HUIBIN YU

Dr. HUIBIN YU

orcid

Research Focus & Metrics

Academic Career Length

12Years (2015-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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1 July 2021 in Biomedicines
Verified
Journal Article
Open access
PDF file
HYHUIBIN YU
HUIBIN YU
RBRyan C. Bruneau
Ryan C. Bruneau
Greg BrennanGreg Brennan
Greg Brennan
Stefan RothenburgStefan Rothenburg
Stefan Rothenburg
Host pattern recognition receptors (PRRs) sense pathogen-associated molecular patterns (PAMPs), which are molecular signatures shared by different pathogens. Recognition of PAMPs by PRRs initiate innate immune responses via diverse signaling pathways. Over recent decades, advances in our knowledge of innate immune sensing have enhanced our understanding of the host immune response to poxviruses. Multiple PRR families have been implicated in poxvirus detection, mediating the initiation of signaling cascades, activation of transcription factors, and, ultimately, the expression of antiviral effectors. To counteract the host immune defense, poxviruses have evolved a variety of immunomodulators that have diverse strategies to disrupt or circumvent host antiviral responses triggered by PRRs. These interactions influence the outcomes of poxvirus infections. This review focuses on our current knowledge of the roles of PRRs in the recognition of poxviruses, their elicited antiviral effector functions, and how poxviral immunomodulators antagonize PRR-mediated host immune responses.

28 February 2023 in mBio
Verified
Journal Article
Open access
GBGreg Brennan
Greg Brennan
ASAna M. M. Stoian
Ana M. M. Stoian
HYHUIBIN YU
HUIBIN YU
MRM. Julhasur Rahman
M. Julhasur Rahman
SBShefali Banerjee
Shefali Banerjee
Stefan RothenburgStefan Rothenburg
Stefan Rothenburg
Poxviruses are often thought to evolve relatively slowly because they are double-stranded DNA pathogens with proofreading polymerases. However, poxviruses have highly adaptable genomes and can undergo relatively rapid genotypic and phenotypic change, as illustrated by the recent increase in human-to-human transmission of monkeypox virus.

1 January 2019 in Cell Reports
Verified
Journal Article
Open access
KZKunli Zhang
Kunli Zhang
YZYuanfeng Zhang
Yuanfeng Zhang
JXJuan Xue
Juan Xue
QMQingwen Meng
Qingwen Meng
HLHongyang Liu
Hongyang Liu
changjiang wengchangjiang weng
changjiang weng
DExD/H-box helicase members are key receptors for recognizing viral nucleic acids, and they regulate retinoic acid-inducible gene I (RIG-I)-like receptor (RLR)-mediated type I interferon (IFN) production. Here, we report that the DExD/H-box helicase family member DExD/H-box RNA helicase 19 (DDX19) is a negative regulator of type I IFN production. Ectopic expression of DDX19 suppressed poly(I:C) (polyinosinic-polycytidylic acid)- and Sendai-virus-induced type I IFN production, whereas knockdown of DDX19 expression enhanced type I IFN production. Mechanistically, DDX19 inhibited TANK-binds kinase 1 (TBK1)- and inhibitor-κb kinase ε (IKKε)-mediated phosphorylation of interferon regulatory factor 3 (IRF3) by disrupting the interaction between TBK1 or IKKε and IRF3. Additionally, DDX19 recruited Lamtor2 and then formed the TBK1-IKKε-Lamtor2-DDX19-IRF3 complex to suppress IFN production by promoting TBK1 and IKKε degradation. We generated Ddx19 knockout mice using transcription activator-like effector nucleases (TALENs) and found that Ddx19 deficiency in vivo augmented type I IFN production, resulting in suppression of encephalomyocarditis virus replication. These data show that DDX19 is an important negative regulator of RLR-mediated type I IFN production.

1 November 2015 in Journal of Biological Chemistry
Verified
Journal Article
Open access
PDF file
LHLi Huang
Li Huang
QLQinfang Liu
Qinfang Liu
LZLijie Zhang
Lijie Zhang
QZQuan Zhang
Quan Zhang
LHLiang Hu
Liang Hu
CWChangjiang Weng
Changjiang Weng
TRAF family member-associated NF-κB activator (TANK) is a negative regulator of canonical NF-κB signaling in the Toll-like receptor- and B-cell receptor-mediated signaling pathways. However, functions of TANK in viral infection-mediated NF-κB activation remain unclear. Here, we reported that TANK was cleaved by encephalomyocarditis virus 3C at the 197 and 291 glutamine residues, which depends on its cysteine protease activity. In addition, encephalomyocarditis virus 3C impaired the ability of TANK to inhibit TRAF6-mediated NF-κB signaling. Interestingly, we found that several viral proteases encoded by the foot and mouth disease virus, porcine reproductive and respiratory syndrome virus, and equine arteritis virus also cleaved TANK. Our results suggest that TANK is a novel target of some viral proteases, indicating that some positive RNA viruses have evolved to utilize their major proteases to regulate NF-κB activation.

28 February 2023 in Journal of Virology
Verified
Journal Article
Closed access
LHLi Huang
Li Huang
HLHongyang Liu
Hongyang Liu
GYGuangqiang Ye
Guangqiang Ye
XLXiaohong Liu
Xiaohong Liu
WCWeiye Chen
Weiye Chen
changjiang wengchangjiang weng
changjiang weng
African swine fever (ASF), caused by African swine fever virus (ASFV), is a highly contagious and acute hemorrhagic viral disease of domestic pigs, with a high mortality approaching 100%. ASFV has spread rapidly worldwide and caused huge economic losses and ecological consequences.

9 June 2017 in Biochemical Journal
Verified
Journal Article
Open access
PDF file
LHLi Huang
Li Huang
TXTao Xiong
Tao Xiong
HYHUIBIN YU
HUIBIN YU
QZQuan Zhang
Quan Zhang
KZKunli Zhang
Kunli Zhang
changjiang wengchangjiang weng
changjiang weng
TRAF family member-associated NF-κB activator (TANK) is a scaffold protein that assembles into the interferon (IFN) regulator factor 3 (IRF3)-phosphorylating TANK-binding kinase 1 (TBK1)–(IκB) kinase ε (IKKε) complex, where it is involved in regulating phosphorylation of the IRF3 and IFN production. However, the functions of TANK in encephalomyocarditis virus (EMCV) infection-induced type I IFN production are not fully understood. Here, we demonstrated that, instead of stimulating type I IFN production, the EMCV-HB10 strain infection potently inhibited Sendai virus- and polyI:C-induced IRF3 phosphorylation and type I IFN production in HEK293T cells. Mechanistically, EMCV 3C protease (EMCV 3C) cleaved TANK and disrupted the TANK–TBK1–IKKε–IRF3 complex, which resulted in the reduction in IRF3 phosphorylation and type I IFN production. Taken together, our findings demonstrate that EMCV adopts a novel strategy to evade host innate immune responses through cleavage of TANK.