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Article ; Online: The Indirect Antiviral Potential of Long Noncoding RNAs Encoded by IFITM Pseudogenes.

Rahman, Kazi / Compton, Alex A

2021 Volume 95, Issue 21, Page(s) e0068021

Abstract: The interferon-induced transmembrane ( ...

Abstract	The interferon-induced transmembrane (
MeSH term(s)	Antigens, Differentiation/metabolism ; Antiviral Agents/immunology ; Antiviral Agents/pharmacology ; Gene Expression Regulation ; Gene Knockdown Techniques ; Humans ; Influenza A virus/drug effects ; Influenza A virus/immunology ; Influenza A virus/metabolism ; Influenza, Human/immunology ; Influenza, Human/virology ; Interferons/immunology ; Membrane Proteins/immunology ; Membrane Proteins/metabolism ; Pseudogenes ; RNA, Long Noncoding/genetics ; RNA, Long Noncoding/immunology ; RNA, Long Noncoding/pharmacology ; RNA, Messenger/metabolism ; RNA-Binding Proteins/metabolism ; Virus Internalization
Chemical Substances	Antigens, Differentiation ; Antiviral Agents ; IFITM2 protein, human ; IFITM3 protein, human ; Membrane Proteins ; RNA, Long Noncoding ; RNA, Messenger ; RNA-Binding Proteins ; leu-13 antigen ; Interferons (9008-11-1)
Language	English
Publishing date	2021-07-28
Publishing country	United States
Document type	Journal Article
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.00680-21
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Article ; Online: Lessons in self-defence: inhibition of virus entry by intrinsic immunity.

Majdoul, Saliha / Compton, Alex A

Nature reviews. Immunology

2021 Volume 22, Issue 6, Page(s) 339–352

Abstract: Virus entry, consisting of attachment to and penetration into the host target cell, is the first step of the virus life cycle and is a critical 'do or die' event that governs virus emergence in host populations. Most antiviral vaccines induce ... ...

Abstract	Virus entry, consisting of attachment to and penetration into the host target cell, is the first step of the virus life cycle and is a critical 'do or die' event that governs virus emergence in host populations. Most antiviral vaccines induce neutralizing antibodies that prevent virus entry into cells. However, while the prevention of virus invasion by humoral immunity is well appreciated, considerably less is known about the immune defences present within cells (known as intrinsic immunity) that interfere with virus entry. The interferon-induced transmembrane (IFITM) proteins, known for inhibiting fusion between viral and cellular membranes, were once the only factors known to restrict virus entry. However, the progressive development of genetic and pharmacological screening platforms and the onset of the COVID-19 pandemic have galvanized interest in how viruses infiltrate cells and how cells defend against it. Several host factors with antiviral potential are now implicated in the regulation of virus entry, including cholesterol 25-hydroxylase (CH25H), lymphocyte antigen 6E (LY6E), nuclear receptor co-activator protein 7 (NCOA7), interferon-γ-inducible lysosomal thiol reductase (GILT), CD74 and ARFGAP with dual pleckstrin homology domain-containing protein 2 (ADAP2). This Review summarizes what is known and what remains to be understood about the intrinsic factors that form the first line of defence against virus infection.
MeSH term(s)	Antiviral Agents ; COVID-19 ; Humans ; Interferons ; Membrane Proteins/metabolism ; Pandemics ; Virus Internalization
Chemical Substances	Antiviral Agents ; Membrane Proteins ; Interferons (9008-11-1)
Language	English
Publishing date	2021-10-13
Publishing country	England
Document type	Journal Article ; Review ; Research Support, N.I.H., Intramural
ZDB-ID	2062776-2
ISSN	1474-1741 ; 1474-1733
ISSN (online)	1474-1741
ISSN	1474-1733
DOI	10.1038/s41577-021-00626-8
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Zs.A 5565: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Omicron Spike confers enhanced infectivity and interferon resistance to SARS-CoV-2 in human nasal tissue.

Shi, Guoli / Li, Tiansheng / Lai, Kin Kui / Johnson, Reed F / Yewdell, Jonathan W / Compton, Alex A

Nature communications

2024 Volume 15, Issue 1, Page(s) 889

Abstract: Omicron emerged following COVID-19 vaccination campaigns, displaced previous SARS-CoV-2 variants of concern worldwide, and gave rise to lineages that continue to spread. Here, we show that Omicron exhibits increased infectivity in primary adult upper ... ...

