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Article ; Online: Author Correction: MX2-mediated innate immunity against HIV-1 is regulated by serine phosphorylation.

Betancor, Gilberto / Jimenez-Guardeño, Jose M / Lynham, Steven / Antrobus, Robin / Khan, Hataf / Sobala, Andrew / Dicks, Matthew D J / Malim, Michael H

Nature microbiology

2021 Volume 6, Issue 9, Page(s) 1211

Language	English
Publishing date	2021-08-13
Publishing country	England
Document type	Published Erratum
ISSN	2058-5276
ISSN (online)	2058-5276
DOI	10.1038/s41564-021-00960-6
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: MX2-mediated innate immunity against HIV-1 is regulated by serine phosphorylation.

Betancor, Gilberto / Jimenez-Guardeño, Jose M / Lynham, Steven / Antrobus, Robin / Khan, Hataf / Sobala, Andrew / Dicks, Matthew D J / Malim, Michael H

Nature microbiology

2021 Volume 6, Issue 8, Page(s) 1031–1042

Abstract: The antiviral cytokine interferon activates expression of interferon-stimulated genes to establish an antiviral state. Myxovirus resistance 2 (MX2, also known as MxB) is an interferon-stimulated gene that inhibits the nuclear import of HIV-1 and ... ...

Abstract	The antiviral cytokine interferon activates expression of interferon-stimulated genes to establish an antiviral state. Myxovirus resistance 2 (MX2, also known as MxB) is an interferon-stimulated gene that inhibits the nuclear import of HIV-1 and interacts with the viral capsid and cellular nuclear transport machinery. Here, we identified the myosin light chain phosphatase (MLCP) subunits myosin phosphatase target subunit 1 (MYPT1) and protein phosphatase 1 catalytic subunit-β (PPP1CB) as positively-acting regulators of MX2, interacting with its amino-terminal domain. We demonstrated that serine phosphorylation of the N-terminal domain at positions 14, 17 and 18 suppresses MX2 antiviral function, prevents interactions with the HIV-1 capsid and nuclear transport factors, and is reversed by MLCP. Notably, serine phosphorylation of the N-terminal domain also impedes MX2-mediated inhibition of nuclear import of cellular karyophilic cargo. We also found that interferon treatment reduces levels of phosphorylation at these serine residues and outline a homeostatic regulatory mechanism in which repression of MX2 by phosphorylation, together with MLCP-mediated dephosphorylation, balances the deleterious effects of MX2 on normal cell function with innate immunity against HIV-1.
MeSH term(s)	Amino Acid Motifs ; HIV Infections/genetics ; HIV Infections/immunology ; HIV Infections/virology ; HIV-1/genetics ; HIV-1/immunology ; HIV-1/physiology ; HeLa Cells ; Humans ; Immunity, Innate ; Myosin-Light-Chain Phosphatase/genetics ; Myosin-Light-Chain Phosphatase/immunology ; Myosin-Light-Chain Phosphatase/metabolism ; Myxovirus Resistance Proteins/chemistry ; Myxovirus Resistance Proteins/genetics ; Myxovirus Resistance Proteins/immunology ; Phosphorylation ; Protein Domains ; Protein Phosphatase 1/genetics ; Protein Phosphatase 1/immunology ; Serine/metabolism
Chemical Substances	MX2 protein, human ; Myxovirus Resistance Proteins ; Serine (452VLY9402) ; PPP1CB protein, human (EC 3.1.3.16) ; Protein Phosphatase 1 (EC 3.1.3.16) ; Myosin-Light-Chain Phosphatase (EC 3.1.3.53) ; PPP1R12A protein, human (EC 3.1.3.53)
Language	English
Publishing date	2021-07-19
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	2058-5276
ISSN (online)	2058-5276
DOI	10.1038/s41564-021-00937-5
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: A neutralizing epitope on the SD1 domain of SARS-CoV-2 spike targeted following infection and vaccination.

