Flavivirus Antagonism of Type I Interferon Signaling Reveals Prolidase as a Regulator of IFNAR1 Surface Expression

Type I interferon (IFN-α/β or IFN-I) signals through two receptor subunits, IFNAR1 and IFNAR2, to orchestrate sterile and infectious immunity. Cellular pathways that regulate IFNAR1 are often targeted by viruses to suppress the antiviral effects of IFN-I. Here we report that encephalitic flaviviruse...

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Published in	Cell host & microbe Vol. 18; no. 1; pp. 61 - 74
Main Authors	Lubick, Kirk J., Robertson, Shelly J., McNally, Kristin L., Freedman, Brett A., Rasmussen, Angela L., Taylor, R. Travis, Walts, Avram D., Tsuruda, Seitaro, Sakai, Mizuki, Ishizuka, Mariko, Boer, Elena F., Foster, Erin C., Chiramel, Abhilash I., Addison, Conrad B., Green, Richard, Kastner, Daniel L., Katze, Michael G., Holland, Steven M., Forlino, Antonella, Freeman, Alexandra F., Boehm, Manfred, Yoshii, Kentaro, Best, Sonja M.
Format	Journal Article
Language	English
Published	United States Elsevier Inc 08.07.2015
Subjects	Dipeptidases - metabolism Encephalitis Viruses, Tick-Borne - immunology Fibroblasts - immunology Host-Pathogen Interactions Humans Interferon Type I - metabolism Protein Binding Receptor, Interferon alpha-beta - metabolism Signal Transduction Viral Nonstructural Proteins - metabolism West Nile virus - immunology
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Abstract	Type I interferon (IFN-α/β or IFN-I) signals through two receptor subunits, IFNAR1 and IFNAR2, to orchestrate sterile and infectious immunity. Cellular pathways that regulate IFNAR1 are often targeted by viruses to suppress the antiviral effects of IFN-I. Here we report that encephalitic flaviviruses, including tick-borne encephalitis virus and West Nile virus, antagonize IFN-I signaling by inhibiting IFNAR1 surface expression. Loss of IFNAR1 was associated with binding of the viral IFN-I antagonist, NS5, to prolidase (PEPD), a cellular dipeptidase implicated in primary immune deficiencies in humans. Prolidase was required for IFNAR1 maturation and accumulation, activation of IFNβ-stimulated gene induction, and IFN-I-dependent viral control. Human fibroblasts derived from patients with genetic prolidase deficiency exhibited decreased IFNAR1 surface expression and reduced IFNβ-stimulated signaling. Thus, by understanding flavivirus IFN-I antagonism, prolidase is revealed as a central regulator of IFN-I responses. [Display omitted] •TBEV and WNV inhibit surface expression of the interferon α/β (IFN-I) receptor, IFNAR1•The viral IFN antagonist NS5 binds to prolidase to prevent IFNAR1 surface expression•Prolidase is required for surface expression of IFNAR1•IFN signaling is compromised in fibroblasts from humans with prolidase deficiency Tick-borne encephalitis virus and West Nile virus antagonize type I interferon (IFN-I) signaling through unknown mechanisms. Lubick et al. demonstrate that prolidase promotes surface expression of the IFN-I receptor, IFNAR1, and is a target of viral antagonism. Further, prolidase deficiency in humans is associated with compromised IFN-I signaling.
AbstractList	Type I interferon (IFN-α/β or IFN-I) signals through two receptor subunits, IFNAR1 and IFNAR2, to orchestrate sterile and infectious immunity. Cellular pathways that regulate IFNAR1 are often targeted by viruses to suppress the antiviral effects of IFN-I. Here we report that encephalitic flaviviruses, including tick-borne encephalitis virus and West Nile virus, antagonize IFN-I signaling by inhibiting IFNAR1 surface expression. Loss of IFNAR1 was associated with binding of the viral IFN-I antagonist, NS5, to prolidase (PEPD), a cellular dipeptidase implicated in primary immune deficiencies in humans. Prolidase was required for IFNAR1 maturation and accumulation, activation of IFNβ-stimulated gene induction, and IFN-I-dependent viral control. Human fibroblasts derived from patients with genetic prolidase deficiency exhibited decreased IFNAR1 surface expression and reduced IFNβ-stimulated signaling. Thus, by understanding flavivirus IFN-I antagonism, prolidase is revealed as a central regulator of IFN-I