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Sars Cov 2 Hijacks sentence examples within host immune system

host immune system

Like other coronavirae, SARS-CoV-2 hijacks host cell secretory machinery to produce viral proteins that compose the nascent virions; including Spike (S), Envelope (E) and Membrane (M) proteins, the most exposed transmembrane proteins to the host immune system.

SARS-CoV-2 integral membrane proteins shape the serological responses of patients with COVID-19

host immune system

Similar to other coronavirae, SARS-CoV-2 hijacks the host cell complex secretory machinery to produce properly folded viral proteins that will compose the nascent virions; including Spike, Envelope and Membrane proteins, the most exposed membrane viral proteins to the host immune system.

SARS-CoV2 envelop proteins reshape the serological responses of COVID-19 patients

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10.1016/j.isci.2021.103185

Like other coronavirae, SARS-CoV-2 hijacks host cell secretory machinery to produce viral proteins that compose the nascent virions; including Spike (S), Envelope (E) and Membrane (M) proteins, the most exposed transmembrane proteins to the host immune system.

SARS-CoV-2 integral membrane proteins shape the serological responses of patients with COVID-19

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10.1038/s41423-020-00603-6

We hypothesized that SARS-CoV-2 hijacks the host ubiquitin system to enhance ORF7a’s ability to antagonize IFN-I responses.

Ubiquitination of SARS-CoV-2 ORF7a promotes antagonism of interferon response

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10.1101/2021.02.15.431237

Similar to other coronavirae, SARS-CoV-2 hijacks the host cell complex secretory machinery to produce properly folded viral proteins that will compose the nascent virions; including Spike, Envelope and Membrane proteins, the most exposed membrane viral proteins to the host immune system.

SARS-CoV2 envelop proteins reshape the serological responses of COVID-19 patients

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10.32388/PE4TSQ.4

SARS-CoV-2 hijacks the host cell glycotransferase resulting in spike protein glycosylation resembling blood type antigens.

Miglustat: A glycotransferase inhibitor for Covid-19 treatment

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10.3389/fcimb.2021.678482

Transcriptome analysis of infected pancreatic cultures confirmed that SARS-CoV-2 hijacks the ribosomal machinery in these cells.

Deleterious Effects of SARS-CoV-2 Infection on Human Pancreatic Cells

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10.36648/1791-809X.15.2.807

SARS-CoV-2 hijacks the host cell glycotransferase resulting in spike protein glycosylation resembling blood type antigens.

Miglustat: A Glycotransferase Inhibitorfor Covid-19 Treatment

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10.1101/2021.02.01.21250846

Transcriptome analysis of infected pancreatic cultures confirmed that SARS-CoV-2 hijacks the ribosomal machinery in these cells.

Deleterious effects of SARS-CoV-2 infection on human pancreatic cells

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10.2139/SSRN.3821960

Similar to other coronavirae, SARS-CoV-2 hijacks the host cell complex secretory machinery to produce properly folded viral proteins that will compose the nascent virions; including Spike, Envelope and Membrane proteins, the most exposed membrane viral proteins to the host immune system.

SARS-CoV2 Envelop Proteins Reshape the Serological Responses of COVID-19 Patients

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10.1038/s41392-021-00786-y

1i, j), implying that SARS-CoV-2 hijacks host hnRNP A2/B1 protein redistribution through direct binding with NSP1 to impair host innate immunity to facilitate SARS-CoV-2 infection.

Attenuating innate immunity and facilitating β-coronavirus infection by NSP1 of SARS-CoV-2 through specific redistributing hnRNP A2/B1 cellular localization

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10.1101/2021.06.21.449284

Here, we provide evidence that SARS-CoV-2 hijacks the glycosylation biosynthetic, ER-stress and UPR machineries for viral replication using a time-resolved (0-48 hours post infection, hpi) total, membrane as well as glycoproteome mapping and orthogonal validation.