Seow, Jeffrey / Khan, Hataf / Rosa, Annachiara / Calvaresi, Valeria / Graham, Carl / Pickering, Suzanne / Pye, Valerie E / Cronin, Nora B / Huettner, Isabella / Malim, Michael H / Politis, Argyris / Cherepanov, Peter / Doores, Katie J

Cell reports

2022 Volume 40, Issue 8, Page(s) 111276

Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike is the target for neutralizing antibodies elicited following both infection and vaccination. While extensive research has shown that the receptor binding domain (RBD) and, to a lesser ... ...

Abstract	Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike is the target for neutralizing antibodies elicited following both infection and vaccination. While extensive research has shown that the receptor binding domain (RBD) and, to a lesser extent, the N-terminal domain (NTD) are the predominant targets for neutralizing antibodies, identification of neutralizing epitopes beyond these regions is important for informing vaccine development and understanding antibody-mediated immune escape. Here, we identify a class of broadly neutralizing antibodies that bind an epitope on the spike subdomain 1 (SD1) and that have arisen from infection or vaccination. Using cryo-electron microscopy (cryo-EM) and hydrogen-deuterium exchange coupled to mass spectrometry (HDX-MS), we show that SD1-specific antibody P008_60 binds an epitope that is not accessible within the canonical prefusion states of the SARS-CoV-2 spike, suggesting a transient conformation of the viral glycoprotein that is vulnerable to neutralization.
MeSH term(s)	Antibodies, Neutralizing ; Antibodies, Viral ; COVID-19 ; Cryoelectron Microscopy ; Epitopes ; Humans ; Neutralization Tests ; SARS-CoV-2 ; Spike Glycoprotein, Coronavirus ; Syndactyly ; Vaccination
Chemical Substances	Antibodies, Neutralizing ; Antibodies, Viral ; Epitopes ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2
Language	English
Publishing date	2022-08-11
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2022.111276
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Impaired humoral and T cell response to vaccination against SARS-CoV-2 in chronic myeloproliferative neoplasm patients treated with ruxolitinib.

Blood cancer journal

2022 Volume 12, Issue 4, Page(s) 73

MeSH term(s)	COVID-19/prevention & control ; Humans ; Neoplasms ; Nitriles ; Pyrazoles ; Pyrimidines ; SARS-CoV-2 ; T-Lymphocytes ; Vaccination
Chemical Substances	Nitriles ; Pyrazoles ; Pyrimidines ; ruxolitinib (82S8X8XX8H)
Language	English
Publishing date	2022-04-22
Publishing country	United States
Document type	Letter ; Research Support, Non-U.S. Gov't
ZDB-ID	2600560-8
ISSN	2044-5385 ; 2044-5385
ISSN (online)	2044-5385
ISSN	2044-5385
DOI	10.1038/s41408-022-00651-3
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Article ; Online: Repeated vaccination against SARS-CoV-2 elicits robust polyfunctional T cell response in allogeneic stem cell transplantation recipients.

Harrington, Patrick / Doores, Katie J / Saha, Chandan / Saunders, Jamie / Child, Fiona / Dillon, Richard / Saglam, Sukran / Raj, Kavita / McLornan, Donal / Avenoso, Daniele / Kordasti, Shahram / O'Reilly, Amy / Espehana, Andreas / Lechmere, Thomas / Khan, Hataf / Malim, Michael H / Harrison, Claire / Mehra, Varun / de Lavallade, Hugues

Cancer cell

2021 Volume 39, Issue 12, Page(s) 1654

Language	English
Publishing date	2021-12-15
Publishing country	United States
Document type	Published Erratum
ZDB-ID	2078448-X
ISSN	1878-3686 ; 1535-6108
ISSN (online)	1878-3686
ISSN	1535-6108
DOI	10.1016/j.ccell.2021.11.011
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: The complement pattern recognition molecule CL-11 promotes invasion and injury of respiratory epithelial cells by SARS-CoV-2.