responses. [Display omitted] •TBEV and WNV inhibit surface expression of the interferon α/β (IFN-I) receptor, IFNAR1•The viral IFN antagonist NS5 binds to prolidase to prevent IFNAR1 surface expression•Prolidase is required for surface expression of IFNAR1•IFN signaling is compromised in fibroblasts from humans with prolidase deficiency Tick-borne encephalitis virus and West Nile virus antagonize type I interferon (IFN-I) signaling through unknown mechanisms. Lubick et al. demonstrate that prolidase promotes surface expression of the IFN-I receptor, IFNAR1, and is a target of viral antagonism. Further, prolidase deficiency in humans is associated with compromised IFN-I signaling. Type I interferon (IFN-α/β or IFN-I) signals through two receptor subunits, IFNAR1 and IFNAR2, to orchestrate sterile and infectious immunity. Cellular pathways that regulate IFNAR1 are often targeted by viruses to suppress the antiviral effects of IFN-I. Here we report that encephalitic flaviviruses, including tick-borne encephalitis virus and West Nile virus, antagonize IFN-I signaling by inhibiting IFNAR1 surface expression. Loss of IFNAR1 was associated with binding of the viral IFN-I antagonist, NS5, to prolidase (PEPD), a cellular dipeptidase implicated in primary immune deficiencies in humans. Prolidase was required for IFNAR1 maturation and accumulation, activation of IFNβ-stimulated gene induction, and IFN-I-dependent viral control. Human fibroblasts derived from patients with genetic prolidase deficiency exhibited decreased IFNAR1 surface expression and reduced IFNβ-stimulated signaling. Thus, by understanding flavivirus IFN-I antagonism, prolidase is revealed as a central regulator of IFN-I responses. Type I interferon (IFN-α/β or IFN-I) signals through two receptor subunits, IFNAR1 and IFNAR2, to orchestrate sterile and infectious immunity. Cellular pathways that regulate IFNAR1 are often targeted by viruses to suppress the antiviral effects of IFN-I. Here we report that encephalitic flaviviruses, including tick-borne encephalitis virus and West Nile virus, antagonize IFN-I signaling by inhibiting IFNAR1 surface expression. Loss of IFNAR1 was associated with binding of the viral IFN-I antagonist, NS5, to prolidase (PEPD), a cellular dipeptidase implicated in primary immune deficiencies in humans. Prolidase was required for IFNAR1 maturation and accumulation, activation of IFNβ-stimulated gene induction, and IFN-I-dependent viral control. Human fibroblasts derived from patients with genetic prolidase deficiency exhibited decreased IFNAR1 surface expression and reduced IFNβ-stimulated signaling. Thus, by understanding flavivirus IFN-I antagonism, prolidase is revealed as a central regulator of IFN-I responses.Type I interferon (IFN-α/β or IFN-I) signals through two receptor subunits, IFNAR1 and IFNAR2, to orchestrate sterile and infectious immunity. Cellular pathways that regulate IFNAR1 are often targeted by viruses to suppress the antiviral effects of IFN-I. Here we report that encephalitic flaviviruses, including tick-borne encephalitis virus and West Nile virus, antagonize IFN-I signaling by inhibiting IFNAR1 surface expression. Loss of IFNAR1 was associated with binding of the viral IFN-I antagonist, NS5, to prolidase (PEPD), a cellular dipeptidase implicated in primary immune deficiencies in humans. Prolidase was required for IFNAR1 maturation and accumulation, activation of IFNβ-stimulated gene induction, and IFN-I-dependent viral control. Human fibroblasts derived from patients with genetic prolidase deficiency exhibited decreased IFNAR1 surface expression and reduced IFNβ-stimulated signaling. Thus, by understanding flavivirus IFN-I antagonism, prolidase is revealed as a central regulator of IFN-I responses.
Author	Foster, Erin C. Yoshii, Kentaro Ishizuka, Mariko Boer, Elena F. Rasmussen, Angela L. Sakai, Mizuki Taylor, R. Travis Lubick, Kirk J. Freeman, Alexandra F. Kastner, Daniel L. Holland, Steven M. McNally, Kristin L. Addison, Conrad B. Green, Richard Forlino, Antonella Tsuruda, Seitaro Freedman, Brett A. Katze, Michael G. Robertson, Shelly J. Best, Sonja M. Boehm, Manfred Chiramel, Abhilash I. Walts, Avram D.
