TIM-1 Promotes Japanese Encephalitis Virus Entry and Infection

Niu, Jichen; Jiang, Ya Qiong; Xu, Hao; Zhao, Changjing; Zhou, Guodong; Pu-yan, Chen; Cao, Ruibing

doi:10.3390/v10110630

Cited by 35 publications

(25 citation statements)

References 47 publications

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“…Given that an increase in cellular autophagy facilitates the production of many viruses, a common evolutionary selection exists among various viruses to trigger or activate autophagy [16,22]. Additionally, TIM-1 is recognized as a cellular receptor of various viruses to facilitate viral infection [39,40,41,42,43,44,45,46]. In this study, we showed a novel role of TIM-1 to activate autophagy through the TIM-1-p85 signaling axis in the early phase of DENV infection, suggesting the dependence of TIM-1 on the activation of autophagy of DENV infection.…”

Section: Discussionmentioning

confidence: 99%

“…TIM-1 is also known as Hepatitis A virus (HAV) cellular receptor 1 (HAVCR1), which was first identified as an HAV cellular receptor [38]. Moreover, growing evidence has proven TIM-1 to be a cellular receptor which facilitates viral infection, and existent in a number of various viruses, including Ebola virus (EBOV), Marburg virus (MARV), Lassa virus, HAV, Hepatitis C virus (HCV), JEV, and DENV [39,40,41,42,43,44,45,46]. Several findings have elucidated that TIM-1-mediated enhancement of infection mainly depends on the association of PtdSer exposed on the viral envelop [42,47].…”

Section: Introductionmentioning

confidence: 99%

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TIM-1 As a Signal Receptor Triggers Dengue Virus-Induced Autophagy

Chu¹,

Yang

Peng³

et al. 2019

IJMS

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Dengue virus (DENV) infection triggers the activation of autophagy to facilitate the viral replication cycle from various aspects. Although a number of stimulators are proposed to activate autophagy, none of them appears prior to the uncoating process. Given that T-cell immunoglobulin and mucin domain 1 (TIM-1) receptor is a putative DENV receptor and promotes apoptotic body clearance by autophagy induction, it raises the possibility that TIM-1 may participate in the activation of DENV-induced autophagy. In this study, confocal images first revealed the co-localization of TIM-1 with autophagosomes in DENV-induced autophagy rather than rapamycin-induced autophagy, suggesting the co-transportation of TIM-1 with DENV during infection. The treatment of siRNA to knockdown TIM-1 expression in DENV-infected GFP-microtubule-associated protein light chain 3 (LC3)-Huh7.5 cells revealed that TIM-1 is required not only for DENV cellular internalization but also for autophagy activation. Furthermore, knockdown p85, a subunit of phosphoinositide 3-kinases (PI3Ks), which is co-localized with TIM-1 at rab5-positive endosomes caused the reduction of autophagy, indicating that TIM-1-mediated DENV-induced autophagy requires p85. Taken together, the current study uncovered TIM-1 as a novel factor for triggering autophagy in DENV infection through TIM-1-p85 axis, in addition to serving as a DENV receptor.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

TIM-1 As a Signal Receptor Triggers Dengue Virus-Induced Autophagy

Chu¹,

Yang

Peng³

et al. 2019

IJMS

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“…28 In contrast, TIM-3 and TIM-4 are expressed only in antigen presenting cells (APC), where it mediates the engulfment of apoptotic bodies.The role of TIM receptors during viral infection has just been elucidated and several studies have shown its importance as a common attachment factor for a variety of enveloped viruses through direct interaction with PS of viral envelope 14,15,22,24,29. TIM-1 and -4 expression increases infection of all DENV serotypes and other flaviviruses such as YFV,14 ZIKV,30,31 JEV,32 and WNV 15 in a PSdependent manner. TIM is well described in particular for DENV infection.…”