Abstract	Omicron emerged following COVID-19 vaccination campaigns, displaced previous SARS-CoV-2 variants of concern worldwide, and gave rise to lineages that continue to spread. Here, we show that Omicron exhibits increased infectivity in primary adult upper airway tissue relative to Delta. Using recombinant forms of SARS-CoV-2 and nasal epithelial cells cultured at the liquid-air interface, we show that mutations unique to Omicron Spike enable enhanced entry into nasal tissue. Unlike earlier variants of SARS-CoV-2, our findings suggest that Omicron enters nasal cells independently of serine transmembrane proteases and instead relies upon metalloproteinases to catalyze membrane fusion. Furthermore, we demonstrate that this entry pathway unlocked by Omicron Spike enables evasion from constitutive and interferon-induced antiviral factors that restrict SARS-CoV-2 entry following attachment. Therefore, the increased transmissibility exhibited by Omicron in humans may be attributed not only to its evasion of vaccine-elicited adaptive immunity, but also to its superior invasion of nasal epithelia and resistance to the cell-intrinsic barriers present therein.
MeSH term(s)	Adult ; Humans ; Interferons ; SARS-CoV-2/genetics ; COVID-19 Vaccines ; COVID-19 ; Nasal Mucosa ; Serine Endopeptidases/genetics ; Serine Proteases ; Spike Glycoprotein, Coronavirus/genetics
Chemical Substances	Interferons (9008-11-1) ; COVID-19 Vaccines ; Serine Endopeptidases (EC 3.4.21.-) ; Serine Proteases (EC 3.4.-) ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2
Language	English
Publishing date	2024-01-30
Publishing country	England
Document type	Journal Article
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-024-45075-8
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Omicron Spike confers enhanced infectivity and interferon resistance to SARS-CoV-2 in human nasal tissue.

Shi, Guoli / Li, Tiansheng / Lai, Kin Kui / Johnson, Reed F / Yewdell, Jonathan W / Compton, Alex A

bioRxiv : the preprint server for biology

2023

Abstract	Omicron emerged following COVID-19 vaccination campaigns, displaced previous SARS-CoV-2 variants of concern worldwide, and gave rise to lineages that continue to spread. Here, we show that Omicron exhibits increased infectivity in primary adult upper airway tissue relative to Delta. Using recombinant forms of SARS-CoV-2 and nasal epithelial cells cultured at the liquid-air interface, enhanced infectivity maps to the step of cellular entry and evolved recently through mutations unique to Omicron Spike. Unlike earlier variants of SARS-CoV-2, Omicron enters nasal cells independently of serine transmembrane proteases and instead relies upon metalloproteinases to catalyze membrane fusion. This entry pathway unlocked by Omicron Spike enables evasion of constitutive and interferon-induced antiviral factors that restrict SARS-CoV-2 entry following attachment. Therefore, the increased transmissibility exhibited by Omicron in humans may be attributed not only to its evasion of vaccine-elicited adaptive immunity, but also to its superior invasion of nasal epithelia and resistance to the cell-intrinsic barriers present therein.
Language	English
Publishing date	2023-10-12
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.05.06.539698
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: CD225 Proteins: A Family Portrait of Fusion Regulators.

Coomer, Charles A / Rahman, Kazi / Compton, Alex A

Trends in genetics : TIG

2021 Volume 37, Issue 5, Page(s) 406–410

Abstract: The CD225 superfamily regulates vesicular membrane fusion events essential to neurotransmission, immunity, development, and metabolism. Its importance to physiology is reinforced by the identification of polymorphisms associated with disease. This ... ...

Abstract	The CD225 superfamily regulates vesicular membrane fusion events essential to neurotransmission, immunity, development, and metabolism. Its importance to physiology is reinforced by the identification of polymorphisms associated with disease. This article highlights the shared features that drive the function of CD225 proteins such as interferon-inducible transmembrane proteins 3 (IFITM3) and proline-rich transmembrane protein 2 (PRRT2) and is intended to catalyze efforts towards characterizing the lesser-known family members.
MeSH term(s)	Animals ; Antigens, Differentiation/chemistry ; Antigens, Differentiation/genetics ; Antigens, Differentiation/metabolism ; Exocytosis/physiology ; Host-Pathogen Interactions/immunology ; Humans ; Membrane Fusion/physiology ; Membrane Proteins/genetics ; Membrane Proteins/immunology ; Membrane Proteins/metabolism ; Multigene Family ; Nerve Tissue Proteins/metabolism ; Virus Internalization
Chemical Substances	Antigens, Differentiation ; Membrane Proteins ; Nerve Tissue Proteins ; PRRT2 protein, human ; fragilis protein, mouse ; leu-13 antigen
Language	English
Publishing date	2021-01-29
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	619240-3
ISSN	1362-4555 ; 0168-9525 ; 0168-9479
ISSN (online)	1362-4555
ISSN	0168-9525 ; 0168-9479
DOI	10.1016/j.tig.2021.01.004
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Zs.A 2272: Show issues

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Article ; Online: Restriction of Influenza A Virus by SERINC5.

