecipitation. Complexes of endogenous IFNα and intrabody could be visualized in the ER of Poly (I:C) stimulated RAW 264.7 macrophages and D1 dendritic cells. Infection of macrophages and dendritic cells with the vesicular stomatitis virus VSV-AV2 is attenuated by IFNα and IFNβ. The intrabody increased virus proliferation in RAW 264.7 macrophages and D1 dendritic cells under IFNβ-neutralizing conditions. To analyze if all IFNα isoforms are recognized by the intrabody was not in the focus of this study. Provided that binding of the intrabody to all isoforms was confirmed, the establishment of transgenic intrabody mice would be promising for studying the function of IFNα during viral infection and autoimmune diseases.

Identifiants

pubmed: 30990863
doi: 10.1371/journal.pone.0215062
pii: PONE-D-18-28638
pmc: PMC6467385
doi:

Substances chimiques

Interferon-alpha 0
Single-Chain Antibodies 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

e0215062

Déclaration de conflit d'intérêts

The authors have declared that no competing interests exist.

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Auteurs

Konrad Büssow (K)

Department Structure and Function of Proteins, Helmholtz Centre for Infection Research, Braunschweig, Germany.

Philipp Themann (P)

Department Structure and Function of Proteins, Helmholtz Centre for Infection Research, Braunschweig, Germany.

Sabine Luu (S)

Department Structure and Function of Proteins, Group Recombinant Protein Expression Helmholtz Centre for Infection Research, Braunschweig, Germany.

Paul Pentrowski (P)

Department Structure and Function of Proteins, Group Recombinant Protein Expression Helmholtz Centre for Infection Research, Braunschweig, Germany.

Claudia Harting (C)

Department Structure and Function of Proteins, Group Recombinant Protein Expression Helmholtz Centre for Infection Research, Braunschweig, Germany.

Mira Majewski (M)

Department Structure and Function of Proteins, Helmholtz Centre for Infection Research, Braunschweig, Germany.

Veith Vollmer (V)

Department Structure and Function of Proteins, Helmholtz Centre for Infection Research, Braunschweig, Germany.

Mario Köster (M)

Group Model Systems for Infection and Immunity, Helmholtz Centre for Infection Research, Braunschweig, Germany.

Martina Grashoff (M)

Group Innate Immunity and Infection, Helmholtz Centre for Infection Research, Braunschweig, Germany.

Rainer Zawatzky (R)

Department Virale Transformationsmechanismen, Deutsches Krebsforschungszentrum (DKFZ), Heidelberg, Germany.

Joop Van den Heuvel (J)

Department Structure and Function of Proteins, Group Recombinant Protein Expression Helmholtz Centre for Infection Research, Braunschweig, Germany.

Andrea Kröger (A)

Institute of Medical Microbiology, Otto-von-Guericke-University, Magdeburg, Germany.

Thomas Böldicke (T)

Department Structure and Function of Proteins, Helmholtz Centre for Infection Research, Braunschweig, Germany.

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Classifications MeSH