mentioning

confidence: 99%

Viral receptors for flaviviruses: Not only gatekeepers

Oliveira

Peron²

2019

Journal of Leukocyte Biology

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Arboviruses have been a huge threat for human health since the discovery of yellow fever virus in 1901. Arboviruses are arthropod born viruses, mainly transmitted by mosquitoes and ticks, responsible for more than thousands of deaths annually. The Flavivirideae family is probably the most clinically relevant, as it is composed of very important agents, such as dengue, yellow fever, West Nile, Japanese encephalitis, and, recently, Zika virus. Intriguingly, despite their structural and genomic similarities, flaviviruses may cause conditions ranging from mild infections with fever, cutaneous rash, and headache, to very severe cases, such as hemorrhagic fever, encephalitis, Guillain‐Barré syndrome, and microcephaly. These differences may greatly rely on viral burden, tissue tropism, and mechanisms of immune evasion that may depend on both viral and host genetic factors. Unfortunately, very little is known about the biology of these factors, and how they orchestrate these differences. In this context, viral structural proteins and host cellular receptors may have a great relevance, as their interaction dictates not only viral tissue tropism, but also a plethora on intracellular mechanisms that may greatly account for either failure or success of infection. A great number of viral receptors have been described so far, although there is still a huge gap in understanding their overall role during infection. Here we discuss some important aspects triggered after the interaction of flaviviruses and host membrane receptors, and how they change the overall outcome of the infection.

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“…In addition to the viruses described above, recent studies demonstrated that Japanese encephalitis, hepatitis C, Tacaribe, and Ross River can use at least one of PtdSer-binding molecular mechanisms for their binding to cells [58–60].…”

Section: Identification Of Molecular Mechanisms Mediating Envelope Ptmentioning

confidence: 99%

Roles of phosphatidylserine exposed on the viral envelope and cell membrane in HIV-1 replication

et al. 2019

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Phosphatidylserine (PtdSer) is usually present only in the inner leaf of the lipid bilayers of the cell membrane, but is exposed on the outer leaf when cells are activated and/or die. Exposure of PtdSer has physiological functions. For example, the PtdSer exposed on dead cells can serve as “eat-me signals” for phagocytes to clear dead cells by phagocytosis, which prevents autoimmune reactions and inflammation. HIV-1 induces PtdSer exposure on infected and target cells and it also exposes PtdSer on its envelope. Recent studies showed that PtdSer exposed on the HIV-1 envelope and infected and target cells can facilitate or inhibit multiple steps of HIV-1 replication.At the virus binding and entry steps, interaction of the envelope PtdSer and the host’s PtdSer-binding molecules can enhance HIV-1 infection of cells by facilitating virus attachment. At the virus budding step, HIV-1 can be trapped on the cell surface by one family of PtdSer-binding receptors, T-cell immunoglobulin mucin domain proteins (TIM)-1, 3, and 4 expressed on virus producer cells. Although this trapping can inhibit release of HIV-1, one of the HIV-1 accessory gene products, Negative Factor (Nef), can counteract virus trapping by TIM family receptors (TIMs) by inducing the internalization of these receptors. HIV-1 infection can induce exposure of PtdSer on infected cells by inducing cell death. A soluble PtdSer-binding protein in serum, protein S, bridges PtdSer exposed on HIV-1-infected cells and a receptor tyrosine kinase, Mer, expressed on macrophages and mediate phagocytic clearance of HIV-1 infected cells. HIV-1 can also induce exposure of PtdSer on target cells at the virus binding step. Binding of HIV-1 envelope proteins to its receptor (CD4) and co-receptors (CXCR4 or CCR5) elicit signals that induce PtdSer exposure on target cells by activating TMEM16F, a phospholipid scramblase. PtdSer exposed on target cells enhances HIV-1 infection by facilitating fusion between the viral envelope and target cell membrane. Because various other phospholipid channels mediating PtdSer exposure have recently been identified, it will be of interest to examine how HIV-1 actively interacts with these molecules to manipulate PtdSer exposure levels on cells and viral envelope to support its replication.

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TIM-1 Promotes Japanese Encephalitis Virus Entry and Infection

Cited by 35 publications

References 47 publications

TIM-1 As a Signal Receptor Triggers Dengue Virus-Induced Autophagy

TIM-1 As a Signal Receptor Triggers Dengue Virus-Induced Autophagy

Viral receptors for flaviviruses: Not only gatekeepers

Roles of phosphatidylserine exposed on the viral envelope and cell membrane in HIV-1 replication

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