tetano
Editor, Senior Moderator
J Exp Med. 2017 Feb 28. pii: jem.20161270. doi: 10.1084/jem.20161270. [Epub ahead of print]
[h=1]ZMPSTE24 defends against influenza and other pathogenic viruses.[/h] Fu B[SUP]1[/SUP], Wang L[SUP]2[/SUP], Li S[SUP]3[/SUP], Dorf ME[SUP]4[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] Zinc metallopeptidase STE24 (ZMPSTE24) is a transmembrane metalloprotease whose catalytic activity is critical for processing lamin A on the inner nuclear membrane and clearing clogged translocons on the endoplasmic reticulum. We now report ZMPSTE24 is a virus-specific effector that restricts enveloped RNA and DNA viruses, including influenza A, Zika, Ebola, Sindbis, vesicular stomatitis, cowpox, and vaccinia, but not murine leukemia or adenovirus. ZMPSTE24-mediated antiviral action is independent of protease activity. Coimmunoprecipitation studies indicate ZMPSTE24 can complex with proteins of the interferon-induced transmembrane protein (IFITM) family. IFITM proteins impede viral entry, and ZMPSTE24 expression is necessary for IFITM antiviral activity. In vivo studies demonstrate ZMPSTE24-deficient mice display higher viral burdens, enhanced cytokine production, and increased mortality after influenza infection. Collectively, these findings identify ZMPSTE24 as an intrinsic broad-spectrum antiviral protein and provide insights into antiviral defense mechanisms.
? 2017 Fu et al.
PMID: 28246125 DOI: 10.1084/jem.20161270
[PubMed - as supplied by publisher]
[h=1]ZMPSTE24 defends against influenza and other pathogenic viruses.[/h] Fu B[SUP]1[/SUP], Wang L[SUP]2[/SUP], Li S[SUP]3[/SUP], Dorf ME[SUP]4[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] Zinc metallopeptidase STE24 (ZMPSTE24) is a transmembrane metalloprotease whose catalytic activity is critical for processing lamin A on the inner nuclear membrane and clearing clogged translocons on the endoplasmic reticulum. We now report ZMPSTE24 is a virus-specific effector that restricts enveloped RNA and DNA viruses, including influenza A, Zika, Ebola, Sindbis, vesicular stomatitis, cowpox, and vaccinia, but not murine leukemia or adenovirus. ZMPSTE24-mediated antiviral action is independent of protease activity. Coimmunoprecipitation studies indicate ZMPSTE24 can complex with proteins of the interferon-induced transmembrane protein (IFITM) family. IFITM proteins impede viral entry, and ZMPSTE24 expression is necessary for IFITM antiviral activity. In vivo studies demonstrate ZMPSTE24-deficient mice display higher viral burdens, enhanced cytokine production, and increased mortality after influenza infection. Collectively, these findings identify ZMPSTE24 as an intrinsic broad-spectrum antiviral protein and provide insights into antiviral defense mechanisms.
? 2017 Fu et al.
PMID: 28246125 DOI: 10.1084/jem.20161270
[PubMed - as supplied by publisher]