Polycarpou, Anastasia / Wagner-Gamble, Tara / Greenlaw, Roseanna / O'Neill, Lauren A. / Khan, Hataf / Malim, Michael M / Romano, Marco / Smolarek, Dorota / Doores, Katie J / Wallis, Russell / Klavinskis, Linda S / Sacks, Steven

bioRxiv

Abstract: Collectin-11 is a soluble C-type lectin produced at epithelial surfaces to initiate pathogen elimination by complement. Given the respiratory epithelium is a source of CL-11 and downstream complement-pathway components, we investigated the potential of ... ...

Abstract	Collectin-11 is a soluble C-type lectin produced at epithelial surfaces to initiate pathogen elimination by complement. Given the respiratory epithelium is a source of CL-11 and downstream complement-pathway components, we investigated the potential of CL-11 to impact the pathogenicity of SARS-CoV-2. While the SARS-CoV-2 spike trimer could bind CL-11 and trigger complement activation followed by MAC formation, the virus was resistant to lysis. Surprisingly, virus production by infected respiratory epithelial cells was enhanced by CL-11 opsonisation of virus but this effect was fully inhibited by sugar-blockade of CL-11. Moreover, SARS-CoV-2 spike protein expressed at the bronchial epithelial cell surface was associated with increased CL-11 binding and MAC formation. We propose that SARS-CoV-2 pathogenicity is exacerbated both by resistance to complement and CL-11 driven respiratory cell invasion and injury at the portal of entry. Contrary to expectation, CL-11 blockade could offer a novel approach to limit the pathogenicity of SARS-CoV-2.
Keywords	covid19
Language	English
Publishing date	2023-12-12
Publisher	Cold Spring Harbor Laboratory
Document type	Article ; Online
DOI	10.1101/2023.12.11.571109
Database	COVID19

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Article ; Online: ChAdOx1 nCoV-19 vaccine elicits monoclonal antibodies with cross-neutralizing activity against SARS-CoV-2 viral variants.

Seow, Jeffrey / Graham, Carl / Hallett, Sadie R / Lechmere, Thomas / Maguire, Thomas J A / Huettner, Isabella / Cox, Daniel / Khan, Hataf / Pickering, Suzanne / Roberts, Rebekah / Waters, Anele / Ward, Christopher C / Mant, Christine / Pitcher, Michael J / Spencer, Jo / Fox, Julie / Malim, Michael H / Doores, Katie J

Cell reports

2022 Volume 39, Issue 5, Page(s) 110757

Abstract: Although the antibody response to COVID-19 vaccination has been studied extensively at the polyclonal level using immune sera, little has been reported on the antibody response at the monoclonal level. Here, we isolate a panel of 44 anti-SARS-CoV-2 ... ...

Abstract	Although the antibody response to COVID-19 vaccination has been studied extensively at the polyclonal level using immune sera, little has been reported on the antibody response at the monoclonal level. Here, we isolate a panel of 44 anti-SARS-CoV-2 monoclonal antibodies (mAbs) from an individual who received two doses of the ChAdOx1 nCoV-19 (AZD1222) vaccine at a 12-week interval. We show that, despite a relatively low serum neutralization titer, Spike-reactive IgG+ B cells are still detectable 9 months post-boost. Furthermore, mAbs with potent neutralizing activity against the current SARS-CoV-2 variants of concern (Alpha, Gamma, Beta, Delta, and Omicron) are present. The vaccine-elicited neutralizing mAbs form eight distinct competition groups and bind epitopes overlapping with neutralizing mAbs elicited following SARS-CoV-2 infection. AZD1222-elicited mAbs are more mutated than mAbs isolated from convalescent donors 1-2 months post-infection. These findings provide molecular insights into the AZD1222 vaccine-elicited antibody response.
MeSH term(s)	Antibodies, Monoclonal ; Antibodies, Neutralizing ; Antibodies, Viral ; COVID-19/prevention & control ; COVID-19 Vaccines ; ChAdOx1 nCoV-19 ; Humans ; SARS-CoV-2 ; Vaccination
Chemical Substances	Antibodies, Monoclonal ; Antibodies, Neutralizing ; Antibodies, Viral ; COVID-19 Vaccines ; ChAdOx1 nCoV-19 (B5S3K2V0G8)
Language	English
Publishing date	2022-04-15
Publishing country	United States
Document type	Journal Article
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2022.110757
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: TMPRSS2 promotes SARS-CoV-2 evasion from NCOA7-mediated restriction.

