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Inhibition of IRGM establishes a robust antiviral immune state to restrict pathogenic viruses

Nath, Parej ; Chauhan, Nishant Ranjan ; Jena, Kautilya Kumar ; [et al.]

EMBO ; 2021

In: EMBO reports Vol. 22, No. 11 ( 2021-11-04)

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In: EMBO reports, EMBO, Vol. 22, No. 11 ( 2021-11-04)

Type of Medium: Online Resource

ISSN: 1469-221X , 1469-3178

URL: Article

DOI: 10.15252/embr.202152948

Language: English

Publisher: EMBO

Publication Date: 2021

detail.hit.zdb_id: 2025376-X

SSG: 12

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Moxidectin and Ivermectin Inhibit SARS-CoV-2 Replication in Vero E6 Cells but Not in Human Primary Bronchial Epithelial Cells

Dinesh Kumar, Nilima ; ter Ellen, Bram M. ; Bouma, Ellen M. ; [et al.]

American Society for Microbiology ; 2022

In: Antimicrobial Agents and Chemotherapy Vol. 66, No. 1 ( 2022-01-18)

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In: Antimicrobial Agents and Chemotherapy, American Society for Microbiology, Vol. 66, No. 1 ( 2022-01-18)

Abstract: Antiviral therapies are urgently needed to treat and limit the development of severe COVID-19 disease. Ivermectin, a broad-spectrum anti-parasitic agent, has been shown to have anti-SARS-CoV-2 activity in Vero cells at a concentration of 5 μM. These limited in vitro results triggered the investigation of ivermectin as a treatment option to alleviate COVID-19 disease. However, in April 2021, the World Health Organization stated the following: “The current evidence on the use of ivermectin to treat COVID-19 patients is inconclusive.” It is speculated that the in vivo concentration of ivermectin is too low to exert a strong antiviral effect. Here, we performed a head-to-head comparison of the antiviral activity of ivermectin and the structurally related, but metabolically more stable moxidectin in multiple in vitro models of SARS-CoV-2 infection, including physiologically relevant human respiratory epithelial cells. Both moxidectin and ivermectin exhibited antiviral activity in Vero E6 cells. Subsequent experiments revealed that these compounds predominantly act on the steps following virus cell entry. Surprisingly, however, in human-airway-derived cell models, both moxidectin and ivermectin failed to inhibit SARS-CoV-2 infection, even at concentrations of 10 μM. These disappointing results call for a word of caution in the interpretation of anti-SARS-CoV-2 activity of drugs solely based on their activity in Vero cells. Altogether, these findings suggest that even using a high-dose regimen of ivermectin, or switching to another drug in the same class, is unlikely to be useful for treatment of SARS-CoV-2 in humans.

Type of Medium: Online Resource

ISSN: 0066-4804 , 1098-6596

URL: Article

DOI: 10.1128/AAC.01543-21

RVK:

XA 24552

Language: English

Publisher: American Society for Microbiology

Publication Date: 2022

detail.hit.zdb_id: 1496156-8

SSG: 12

SSG: 15,3

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Resveratrol and Pterostilbene Inhibit SARS-CoV-2 Replication in Air–Liquid Interface Cultured Human Primary Bronchial Epithelial Cells

ter Ellen, Bram M. ; Dinesh Kumar, Nilima ; Bouma, Ellen M. ; [et al.]

MDPI AG ; 2021

In: Viruses Vol. 13, No. 7 ( 2021-07-10), p. 1335-

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In: Viruses, MDPI AG, Vol. 13, No. 7 ( 2021-07-10), p. 1335-

Abstract: The current COVID-19 pandemic is caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and has an enormous impact on human health and economy. In search for therapeutic options, researchers have proposed resveratrol, a food supplement with known antiviral, anti-inflammatory, and antioxidant properties as an advantageous antiviral therapy for SARS-CoV-2 infection. Here, we provide evidence that both resveratrol and its metabolically more stable structural analog, pterostilbene, exhibit potent antiviral properties against SARS-CoV-2 in vitro. First, we show that resveratrol and pterostilbene antiviral activity in African green monkey kidney cells. Both compounds actively inhibit virus replication within infected cells as reduced virus progeny production was observed when the compound was added at post-inoculation conditions. Without replenishment of the compound, antiviral activity was observed up to roughly five rounds of replication, demonstrating the long-lasting effect of these compounds. Second, as the upper respiratory tract represents the initial site of SARS-CoV-2 replication, we also assessed antiviral activity in air–liquid interface (ALI) cultured human primary bronchial epithelial cells, isolated from healthy volunteers. Resveratrol and pterostilbene showed a strong antiviral effect in these cells up to 48 h post-infection. Collectively, our data indicate that resveratrol and pterostilbene are promising antiviral compounds to inhibit SARS-CoV-2 infection. Because these results represent laboratory findings in cells, we advocate evaluation of these compounds in clinical trials before statements are made whether these drugs are advantageous for COVID-19 treatment.