AuthorAffiliation	7 Immunopathogenesis Section, Laboratory of Clinical Infectious Diseases, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD, 20814, USA 6 Metabolic, Cardiovascular and Inflammatory Disease Genomics Branch, National Human Genome Research Institute, NIH, Bethesda, MD, 20892, USA 1 Laboratory of Virology, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, NIH, Hamilton, MT, 59840, USA 4 Translational Medicine Branch, National Heart, Lung, and Blood Institute, NIH, Bethesda, MD, 20892, USA 5 Laboratory of Public Health, Graduate School of Veterinary Medicine, Hokkaido University, Sapporo, Hokkaido, 060-0818, Japan 8 Department of Molecular Medicine, Biochemistry Unit, University of Pavia, 27100 Pavia, Italy 2 Department of Microbiology, University of Washington, Seattle, Washington, 98109, USA 3 Department of Medical Microbiology and Immunology, College of Medicine, University of Toledo Health Science Campus, Toledo, OH, 43614, USA
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Travis organization: Department of Medical Microbiology and Immunology, College of Medicine, University of Toledo Health Science Campus, Toledo, OH 43614, USA – sequence: 7 givenname: Avram D. surname: Walts fullname: Walts, Avram D. organization: Translational Medicine Branch, National Heart, Lung, and Blood Institute, NIH, Bethesda, MD 20892, USA – sequence: 8 givenname: Seitaro surname: Tsuruda fullname: Tsuruda, Seitaro organization: Laboratory of Public Health, Graduate School of Veterinary Medicine, Hokkaido University, Sapporo, Hokkaido, 060-0818, Japan – sequence: 9 givenname: Mizuki surname: Sakai fullname: Sakai, Mizuki organization: Laboratory of Public Health, Graduate School of Veterinary Medicine, Hokkaido University, Sapporo, Hokkaido, 060-0818, Japan – sequence: 10 givenname: Mariko surname: Ishizuka fullname: Ishizuka, Mariko organization: Laboratory of Public Health, Graduate School of Veterinary Medicine, Hokkaido University, Sapporo, Hokkaido, 060-0818, Japan – sequence: 11 givenname: Elena F. surname: Boer fullname: Boer, Elena F. organization: Laboratory of Virology, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, NIH, Hamilton, MT 59840, USA – sequence: 12 givenname: Erin C. surname: Foster fullname: Foster, Erin C. organization: Laboratory of Virology, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, NIH, Hamilton, MT 59840, USA – sequence: 13 givenname: Abhilash I. surname: Chiramel fullname: Chiramel, Abhilash I. organization: Laboratory of Virology, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, NIH, Hamilton, MT 59840, USA – sequence: 14 givenname: Conrad B. surname: Addison fullname: Addison, Conrad B. organization: Laboratory of Virology, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, NIH, Hamilton, MT 59840, USA – sequence: 15 givenname: Richard surname: Green fullname: Green, Richard organization: Department of Microbiology, University of Washington, Seattle, WA 98109, USA – sequence: 16 givenname: Daniel L. surname: Kastner fullname: Kastner, Daniel L. organization: Metabolic, Cardiovascular and Inflammatory Disease Genomics Branch, National Human Genome Research Institute, NIH, Bethesda, MD 20892, USA – sequence: 17 givenname: Michael G. surname: Katze fullname: Katze, Michael G. organization: Department of Microbiology, University of Washington, Seattle, WA 98109, USA – sequence: 18 givenname: Steven M. surname: Holland fullname: Holland, Steven M. organization: Immunopathogenesis Section, Laboratory of Clinical Infectious Diseases, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20814, USA – sequence: 19 givenname: Antonella surname: Forlino fullname: Forlino, Antonella organization: Department of Molecular Medicine, Biochemistry Unit, University of Pavia, 27100 Pavia, Italy – sequence: 20 givenname: Alexandra F. surname: Freeman fullname: Freeman, Alexandra F. organization: Immunopathogenesis Section, Laboratory of Clinical Infectious Diseases, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20814, USA – sequence: 21 givenname: Manfred surname: Boehm fullname: Boehm, Manfred organization: Translational Medicine Branch, National Heart, Lung, and Blood Institute, NIH, Bethesda, MD 20892, USA – sequence: 22 givenname: Kentaro surname: Yoshii fullname: Yoshii, Kentaro organization: Laboratory of Public Health, Graduate School of Veterinary Medicine, Hokkaido University, Sapporo, Hokkaido, 060-0818, Japan – sequence: 23 givenname: Sonja M. surname: Best fullname: Best, Sonja M. email: sbest@niaid.nih.gov organization: Laboratory of Virology, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, NIH, Hamilton, MT 59840, USA
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Snippet	Type I interferon (IFN-α/β or IFN-I) signals through two receptor subunits, IFNAR1 and IFNAR2, to orchestrate sterile and infectious immunity. Cellular...
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SubjectTerms	Dipeptidases - metabolism Encephalitis Viruses, Tick-Borne - immunology Fibroblasts - immunology Host-Pathogen Interactions Humans Interferon Type I - metabolism Protein Binding Receptor, Interferon alpha-beta - metabolism Signal Transduction Viral Nonstructural Proteins - metabolism West Nile virus - immunology
Title	Flavivirus Antagonism of Type I Interferon Signaling Reveals Prolidase as a Regulator of IFNAR1 Surface Expression
URI	https://dx.doi.org/10.1016/j.chom.2015.06.007 https://www.ncbi.nlm.nih.gov/pubmed/26159719 https://www.proquest.com/docview/1695757776 https://pubmed.ncbi.nlm.nih.gov/PMC4505794
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