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  1. Article ; Online: Immune responses following BNT162b2 XBB.1.5 vaccination in patients on haemodialysis in Germany.

    Cossmann, Anne / Hoffmann, Markus / Stankov, Metodi V / Lürken, Karsten / Morillas Ramos, Gema / Kempf, Amy / Nehlmeier, Inga / Pöhlmann, Stefan / Behrens, Georg M N / Dopfer-Jablonka, Alexandra

    The Lancet. Infectious diseases

    2024  Volume 24, Issue 3, Page(s) e145–e146

    MeSH term(s) Humans ; BNT162 Vaccine ; Germany/epidemiology ; Renal Dialysis ; Immunity ; Vaccination ; Antibodies, Viral
    Chemical Substances BNT162 Vaccine ; Antibodies, Viral
    Language English
    Publishing date 2024-01-08
    Publishing country United States
    Document type Letter
    ZDB-ID 2061641-7
    ISSN 1474-4457 ; 1473-3099
    ISSN (online) 1474-4457
    ISSN 1473-3099
    DOI 10.1016/S1473-3099(23)00783-1
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5743: Show issues Location:
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  2. Article ; Online: Cytoskeletal β-tubulin and cysteine cathepsin L deregulation by SARS-CoV-2 spike protein interaction with the neuronal model cell line SH-SY5Y.

    Oliveira, Bernardo R / Nehlmeier, Inga / Kempf, Amy Madeleine / Venugopalan, Vaishnavi / Rehders, Maren / Ceniza, Marianne E P / Cavalcanti, Pedro A de T P V / Hoffmann, Markus / Pöhlmann, Stefan / Brix, Klaudia

    Biochimie

    2024  

    Abstract: SARS-CoV-2 mainly infects the respiratory tract but can also target other organs, including the central nervous system. While it was recently shown that cells of the blood-brain-barrier are permissive to SARS-CoV-2 infection in vitro, it remains debated ... ...

    Abstract SARS-CoV-2 mainly infects the respiratory tract but can also target other organs, including the central nervous system. While it was recently shown that cells of the blood-brain-barrier are permissive to SARS-CoV-2 infection in vitro, it remains debated whether neurons can be infected. In this study, we demonstrate that vesicular stomatitis virus particles pseudotyped with the spike protein of SARS-CoV-2 variants WT, Alpha, Delta and Omicron enter the neuronal model cell line SH-SY5Y. Cell biological analyses of the pseudo-virus treated cultures showed marked alterations in microtubules of SH-SY5Y cells. Because the changes in β-tubulin occurred in most cells, but only few were infected, we further asked whether interaction of the cells with spike protein might be sufficient to cause molecular and structural changes. For this, SH-SY5Y cells were incubated with trimeric spike proteins for time intervals of up to 24 h. CellProfiler™-based image analyses revealed changes in the intensities of microtubule staining in spike protein-incubated cells. Furthermore, expression of the spike protein-processing protease cathepsin L was found to be up-regulated by wild type, Alpha and Delta spike protein pseudotypes and cathepsin L was found to be secreted from spike protein-treated cells. We conclude that the mere interaction of the SARS-CoV-2 with neuronal cells can affect cellular architecture and proteolytic capacities. The molecular mechanisms underlying SARS-CoV-2 spike protein induced cytoskeletal changes in neuronal cells remain elusive and require future studies.
    Language English
    Publishing date 2024-03-01
    Publishing country France
    Document type Journal Article
    ZDB-ID 120345-9
    ISSN 1638-6183 ; 0300-9084
    ISSN (online) 1638-6183
    ISSN 0300-9084
    DOI 10.1016/j.biochi.2024.02.006
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  3. Article ; Online: Omicron sublineage BQ.1.1 resistance to monoclonal antibodies.

    Arora, Prerna / Kempf, Amy / Nehlmeier, Inga / Schulz, Sebastian R / Jäck, Hans-Martin / Pöhlmann, Stefan / Hoffmann, Markus

    The Lancet. Infectious diseases

    2022  Volume 23, Issue 1, Page(s) 22–23

    MeSH term(s) Humans ; Antibodies, Monoclonal/therapeutic use ; Antibodies, Viral ; Antibodies, Neutralizing
    Chemical Substances Antibodies, Monoclonal ; Antibodies, Viral ; Antibodies, Neutralizing
    Language English
    Publishing date 2022-11-18
    Publishing country United States
    Document type Letter
    ZDB-ID 2061641-7
    ISSN 1474-4457 ; 1473-3099
    ISSN (online) 1474-4457
    ISSN 1473-3099
    DOI 10.1016/S1473-3099(22)00733-2
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Effect of hybrid immunity and bivalent booster vaccination on omicron sublineage neutralisation.