Lai, Kin Kui / Munro, James B / Shi, Guoli / Majdoul, Saliha / Compton, Alex A / Rein, Alan

mBio

2022 Volume 13, Issue 6, Page(s) e0292322

Abstract: Serine incorporator 5 (Ser5), a transmembrane protein, has recently been identified as a host antiviral factor against human immunodeficiency virus (HIV)-1 and gammaretroviruses like murine leukemia viruses (MLVs). It is counteracted by HIV-1 Nef and MLV ...

Abstract	Serine incorporator 5 (Ser5), a transmembrane protein, has recently been identified as a host antiviral factor against human immunodeficiency virus (HIV)-1 and gammaretroviruses like murine leukemia viruses (MLVs). It is counteracted by HIV-1 Nef and MLV glycogag. We have investigated whether it has antiviral activity against influenza A virus (IAV), as well as retroviruses. Here, we demonstrated that Ser5 inhibited HIV-1-based pseudovirions bearing IAV hemagglutinin (HA); as expected, the Ser5 effect on this glycoprotein was antagonized by HIV-1 Nef protein. We found that Ser5 inhibited the virus-cell and cell-cell fusion of IAV, apparently by interacting with HA proteins. Most importantly, overexpressed and endogenous Ser5 inhibited infection by authentic IAV. Single-molecular fluorescent resonance energy transfer (smFRET) analysis further revealed that Ser5 both destabilized the pre-fusion conformation of IAV HA and inhibited the coiled-coil formation during membrane fusion. Ser5 is expressed in cultured small airway epithelial cells, as well as in immortal human cell lines. In summary, Ser5 is a host antiviral factor against IAV which acts by blocking HA-induced membrane fusion.
MeSH term(s)	Animals ; Mice ; Humans ; Influenza A virus ; Hemagglutinins ; Membrane Proteins/metabolism ; Leukemia Virus, Murine ; Cell Line
Chemical Substances	Hemagglutinins ; Membrane Proteins ; SERINC5 protein, human
Language	English
Publishing date	2022-11-21
Publishing country	United States
Document type	Journal Article
ZDB-ID	2557172-2
ISSN	2150-7511 ; 2161-2129
ISSN (online)	2150-7511
ISSN	2161-2129
DOI	10.1128/mbio.02923-22
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: They Might Be Giants: Does Syncytium Formation Sink or Spread HIV Infection?

Compton, Alex A / Schwartz, Olivier

PLoS pathogens

2017 Volume 13, Issue 2, Page(s) e1006099

MeSH term(s)	Animals ; Giant Cells/virology ; HIV/physiology ; HIV Infections/virology ; Humans
Language	English
Publishing date	2017-02-02
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7366
ISSN (online)	1553-7374
ISSN	1553-7366
DOI	10.1371/journal.ppat.1006099
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Article ; Online: Cholesterol Binds the Amphipathic Helix of IFITM3 and Regulates Antiviral Activity

Rahman, Kazi / Datta, Siddhartha A.K. / Beaven, Andrew H. / Jolley, Abigail A. / Sodt, Alexander J. / Compton, Alex A.

Journal of Molecular Biology. 2022 Oct., v. 434, no. 19 p.167759-

2022

Abstract: The interferon-induced transmembrane (IFITM) proteins broadly inhibit the entry of diverse pathogenic viruses, including Influenza A virus (IAV), Zika virus, HIV-1, and SARS coronaviruses by inhibiting virus-cell membrane fusion. IFITM3 was previously ... ...

Abstract	The interferon-induced transmembrane (IFITM) proteins broadly inhibit the entry of diverse pathogenic viruses, including Influenza A virus (IAV), Zika virus, HIV-1, and SARS coronaviruses by inhibiting virus-cell membrane fusion. IFITM3 was previously shown to disrupt cholesterol trafficking, but the functional relationship between IFITM3 and cholesterol remains unclear. We previously showed that inhibition of IAV entry by IFITM3 is associated with its ability to promote cellular membrane rigidity, and these activities are functionally linked by a shared requirement for the amphipathic helix (AH) found in the intramembrane domain (IMD) of IFITM3. Furthermore, it has been shown that the AH of IFITM3 alters lipid membranes in vitro in a cholesterol-dependent manner. Therefore, we aimed to elucidate the relationship between IFITM3 and cholesterol in more detail. Using a fluorescence-based in vitro binding assay, we found that a peptide derived from the AH of IFITM3 directly interacted with the cholesterol analog, NBD-cholesterol, while other regions of the IFITM3 IMD did not, and native cholesterol competed with this interaction. In addition, recombinant full-length IFITM3 protein also exhibited NBD-cholesterol binding activity. Importantly, previously characterized mutations within the AH of IFITM3 that strongly inhibit antiviral function (F63Q and F67Q) disrupted AH structure in solution, inhibited cholesterol binding in vitro, and restricted bilayer insertion in silico. Our data suggest that direct interactions with cholesterol may contribute to the inhibition of membrane fusion pore formation by IFITM3. These findings may facilitate the design of therapeutic peptides for use in broad-spectrum antiviral therapy.
Keywords	Influenza A virus ; Severe acute respiratory syndrome-related coronavirus ; Zika virus ; antiviral properties ; cell membranes ; cholesterol ; computer simulation ; membrane fusion ; molecular biology ; peptides ; surfactants ; therapeutics ; interferon ; IFITM ; virus ; fusion
Language	English
Dates of publication	2022-10
Publishing place	Elsevier Ltd
Document type	Article ; Online
Note	Use and reproduction
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2022.167759
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Omicron Spike confers enhanced infectivity and interferon resistance to SARS-CoV-2 in human nasal tissue