Khan, Hataf / Winstone, Helena / Jimenez-Guardeño, Jose M / Graham, Carl / Doores, Katie J / Goujon, Caroline / Matthews, David A / Davidson, Andrew D / Rihn, Suzannah J / Palmarini, Massimo / Neil, Stuart J D / Malim, Michael H

PLoS pathogens

2021 Volume 17, Issue 11, Page(s) e1009820

Abstract: Interferons play a critical role in regulating host immune responses to SARS-CoV-2, but the interferon (IFN)-stimulated gene (ISG) effectors that inhibit SARS-CoV-2 are not well characterized. The IFN-inducible short isoform of human nuclear receptor ... ...

Abstract	Interferons play a critical role in regulating host immune responses to SARS-CoV-2, but the interferon (IFN)-stimulated gene (ISG) effectors that inhibit SARS-CoV-2 are not well characterized. The IFN-inducible short isoform of human nuclear receptor coactivator 7 (NCOA7) inhibits endocytic virus entry, interacts with the vacuolar ATPase, and promotes endo-lysosomal vesicle acidification and lysosomal protease activity. Here, we used ectopic expression and gene knockout to demonstrate that NCOA7 inhibits infection by SARS-CoV-2 as well as by lentivirus particles pseudotyped with SARS-CoV-2 Spike in lung epithelial cells. Infection with the highly pathogenic, SARS-CoV-1 and MERS-CoV, or seasonal, HCoV-229E and HCoV-NL63, coronavirus Spike-pseudotyped viruses was also inhibited by NCOA7. Importantly, either overexpression of TMPRSS2, which promotes plasma membrane fusion versus endosomal fusion of SARS-CoV-2, or removal of Spike's polybasic furin cleavage site rendered SARS-CoV-2 less sensitive to NCOA7 restriction. Collectively, our data indicate that furin cleavage sensitizes SARS-CoV-2 Spike to the antiviral consequences of endosomal acidification by NCOA7, and suggest that the acquisition of furin cleavage may have favoured the co-option of cell surface TMPRSS proteases as a strategy to evade the suppressive effects of IFN-induced endo-lysosomal dysregulation on virus infection.
MeSH term(s)	COVID-19/virology ; Cell Line ; Endosomes/metabolism ; Furin/genetics ; Furin/metabolism ; Gene Expression ; Humans ; Immune Evasion ; Interferons/metabolism ; Lysosomes/enzymology ; Nuclear Receptor Coactivators/genetics ; Nuclear Receptor Coactivators/metabolism ; Protein Isoforms ; Proteolysis ; SARS-CoV-2/physiology ; Serine Endopeptidases/genetics ; Serine Endopeptidases/metabolism ; Spike Glycoprotein, Coronavirus/metabolism ; Viral Pseudotyping ; Virus Internalization
Chemical Substances	NCOA7 protein, human ; Nuclear Receptor Coactivators ; Protein Isoforms ; Spike Glycoprotein, Coronavirus ; Interferons (9008-11-1) ; Serine Endopeptidases (EC 3.4.21.-) ; TMPRSS2 protein, human (EC 3.4.21.-) ; FURIN protein, human (EC 3.4.21.75) ; Furin (EC 3.4.21.75)
Language	English
Publishing date	2021-11-22
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7374
ISSN (online)	1553-7374
ISSN	1553-7374
DOI	10.1371/journal.ppat.1009820
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: ChAdOx1 nCoV-19 vaccine elicits monoclonal antibodies with cross-neutralizing activity against SARS-CoV-2 viral variants