    Hoffmann, Markus / Behrens, Georg M N / Arora, Prerna / Kempf, Amy / Nehlmeier, Inga / Cossmann, Anne / Manthey, Luis / Dopfer-Jablonka, Alexandra / Pöhlmann, Stefan

    The Lancet. Infectious diseases

    2022  Volume 23, Issue 1, Page(s) 25–28

    MeSH term(s) Humans ; Adaptive Immunity ; Vaccination ; Antibodies, Viral
    Chemical Substances Antibodies, Viral
    Language English
    Publishing date 2022-12-05
    Publishing country United States
    Document type Letter
    ZDB-ID 2061641-7
    ISSN 1474-4457 ; 1473-3099
    ISSN (online) 1474-4457
    ISSN 1473-3099
    DOI 10.1016/S1473-3099(22)00792-7
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  5. Article ; Online: Polyvalent Nano-Lectin Potently Neutralizes SARS-CoV-2 by Targeting Glycans on the Viral Spike Protein.

    Budhadev, Darshita / Hooper, James / Rocha, Cheila / Nehlmeier, Inga / Kempf, Amy Madeleine / Hoffmann, Markus / Krüger, Nadine / Zhou, Dejian / Pöhlmann, Stefan / Guo, Yuan

    JACS Au

    2023  Volume 3, Issue 6, Page(s) 1755–1766

    Abstract: Mutations in spike (S) protein epitopes allow SARS-CoV-2 variants to evade antibody responses induced by infection and/or vaccination. In contrast, mutations in glycosylation sites across SARS-CoV-2 variants are very rare, making glycans a potential ... ...

    Abstract Mutations in spike (S) protein epitopes allow SARS-CoV-2 variants to evade antibody responses induced by infection and/or vaccination. In contrast, mutations in glycosylation sites across SARS-CoV-2 variants are very rare, making glycans a potential robust target for developing antivirals. However, this target has not been adequately exploited for SARS-CoV-2, mostly due to intrinsically weak monovalent protein-glycan interactions. We hypothesize that polyvalent nano-lectins with flexibly linked carbohydrate recognition domains (CRDs) can adjust their relative positions and bind multivalently to S protein glycans, potentially exerting potent antiviral activity. Herein, we displayed the CRDs of DC-SIGN, a dendritic cell lectin known to bind to diverse viruses, polyvalently onto 13 nm gold nanoparticles (named G13-CRD). G13-CRD bound strongly and specifically to target glycan-coated quantum dots with sub-nM
    Language English
    Publishing date 2023-06-12
    Publishing country United States
    Document type Journal Article
    ISSN 2691-3704
    ISSN (online) 2691-3704
    DOI 10.1021/jacsau.3c00163
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: TMPRSS2 Is Essential for SARS-CoV-2 Beta and Omicron Infection.

    Metzdorf, Kristin / Jacobsen, Henning / Greweling-Pils, Marina C / Hoffmann, Markus / Lüddecke, Tatjana / Miller, Felicitas / Melcher, Lars / Kempf, Amy M / Nehlmeier, Inga / Bruder, Dunja / Widera, Marek / Ciesek, Sandra / Pöhlmann, Stefan / Čičin-Šain, Luka

    Viruses

    2023  Volume 15, Issue 2

    Abstract: The COVID-19 pandemic remains a global health threat and novel antiviral strategies are urgently needed. SARS-CoV-2 employs the cellular serine protease TMPRSS2 for entry into lung cells, and TMPRSS2 inhibitors are being developed for COVID-19 therapy. ... ...

    Abstract The COVID-19 pandemic remains a global health threat and novel antiviral strategies are urgently needed. SARS-CoV-2 employs the cellular serine protease TMPRSS2 for entry into lung cells, and TMPRSS2 inhibitors are being developed for COVID-19 therapy. However, the SARS-CoV-2 Omicron variant, which currently dominates the pandemic, prefers the endo/lysosomal cysteine protease cathepsin L over TMPRSS2 for cell entry, raising doubts as to whether TMPRSS2 inhibitors would be suitable for the treatment of patients infected with the Omicron variant. Nevertheless, the contribution of TMPRSS2 to the spread of SARS-CoV-2 in the infected host is largely unclear. In this study, we show that the loss of TMPRSS2 strongly reduced the replication of the Beta variant in the nose, trachea and lung of C57BL/6 mice, and protected the animals from weight loss and disease. The infection of mice with the Omicron variant did not cause disease, as expected, but again, TMPRSS2 was essential for efficient viral spread in the upper and lower respiratory tract. These results identify the key role of TMPRSS2 in SARS-CoV-2 Beta and Omicron infection, and highlight TMPRSS2 as an attractive target for antiviral intervention.
    MeSH term(s) Animals ; Humans ; Mice ; Antiviral Agents/pharmacology ; Antiviral Agents/therapeutic use ; COVID-19 ; Mice, Inbred C57BL ; Pandemics ; SARS-CoV-2 ; Serine Endopeptidases/genetics
    Chemical Substances Antiviral Agents ; Serine Endopeptidases (EC 3.4.21.-) ; TMPRSS2 protein, human (EC 3.4.21.-) ; TMPRSS2 protein, mouse (EC 3.4.21.-)
    Language English
    Publishing date 2023-01-18
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2516098-9
    ISSN 1999-4915 ; 1999-4915
    ISSN (online) 1999-4915
    ISSN 1999-4915
    DOI 10.3390/v15020271
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  7. Article ; Online: Host cell entry and neutralisation sensitivity of the SARS-CoV-2 XBB.1.16 lineage.