Type of Medium: Online Resource

ISSN: 1999-4915

URL: Article

DOI: 10.3390/v13071335

Language: English

Publisher: MDPI AG

Publication Date: 2021

detail.hit.zdb_id: 2516098-9

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Repurposing the HCV NS3–4A protease drug boceprevir as COVID-19 therapeutics

Oerlemans, Rick ; Ruiz-Moreno, Angel Jonathan ; Cong, Yingying ; [et al.]

Royal Society of Chemistry (RSC) ; 2021

In: RSC Medicinal Chemistry Vol. 12, No. 3 ( 2021), p. 370-379

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In: RSC Medicinal Chemistry, Royal Society of Chemistry (RSC), Vol. 12, No. 3 ( 2021), p. 370-379

Abstract: The rapid growth of COVID-19 cases is causing an increasing death toll and also paralyzing the world economy. De novo drug discovery takes years to move from idea and/or pre-clinic to market, and it is not a short-term solution for the current SARS-CoV-2 pandemic. Drug repurposing is perhaps the only short-term solution, while vaccination is a middle-term solution. Here, we describe the discovery path of the HCV NS3–4A protease inhibitors boceprevir and telaprevir as SARS-CoV-2 main protease (3CLpro) inhibitors. Based on our hypothesis that α-ketoamide drugs can covalently bind to the active site cysteine of the SARS-CoV-2 3CLpro, we performed docking studies, enzyme inhibition and co-crystal structure analyses and finally established that boceprevir, but not telaprevir, inhibits replication of SARS-CoV-2 and mouse hepatitis virus (MHV), another coronavirus, in cell culture. Based on our studies, the HCV drug boceprevir deserves further attention as a repurposed drug for COVID-19 and potentially other coronaviral infections as well.

Type of Medium: Online Resource

ISSN: 2632-8682

URL: Article

DOI: 10.1039/D0MD00367K

Language: English

Publisher: Royal Society of Chemistry (RSC)

Publication Date: 2021

detail.hit.zdb_id: 3005515-5

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Cooperativity of catalytic and lectin-like domain of Trypanosoma congolense trans-sialidase modulates its catalytic activity

Waespy, Mario ; Gbem, Thaddeus Termulun ; Dinesh Kumar, Nilima ; [et al.]

Public Library of Science (PLoS) ; 2022

In: PLOS Neglected Tropical Diseases Vol. 16, No. 2 ( 2022-2-7), p. e0009585-

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In: PLOS Neglected Tropical Diseases, Public Library of Science (PLoS), Vol. 16, No. 2 ( 2022-2-7), p. e0009585-

Abstract: Trans-sialidases (TS) represent a multi-gene family of unusual enzymes, which catalyse the transfer of terminal sialic acids (Sia) from sialoglycoconjugates to terminal galactose or N -acetylgalactosamine residues of oligosaccharides without the requirement of CMP-Neu5Ac, the activated Sia used by typical sialyltransferases. Enzymes comprise a N-terminal catalytic domain (CD) followed by a lectin-like domain (LD). Most work on trypanosomal TS has been done on enzymatic activities focusing on the CD of TS from Trypanosoma cruzi (causing Chagas disease in Latin America), subspecies of Trypanosoma brucei , (causing human sleeping sickness in Africa) and Trypanosoma congolense (causing African Animal Trypanosomosis in livestock). Previously, we demonstrated that T . congolense TS (TconTS)-LD binds to several carbohydrates, such as 1,4-β-mannotriose. In this study we investigated the influence of TconTS3-LD on Sia transfer efficiency of TconTS1a-CD by swapping domains. in silico analysis on structure models of TconTS enzymes revealed the potential of domain swaps between TconTS1a and TconTS3 without structural disruptions of the enzymes overall topologies. Recombinant domain swapped TconTS1a/TS3 showed clear Sia transfer activity, when using fetuin and lactose as Sia donor and acceptor substrates, respectively. While Sia transfer activity remained unchanged from the level of TconTS1a, hydrolytic release of free Neu5Ac as a side product was suppressed resulting in increased transfer efficiency. Presence of 1,4-β-mannotriose during TS reactions modulates enzyme activities enhancing transfer efficiency possibly due to occupation of the binding site in TconTS1a-LD. Interestingly this effect was in the same range as that observed when swapping TconTS1a-CD and TconTS3-LD. In summary, this study demonstrate the proof-of-principle for swapping CDs and LDs of TconTS and that TconTS3-LD influences enzymatic activity of TconTS1a-CD providing evidence that LDs play pivotal roles in modulating activities and biological functions of TconTS and possibly other TS.