SARS-CoV-2 activates ER stress and Unfolded protein response

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10.1101/2021.07.23.453505

In addition to explaining the increased incidence of SARS in males, these findings indicate that SARS-Cov-2 hijacks epithelial immune signaling to promote infection of the alveolar epithelium and suggest that JAK inhibitors, singly and in combination with NF-KB inhibitors, may exhibit efficacy in preventing or treating COVID-19 SARS.

SARS-CoV-2 Exploits Sexually Dimorphic and Adaptive IFN and TNFa Signaling to Gain Entry into Alveolar Epithelium

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10.1101/2021.07.22.453345

Collectively, our data suggest that SARS-CoV-2 hijacks components of the host antiviral machinery to edit its genome and fuel its evolution.

ADAR mediated A-to-I RNA editing affects SARS-CoV-2 characteristics and fuels its evolution

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Sars Cov 2 Hijacks - Like other coronavirae, SARS-CoV-2 hijacks host cell secretory machinery to produce viral proteins that compose the nascent virions; including Spike (S), Envelope (E) and Membrane (M) proteins, the most exposed transmembrane proteins to the host immune system. [1] We hypothesized that SARS-CoV-2 hijacks the host ubiquitin system to enhance ORF7a’s ability to antagonize IFN-I responses. [2] Similar to other coronavirae, SARS-CoV-2 hijacks the host cell complex secretory machinery to produce properly folded viral proteins that will compose the nascent virions; including Spike, Envelope and Membrane proteins, the most exposed membrane viral proteins to the host immune system. [3] SARS-CoV-2 hijacks the host cell glycotransferase resulting in spike protein glycosylation resembling blood type antigens. [4] Transcriptome analysis of infected pancreatic cultures confirmed that SARS-CoV-2 hijacks the ribosomal machinery in these cells. [5] SARS-CoV-2 hijacks the host cell glycotransferase resulting in spike protein glycosylation resembling blood type antigens. [6] Transcriptome analysis of infected pancreatic cultures confirmed that SARS-CoV-2 hijacks the ribosomal machinery in these cells. [7] Similar to other coronavirae, SARS-CoV-2 hijacks the host cell complex secretory machinery to produce properly folded viral proteins that will compose the nascent virions; including Spike, Envelope and Membrane proteins, the most exposed membrane viral proteins to the host immune system. [8] 1i, j), implying that SARS-CoV-2 hijacks host hnRNP A2/B1 protein redistribution through direct binding with NSP1 to impair host innate immunity to facilitate SARS-CoV-2 infection. [9] Here, we provide evidence that SARS-CoV-2 hijacks the glycosylation biosynthetic, ER-stress and UPR machineries for viral replication using a time-resolved (0-48 hours post infection, hpi) total, membrane as well as glycoproteome mapping and orthogonal validation. [10] In addition to explaining the increased incidence of SARS in males, these findings indicate that SARS-Cov-2 hijacks epithelial immune signaling to promote infection of the alveolar epithelium and suggest that JAK inhibitors, singly and in combination with NF-KB inhibitors, may exhibit efficacy in preventing or treating COVID-19 SARS. [11] Collectively, our data suggest that SARS-CoV-2 hijacks components of the host antiviral machinery to edit its genome and fuel its evolution. [12]

host immune system

Like other coronavirae, SARS-CoV-2 hijacks host cell secretory machinery to produce viral proteins that compose the nascent virions; including Spike (S), Envelope (E) and Membrane (M) proteins, the most exposed transmembrane proteins to the host immune system. [1] Similar to other coronavirae, SARS-CoV-2 hijacks the host cell complex secretory machinery to produce properly folded viral proteins that will compose the nascent virions; including Spike, Envelope and Membrane proteins, the most exposed membrane viral proteins to the host immune system. [2] Similar to other coronavirae, SARS-CoV-2 hijacks the host cell complex secretory machinery to produce properly folded viral proteins that will compose the nascent virions; including Spike, Envelope and Membrane proteins, the most exposed membrane viral proteins to the host immune system. [3]