    Nehlmeier, Inga / Kempf, Amy / Arora, Prerna / Cossmann, Anne / Dopfer-Jablonka, Alexandra / Stankov, Metodi V / Schulz, Sebastian R / Jäck, Hans-Martin / Behrens, Georg M N / Pöhlmann, Stefan / Hoffmann, Markus

    Cellular & molecular immunology

    2023  Volume 20, Issue 8, Page(s) 969–971

    MeSH term(s) Humans ; COVID-19 ; SARS-CoV-2 ; Virus Internalization
    Language English
    Publishing date 2023-05-08
    Publishing country China
    Document type Letter ; Research Support, Non-U.S. Gov't
    ZDB-ID 2435097-7
    ISSN 2042-0226 ; 1672-7681
    ISSN (online) 2042-0226
    ISSN 1672-7681
    DOI 10.1038/s41423-023-01030-z
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Profound neutralization evasion and augmented host cell entry are hallmarks of the fast-spreading SARS-CoV-2 lineage XBB.1.5.

    Hoffmann, Markus / Arora, Prerna / Nehlmeier, Inga / Kempf, Amy / Cossmann, Anne / Schulz, Sebastian R / Morillas Ramos, Gema / Manthey, Luis A / Jäck, Hans-Martin / Behrens, Georg M N / Pöhlmann, Stefan

    Cellular & molecular immunology

    2023  Volume 20, Issue 4, Page(s) 419–422

    MeSH term(s) Humans ; COVID-19 ; SARS-CoV-2 ; Virus Internalization ; Antibodies, Viral ; Spike Glycoprotein, Coronavirus ; Immune Evasion ; Antibodies, Neutralizing
    Chemical Substances Antibodies, Viral ; Spike Glycoprotein, Coronavirus ; Antibodies, Neutralizing ; spike protein, SARS-CoV-2
    Language English
    Publishing date 2023-03-03
    Publishing country China
    Document type Letter ; Research Support, Non-U.S. Gov't
    ZDB-ID 2435097-7
    ISSN 2042-0226 ; 1672-7681
    ISSN (online) 2042-0226
    ISSN 1672-7681
    DOI 10.1038/s41423-023-00988-0
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  9. Article ; Online: Neutralisation sensitivity of SARS-CoV-2 lineages EG.5.1 and XBB.2.3.

    Zhang, Lu / Kempf, Amy / Nehlmeier, Inga / Cossmann, Anne / Dopfer-Jablonka, Alexandra / Stankov, Metodi V / Schulz, Sebastian R / Jäck, Hans-Martin / Behrens, Georg M N / Pöhlmann, Stefan / Hoffmann, Markus

    The Lancet. Infectious diseases

    2023  Volume 23, Issue 10, Page(s) e391–e392

    MeSH term(s) Humans ; COVID-19 ; SARS-CoV-2/genetics
    Language English
    Publishing date 2023-09-13
    Publishing country United States
    Document type Letter ; Research Support, Non-U.S. Gov't
    ZDB-ID 2061641-7
    ISSN 1474-4457 ; 1473-3099
    ISSN (online) 1474-4457
    ISSN 1473-3099
    DOI 10.1016/S1473-3099(23)00547-9
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  10. Article ; Online: SARS-CoV-2 delta variant neutralisation after heterologous ChAdOx1-S/BNT162b2 vaccination.

    Behrens, Georg Mn / Cossmann, Anne / Stankov, Metodi V / Nehlmeier, Inga / Kempf, Amy / Hoffmann, Markus / Pöhlmann, Stefan

    Lancet (London, England)

    2021  Volume 398, Issue 10305, Page(s) 1041–1042

    MeSH term(s) BNT162 Vaccine ; COVID-19 ; COVID-19 Vaccines ; Humans ; SARS-CoV-2 ; Vaccination
    Chemical Substances COVID-19 Vaccines ; BNT162 Vaccine (N38TVC63NU)
    Language English
    Publishing date 2021-08-17
    Publishing country England
    Document type Letter ; Research Support, Non-U.S. Gov't ; Comment
    ZDB-ID 3306-6
    ISSN 1474-547X ; 0023-7507 ; 0140-6736
    ISSN (online) 1474-547X
    ISSN 0023-7507 ; 0140-6736
    DOI 10.1016/S0140-6736(21)01891-2
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