Type of Medium: Online Resource

ISSN: 1935-2735

URL: Article

DOI: 10.1371/journal.pntd.0009585

DOI: 10.1371/journal.pntd.0009585.g001

DOI: 10.1371/journal.pntd.0009585.g002

DOI: 10.1371/journal.pntd.0009585.g003

DOI: 10.1371/journal.pntd.0009585.g004

DOI: 10.1371/journal.pntd.0009585.g005

DOI: 10.1371/journal.pntd.0009585.t001

DOI: 10.1371/journal.pntd.0009585.t002

DOI: 10.1371/journal.pntd.0009585.t003

DOI: 10.1371/journal.pntd.0009585.t004

DOI: 10.1371/journal.pntd.0009585.t005

DOI: 10.1371/journal.pntd.0009585.s001

DOI: 10.1371/journal.pntd.0009585.s002

DOI: 10.1371/journal.pntd.0009585.s003

DOI: 10.1371/journal.pntd.0009585.s004

DOI: 10.1371/journal.pntd.0009585.s005

DOI: 10.1371/journal.pntd.0009585.s006

DOI: 10.1371/journal.pntd.0009585.s007

DOI: 10.1371/journal.pntd.0009585.s008

DOI: 10.1371/journal.pntd.0009585.r001

DOI: 10.1371/journal.pntd.0009585.r002

DOI: 10.1371/journal.pntd.0009585.r003

DOI: 10.1371/journal.pntd.0009585.r004

Language: English

Publisher: Public Library of Science (PLoS)

Publication Date: 2022

detail.hit.zdb_id: 2429704-5

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Image_4.tif

Mauthe, Mario ; Dinesh Kumar, Nilima ; Verlhac, Pauline ; [et al.]

Frontiers Media SA ; 2021

In: Frontiers in Cellular and Infection Microbiology Vol. 11 ( 2021-11-15)

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In: Frontiers in Cellular and Infection Microbiology, Frontiers Media SA, Vol. 11 ( 2021-11-15)

Abstract: ATG13 and FIP200 are two subunits of the ULK kinase complex, a key regulatory component of the autophagy machinery. We have previously found that the FIP200-ATG13 subcomplex controls picornavirus replication outside its role in the ULK kinase complex and autophagy. Here, we characterized HSBP1, a very small cytoplasmic coiled-coil protein, as a novel interactor of FIP200 and ATG13 that binds these two proteins via FIP200. HSBP1 is a novel pro-picornaviral host factor since its knockdown or knockout, inhibits the replication of various picornaviruses. The anti-picornaviral function of the FIP200-ATG13 subcomplex was abolished when HSBP1 was depleted, inferring that this subcomplex negatively regulates HSBP1’s pro-picornaviral function during infections. HSBP1depletion also reduces the stability of ULK kinase complex subunits, resulting in an impairment in autophagy induction. Altogether, our data show that HSBP1 interaction with FIP200-ATG13-containing complexes is involved in the regulation of different cellular pathways.

Type of Medium: Online Resource

ISSN: 2235-2988

URL: Article

DOI: 10.3389/fcimb.2021.745640

DOI: 10.3389/fcimb.2021.745640.s001

DOI: 10.3389/fcimb.2021.745640.s002

DOI: 10.3389/fcimb.2021.745640.s003

DOI: 10.3389/fcimb.2021.745640.s004

Language: Unknown

Publisher: Frontiers Media SA

Publication Date: 2021

detail.hit.zdb_id: 2619676-1

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Correction: N-glycosylation modulates enzymatic activity of Trypanosoma congolense trans-sialidase

Rosenau, Jana ; Grothaus, Isabell Louise ; Yang, Yikun ; [et al.]

