How Influenza Virus Uses Host Cell Pathways during Uncoating

Moreira, Étori Aguiar; Yamauchi, Yohei; Matthias, Patrick

doi:10.3390/cells10071722

Cited by 25 publications

(16 citation statements)

References 258 publications

(321 reference statements)

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“…M1 is a bridge that connects M2, HA, and NA ( Peukes et al, 2020 ). M2 protein is recruited to the cell membrane to mediate membrane scission, and sialic acid connected with HA is destroyed by NA to release the virion ( Moreira et al, 2021 ). In these processes, the viral proteins as well as a large number of host factors are required to mediate the ion channel activity of M2 and its membrane scission.…”

Section: Discussionmentioning

confidence: 99%

YWHAG inhibits influenza a virus replication by suppressing the release of viral M2 protein

Mao

Cao²,

Xu³

et al. 2022

Front. Microbiol.

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Influenza A virus (IAV) poses a serious threat to human life and property. The IAV matrix protein 2 (M2) is significant in viral budding. Increasing studies have proven the important roles of host factors in IAV replication. In this study, immunoprecipitation combined with mass spectrometry revealed that the host protein tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein gamma (YWHAG), which belongs to the 14-3-3 protein scaffold family, interacts with M2. Their interactions were further confirmed by co-immunoprecipitation (Co-IP), immunofluorescence, and confocal microscopy of virus-infected HeLa cells. Moreover, we constructed YWHAG-KO and YWHAG-overexpressing cells and found that YWHAG knockout significantly increased viral production, whereas its overexpression reduced the titer of virus progeny. Therefore, YWHAG is a negative regulatory factor during IAV infection. Further, YWHAG knockout or overexpression had no effect on the binding, entry, or viral RNA replication in the early stages of the virus life cycle. On the contrary, it impaired the release of virions at the plasma membrane as determined using transmission electron microscopy and suppressed the M2-mediated budding of the influenza virus. Importantly, the H158F mutation of YWHAG was found to affect interaction with M2 and its budding. Collectively, our work demonstrates that YWHAG is a novel cellular regulator that targets and mediates the interaction and release of M2.

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Section: Discussionmentioning

confidence: 99%

YWHAG inhibits influenza a virus replication by suppressing the release of viral M2 protein

Mao

Cao²,

Xu³

et al. 2022

Front. Microbiol.

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“…IAV virions are enveloped, pleiomorphic particles in the shape of spheres with a diameter of 100 nm, or filaments with a diameter of 100 nm to 30 µm [20]. They are composed of three main subviral components: an envelope, a layer of matrix 1 (M1) proteins, and a viral ribonucleoprotein (vRNP) core.…”

Section: Influenza a Virus Structurementioning

confidence: 99%

Avian Influenza Virus Tropism in Humans

Bakar¹,

Amrani²,

Kamarulzaman³

et al. 2023

Preprint

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A pandemic happens when a novel influenza A virus is able to infect and transmit efficiently to a new, distinct host species. Although the exact timing of pandemics is uncertain, it is known that both viral and host factors play a role in their emergence. Species-specific interactions between the virus and the host cell determine the virus tropism. These include binding and entering cells, replicating the viral RNA genome within the host cell nucleus, assembling, maturing, and releasing the virus to neighbouring cells, tissues, or organs before transmitting it between individuals. Influenza has a vast and antigenically varied reservoir. In wild aquatic birds, the infection is typically asymptomatic. Avian influenza virus (AIV) can cross into new species, and occasionally, it can acquire the ability to transmit from human to human. A pandemic might occur if a new influenza virus acquires enough adaptive mutations to maintain transmission between people. This review highlights the key determinants AIV must achieve to initiate a human pandemic and describes how AIV mutates to establish tropism and stable human adaptation. Understanding the tropism of AIV may be crucial in preventing virus transmission in humans and may help design vaccines, antivirals and therapeutic agents against the virus.

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“…These routes are commonly defined by the protein coat enveloping the vesicles (e.g., clathrin or caveolin), by their dependence on cholesterol or specific enzymes (e.g., dynamin), and by the involvement of the cytoskeleton (e.g., actin) ( Nabi and Le, 2003 ; Lakadamyali et al, 2004 ; Yarar et al, 2005 ; Boucrot et al, 2006 ; Kaksonen et al, 2006 ; Lajoie and Nabi, 2007 ; Hirschhorn and Ehrlich, 2013 ; Sun and Whittaker, 2013 ; Yamauchi and Helenius, 2013 ; Johannes et al, 2015 ; Staring et al, 2018 ; Moreira et al, 2021 ). The difference in the usage of various endocytic routes is exemplified by the influenza A virus (IAV), which is differentially dependent on clathrin-mediated endocytosis, with dependence on the cellular context ( Sieczkarski and Whittaker, 2002 ; Lakadamyali et al, 2003 ; Zhang and Whittaker, 2014 ; Moreira et al, 2021 ). At the endocytic step per se or after internalization of virus-containing endocytic vesicles, multiple viruses exhibit differential dependence on the structure and function of the actin and microtubule cytoskeleton.…”

Section: Introductionmentioning

confidence: 99%

Mapping of Tilapia Lake Virus entry pathways with inhibitors reveals dependence on dynamin activity and cholesterol but not endosomal acidification

Rass

Kembou-Ringert²,

Zamostiano³

et al. 2022

Front. Cell Dev. Biol.

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Tilapia Lake Virus (TiLV) is an emerging virus lethal to tilapia, which threatens the global tilapia aquaculture with severe implications for food security. TiLV possesses similar features to orthomyxoviruses but is classified in the sole and the monotypic genus Tilapinevirus of the family Amnoonviridae. TiLV enveloped virions encapsidate a genome comprising ten segments of single-stranded, negative RNA. Remarkably, nine of TiLV’s ten major proteins lack sequence homology to any known viral or cellular proteins. The mode of TiLV entry into tilapia cells is not known. Following the measurement of the entry window of TiLV (∼3 h), we applied a panel of inhibitors of known regulators of endocytic functions to map the molecular requirements for TiLV entry. We identified productive entry by quantification of TiLV nucleoprotein expression and the generation of infectious particles. Inhibition of dynamin activity with dynasore or dynole, or depletion of cholesterol with methyl-β-cyclodextrin, strongly inhibited TiLV protein synthesis and infectious virion production. Moreover, inhibition of actin cytoskeleton polymerization with latrunculin A or microtubule polymerization with nocodazole within the entry window resulted in partial inhibition of TiLV infection. In contrast, inhibitors of endosomal acidification (NH4Cl, bafilomycin A1, or chloroquine), an inhibitor of clathrin-coated pit assembly (pitstop 2), and erlotinib—an inhibitor of the endocytic Cyclin G-associated kinase (GAK), did not affect TiLV entry. Altogether, these results suggest that TiLV enters via dynamin-mediated endocytosis in a cholesterol-, cytoskeleton-dependent manner, and clathrin-, pH-independent manner. Thus, despite being an orthomyx-like virus, when compared to the prototypical orthomyxovirus (influenza A virus), TiLV shows a distinct set of requirements for entry into cells.

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How Influenza Virus Uses Host Cell Pathways during Uncoating

Cited by 25 publications

References 258 publications

YWHAG inhibits influenza a virus replication by suppressing the release of viral M2 protein

YWHAG inhibits influenza a virus replication by suppressing the release of viral M2 protein

Avian Influenza Virus Tropism in Humans

Mapping of Tilapia Lake Virus entry pathways with inhibitors reveals dependence on dynamin activity and cholesterol but not endosomal acidification

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