alexa RIG-I Activation By A Protein-deamidating Complex Consisting A Viral Pseudoenzyme And A Cellular Amidotransferase
ISSN: 1948-5964

Journal of Antivirals & Antiretrovirals
Open Access

Like us on:
OMICS International organises 3000+ Global Conferenceseries Events every year across USA, Europe & Asia with support from 1000 more scientific Societies and Publishes 700+ Open Access Journals which contains over 50000 eminent personalities, reputed scientists as editorial board members.

Open Access Journals gaining more Readers and Citations

700 Journals and 15,000,000 Readers Each Journal is getting 25,000+ Readers

This Readership is 10 times more when compared to other Subscription Journals (Source: Google Analytics)

Share This Page

Additional Info

Loading
Loading Please wait..
 

4th World Congress on Virology
October 06-08, 2014 Hilton San Antonio Airport, TX, USA

Pinghui Feng
Accepted Abstracts: J Antivir Antiretrovir
DOI: 10.4172/1948-5964.S1.022
Abstract
Herpesvirus is one of the most ubiquitous pathogens in nature. A remarkable propensity of all herpesviruses is their ability to establish life-long persistent infection, known as latency. Not surprisingly, herpesviruses have evolved diverse strategies to evade and harness cellular signaling, e.g., innate immune response. We have previously reported that gamma herpesviruses utilize the mitochondrion antiviral signaling (MAVS) adaptor and IKKβ kinase to promote viral lytic replication. Specifically, activated IKK phosphorylates viral key transcription factor (RTA) to enable viral gene expression. Additionally, IKKβ was hijacked to induce the degradation of RelA, thereby terminating NF-κB activation and preventing antiviral cytokine production. These findings highlight an intricate immune evasion strategy and suggest that gamma herpesviruses have dedicated mechanism(s) to activate the MAVS-dependent signaling cascade. Activation of pattern recognition receptors is crucial for host innate immune defense and RIG-I is a genuine RNA sensor. We describe here a mechanism of RIG-I activation enabled by amidotransferase-mediated deamidation. To dissect herpesviral immune evasion strategy, we discovered that viral homologues of phosphoribosylformyglycinamide synthase (PFAS), although lacking intrinsic enzyme activity, recruited cellular PFAS to deamidate RIG-I. Accordingly, depletion or biochemical inhibition of PFAS impaired RIG-I deamidation. Purified PFAS and viral homologues thereof deamidate RIG-I in vitro. Glutaminedeamidation within the first CARD synergized with asparagine-deamidation within the ATPase domain to activate RIG-I. Our findings show that viral pseudo enzymes and cellular PFAS activate RIG-I via deamidation, unveiling a new means by which a pattern recognition receptor is activated by an enzyme and identifying a cellular protein deamidase.
Biography
Feng has obtained his Ph.D from University of Missouri-Kansas City and postdoctoral training from Harvard Medical School. He was a Lymphoma Leukemia Society fellow and special fellow, and is currently an American Cancer Society Scholar. He has published more than 30 papers in reputed journals and serves as an editorial member of Journal of Virology, an editor of PLoS Pathogens.
image PDF   |   image HTML
 
Peer Reviewed Journals
 
Make the best use of Scientific Research and information from our 700 + peer reviewed, Open Access Journals
International Conferences 2017-18
 
Meet Inspiring Speakers and Experts at our 3000+ Global Annual Meetings

Contact Us

 
© 2008-2017 OMICS International - Open Access Publisher. Best viewed in Mozilla Firefox | Google Chrome | Above IE 7.0 version
adwords