Elsevier BV ; 2023

In: Journal of Biological Chemistry Vol. 299, No. 6 ( 2023-06), p. 104875-

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In: Journal of Biological Chemistry, Elsevier BV, Vol. 299, No. 6 ( 2023-06), p. 104875-

Type of Medium: Online Resource

ISSN: 0021-9258

URL: Article

DOI: 10.1016/j.jbc.2023.104875

Language: English

Publisher: Elsevier BV

Publication Date: 2023

detail.hit.zdb_id: 2141744-1

detail.hit.zdb_id: 1474604-9

SSG: 12

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N-glycosylation modulates enzymatic activity of Trypanosoma congolense trans-sialidase

Rosenau, Jana ; Grothaus, Isabell Louise ; Yang, Yikun ; [et al.]

Elsevier BV ; 2022

In: Journal of Biological Chemistry Vol. 298, No. 10 ( 2022-10), p. 102403-

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In: Journal of Biological Chemistry, Elsevier BV, Vol. 298, No. 10 ( 2022-10), p. 102403-

Type of Medium: Online Resource

ISSN: 0021-9258

URL: Article

DOI: 10.1016/j.jbc.2022.102403

Language: English

Publisher: Elsevier BV

Publication Date: 2022

detail.hit.zdb_id: 2141744-1

detail.hit.zdb_id: 1474604-9

SSG: 12

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How Viruses Hijack and Modify the Secretory Transport Pathway

Hassan, Zubaida ; Kumar, Nilima Dinesh ; Reggiori, Fulvio ; [et al.]

MDPI AG ; 2021

In: Cells Vol. 10, No. 10 ( 2021-09-24), p. 2535-

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In: Cells, MDPI AG, Vol. 10, No. 10 ( 2021-09-24), p. 2535-

Abstract: Eukaryotic cells contain dynamic membrane-bound organelles that are constantly remodeled in response to physiological and environmental cues. Key organelles are the endoplasmic reticulum, the Golgi apparatus and the plasma membrane, which are interconnected by vesicular traffic through the secretory transport route. Numerous viruses, especially enveloped viruses, use and modify compartments of the secretory pathway to promote their replication, assembly and cell egression by hijacking the host cell machinery. In some cases, the subversion mechanism has been uncovered. In this review, we summarize our current understanding of how the secretory pathway is subverted and exploited by viruses belonging to Picornaviridae, Coronaviridae, Flaviviridae, Poxviridae, Parvoviridae and Herpesviridae families.

Type of Medium: Online Resource

ISSN: 2073-4409

URL: Article

DOI: 10.3390/cells10102535

Language: English

Publisher: MDPI AG

Publication Date: 2021

detail.hit.zdb_id: 2661518-6

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Manipulation of selective macroautophagy by pathogens at a glance

Cong, Yingying ; Dinesh Kumar, Nilima ; Mauthe, Mario ; [et al.]

The Company of Biologists ; 2020

In: Journal of Cell Science Vol. 133, No. 10 ( 2020-05-15)

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In: Journal of Cell Science, The Company of Biologists, Vol. 133, No. 10 ( 2020-05-15)

Abstract: Macroautophagy (hereafter autophagy) is a highly conserved catabolic pathway, which mediates the delivery of unwanted cytoplasmic structures and organelles to lysosomes for degradation. In numerous situations, autophagy is highly selective and exclusively targets specific intracellular components. Selective types of autophagy are a central element of our cell-autonomous innate immunity as they can mediate the turnover of viruses or bacteria, that gain access to the cytoplasm of the cell. Selective autophagy also modulates other aspects of our immunity by turning over specific immunoregulators. Throughout evolution, however, the continuous interaction between this fundamental cellular pathway and pathogens has led several pathogens to develop exquisite mechanisms to inhibit or subvert selective types of autophagy, to promote their intracellular multiplication. This Cell Science at a Glance article and the accompanying poster provides an overview of the selective autophagy of both pathogens, known as xenophagy, and of immunoregulators, and highlights a few archetypal examples that illustrate molecular strategies developed by viruses and bacteria to manipulate selective autophagy for their own benefit.

Type of Medium: Online Resource

ISSN: 1477-9137 , 0021-9533

URL: Article

DOI: 10.1242/jcs.240440

Language: English

Publisher: The Company of Biologists

Publication Date: 2020

detail.hit.zdb_id: 219171-4

detail.hit.zdb_id: 1483099-1

SSG: 12

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