Shi, Guoli / Li, Tiansheng / Lai, Kin Kui / Yewdell, Jonathan W / Compton, Alex A

bioRxiv

Abstract	Omicron emerged following COVID-19 vaccination campaigns, displaced previous SARS-CoV-2 variants of concern worldwide, and gave rise to lineages that continue to spread. Here, we show that Omicron exhibits increased infectivity in primary adult upper airway tissue. Using recombinant forms of SARS-CoV-2 and nasal epithelial cells cultured at the liquid-air interface, enhanced infectivity maps to the step of cellular entry and evolved recently through mutations unique to Omicron Spike. Unlike earlier variants of SARS-CoV-2, Omicron enters nasal cells independently of serine transmembrane proteases and instead relies upon matrix metalloproteinases to catalyze membrane fusion. This entry pathway unlocked by Omicron Spike enables evasion of interferon-induced factors that restrict SARS-CoV-2 entry following attachment. Therefore, the increased transmissibility exhibited by Omicron in humans may be attributed not only to its evasion of vaccine-elicited adaptive immunity, but also to its superior invasion of nasal epithelia and resistance to the cell-intrinsic barriers present therein.
Keywords	covid19
Language	English
Publishing date	2023-05-08
Publisher	Cold Spring Harbor Laboratory
Document type	Article ; Online
DOI	10.1101/2023.05.06.539698
Database	COVID19

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Article ; Online: Cholesterol Binds the Amphipathic Helix of IFITM3 and Regulates Antiviral Activity.

Rahman, Kazi / Datta, Siddhartha A K / Beaven, Andrew H / Jolley, Abigail A / Sodt, Alexander J / Compton, Alex A

Journal of molecular biology

2022 Volume 434, Issue 19, Page(s) 167759

Abstract	The interferon-induced transmembrane (IFITM) proteins broadly inhibit the entry of diverse pathogenic viruses, including Influenza A virus (IAV), Zika virus, HIV-1, and SARS coronaviruses by inhibiting virus-cell membrane fusion. IFITM3 was previously shown to disrupt cholesterol trafficking, but the functional relationship between IFITM3 and cholesterol remains unclear. We previously showed that inhibition of IAV entry by IFITM3 is associated with its ability to promote cellular membrane rigidity, and these activities are functionally linked by a shared requirement for the amphipathic helix (AH) found in the intramembrane domain (IMD) of IFITM3. Furthermore, it has been shown that the AH of IFITM3 alters lipid membranes in vitro in a cholesterol-dependent manner. Therefore, we aimed to elucidate the relationship between IFITM3 and cholesterol in more detail. Using a fluorescence-based in vitro binding assay, we found that a peptide derived from the AH of IFITM3 directly interacted with the cholesterol analog, NBD-cholesterol, while other regions of the IFITM3 IMD did not, and native cholesterol competed with this interaction. In addition, recombinant full-length IFITM3 protein also exhibited NBD-cholesterol binding activity. Importantly, previously characterized mutations within the AH of IFITM3 that strongly inhibit antiviral function (F63Q and F67Q) disrupted AH structure in solution, inhibited cholesterol binding in vitro, and restricted bilayer insertion in silico. Our data suggest that direct interactions with cholesterol may contribute to the inhibition of membrane fusion pore formation by IFITM3. These findings may facilitate the design of therapeutic peptides for use in broad-spectrum antiviral therapy.
MeSH term(s)	Cholesterol/chemistry ; Humans ; Influenza A virus/immunology ; Membrane Proteins/chemistry ; Protein Conformation, alpha-Helical ; RNA-Binding Proteins/chemistry ; Virus Internalization ; Zika Virus/immunology
Chemical Substances	IFITM3 protein, human ; Membrane Proteins ; RNA-Binding Proteins ; Cholesterol (97C5T2UQ7J)
Language	English
Publishing date	2022-07-21
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2022.167759
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