Jeffrey Seow / Carl Graham / Sadie R. Hallett / Thomas Lechmere / Thomas J.A. Maguire / Isabella Huettner / Daniel Cox / Hataf Khan / Suzanne Pickering / Rebekah Roberts / Anele Waters / Christopher C. Ward / Christine Mant / Michael J. Pitcher / Jo Spencer / Julie Fox / Michael H. Malim / Katie J. Doores

Cell Reports, Vol 39, Iss 5, Pp 110757- (2022)

2022

Abstract: Summary: Although the antibody response to COVID-19 vaccination has been studied extensively at the polyclonal level using immune sera, little has been reported on the antibody response at the monoclonal level. Here, we isolate a panel of 44 anti-SARS- ... ...

Abstract	Summary: Although the antibody response to COVID-19 vaccination has been studied extensively at the polyclonal level using immune sera, little has been reported on the antibody response at the monoclonal level. Here, we isolate a panel of 44 anti-SARS-CoV-2 monoclonal antibodies (mAbs) from an individual who received two doses of the ChAdOx1 nCoV-19 (AZD1222) vaccine at a 12-week interval. We show that, despite a relatively low serum neutralization titer, Spike-reactive IgG+ B cells are still detectable 9 months post-boost. Furthermore, mAbs with potent neutralizing activity against the current SARS-CoV-2 variants of concern (Alpha, Gamma, Beta, Delta, and Omicron) are present. The vaccine-elicited neutralizing mAbs form eight distinct competition groups and bind epitopes overlapping with neutralizing mAbs elicited following SARS-CoV-2 infection. AZD1222-elicited mAbs are more mutated than mAbs isolated from convalescent donors 1–2 months post-infection. These findings provide molecular insights into the AZD1222 vaccine-elicited antibody response.
Keywords	CP: Immunology ; Biology (General) ; QH301-705.5
Subject code	570
Language	English
Publishing date	2022-05-01T00:00:00Z
Publisher	Elsevier
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: TMPRSS2 promotes SARS-CoV-2 evasion from NCOA7-mediated restriction.

Hataf Khan / Helena Winstone / Jose M Jimenez-Guardeño / Carl Graham / Katie J Doores / Caroline Goujon / David A Matthews / Andrew D Davidson / Suzannah J Rihn / Massimo Palmarini / Stuart J D Neil / Michael H Malim

PLoS Pathogens, Vol 17, Iss 11, p e

2021 Volume 1009820

Abstract	Interferons play a critical role in regulating host immune responses to SARS-CoV-2, but the interferon (IFN)-stimulated gene (ISG) effectors that inhibit SARS-CoV-2 are not well characterized. The IFN-inducible short isoform of human nuclear receptor coactivator 7 (NCOA7) inhibits endocytic virus entry, interacts with the vacuolar ATPase, and promotes endo-lysosomal vesicle acidification and lysosomal protease activity. Here, we used ectopic expression and gene knockout to demonstrate that NCOA7 inhibits infection by SARS-CoV-2 as well as by lentivirus particles pseudotyped with SARS-CoV-2 Spike in lung epithelial cells. Infection with the highly pathogenic, SARS-CoV-1 and MERS-CoV, or seasonal, HCoV-229E and HCoV-NL63, coronavirus Spike-pseudotyped viruses was also inhibited by NCOA7. Importantly, either overexpression of TMPRSS2, which promotes plasma membrane fusion versus endosomal fusion of SARS-CoV-2, or removal of Spike's polybasic furin cleavage site rendered SARS-CoV-2 less sensitive to NCOA7 restriction. Collectively, our data indicate that furin cleavage sensitizes SARS-CoV-2 Spike to the antiviral consequences of endosomal acidification by NCOA7, and suggest that the acquisition of furin cleavage may have favoured the co-option of cell surface TMPRSS proteases as a strategy to evade the suppressive effects of IFN-induced endo-lysosomal dysregulation on virus infection.
Keywords	Immunologic diseases. Allergy ; RC581-607 ; Biology (General) ; QH301-705.5
Subject code	570 ; 572
Language	English
Publishing date	2021-11-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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