Author

S. Pöhlmann

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Microbiology· 8 Biochemistry· 1 Immunology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 10 Research Focus:host-pathogen & immune response· 8 Organism:human· 7 Assay:proteomics· 6 Research Focus:cell type annotation· 2 Organism:rat· 2 Research Focus:clustering· 1 Research Focus:drug response / drug discovery· 1

Frequent Co-Authors

M. Hoffmann· 6 shared A. Stevaert· 2 shared I. Nehlmeier· 2 shared M. Laporte· 2 shared M. Winkler· 2 shared S. Gaertner· 2 shared V. Raeymaekers· 2 shared A. Cossmann· 1 shared

Activity by Year

2019-2022 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 14 mutual co-author links

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6 shared papersMicrobiology

M. Hoffmann

Mutual co-authors in cluster

Author profile →

10 papers

Recent·Most cited

Development of immortalized rhesus macaque kidney cells supporting infection with a panel of viruses

S. Reiter, S. Gaertner, S. Pöhlmann, M. Winkler

The paper reports the generation of TERT-immortalized rhesus macaque kidney cell lines susceptible to infection by multiple viruses including Zika and primate herpesviruses.

bioRxiv · Jul 18, 2022Microbiology

Primate simplexviruses differ in tropism for macaque cells

H. Hofmann-Winkler, A. R. Siregar, I. Rodriguez Polo, N. Esiyok, S. Gaertner, R. Behr, S. Pöhlmann, M. Winkler

This study compares the tropism of primate simplexviruses in macaque and human cells, finding that McHV1 and PaHV2 replicate efficiently in rhesus macaque cells while HSV1, HSV2, and CeHV2 do not.

bioRxiv · Jul 18, 2022Microbiology

SARS-CoV-2 neutralizing camelid heavy-chain-only antibodies as powerful tools for diagnostic and therapeutic applications

A. Schloer, S. Hirschberg, G. Ben Amor, T. L. Meister, P. Arora, S. Pöhlmann, M. Hoffmann, S. Pfaender, O. Kamal Eddin, J. Kamhieh-Milz, K. Hanack

This study identifies camelid heavy-chain-only antibodies that effectively neutralize SARS-CoV-2 and its variants, showing potential for diagnostic and therapeutic applications.

bioRxiv · Mar 24, 2022Immunology

The Omicron variant is highly resistant against antibody-mediated neutralization - implications for control of the COVID-19 pandemic

M. Hoffmann, N. Krüger, S. Schulz, A. Cossmann, C. Rocha, A. Kempf, I. Nehlmeier, L. Graichen, A.-S. Moldenhauer, M. S. Winkler, M. Lier, A. Dopfer-Jablonka, H.-M. Jäck, G. Behrens, S. Pöhlmann

This study shows the Omicron variant is highly resistant to antibody neutralization, reducing effectiveness of current therapies and vaccines.

bioRxiv · Dec 12, 2021Microbiology

LRRC15 mediates an accessory interaction with the SARS-CoV-2 spike protein

J. Shilts, T. M. Crozier, A. Teixeira-Silva, I. Gabaev, E. J. D. Greenwood, S. J. Watson, B. M. Ortmann, C. M. Gawden-Bone, T. Pauzaite, M. Hoffmann, J. A. Nathan, S. Pöhlmann, P. J. Lehner, G. J. Wright

The paper identifies LRRC15 as a novel host factor that interacts with SARS-CoV-2 spike protein, distinct from ACE2 and other known receptors, and shows it modulates viral infection.

bioRxiv · Sep 25, 2021Biochemistry

A novel class of TMPRSS2 inhibitors potently block SARS-CoV-2 and MERS-CoV viral entry and protect human epithelial lung cells

M. Mahoney, V. C. Damalanka, M. Tartell, D. H. Chung, A. L. Lourenco, D. Pwee, A. E. Mayer Bridwell, M. Hoffmann, J. Voss, P. Karmakar, N. P. Azouz, A. M. Klinger, P. W. Rothlauf, C. E. Thompson, M. Lee, , J. W. Janetka

This paper identifies a novel class of TMPRSS2 inhibitors that effectively block SARS-CoV-2 and MERS-CoV entry and show promise as a therapeutic for COVID-19.

bioRxiv · May 6, 2021Microbiology

The SARS-CoV-2 and other human coronavirus spike proteins are fine-tuned towards temperature and proteases of the human airways

M. Laporte, A. Stevaert, V. Raeymaekers, R. Van Berwaer, K. Martens, S. Pöhlmann, L. Naesens

This paper identifies how SARS-CoV-2 and other coronaviruses' spike proteins are adapted to specific airway temperatures and proteases, enhancing their transmission and pathogenicity.

bioRxiv · Nov 9, 2020Microbiology

Rapid SARS-CoV-2 Adaptation to Available Cellular Proteases

M. Z. Chaudhry, K. Eschke, M. Hoffmann, M. Grashoff, L. Abassi, Y. Kim, L. Brunotte, S. Ludwig, A. Kroeger, F. Klawonn, S. Pöhlmann, L. Cicin-Sain

This study shows SARS-CoV-2 adapts to Vero E6 cells by losing the furin cleavage motif in spike protein, but retains wildtype sequences, enabling reverse adaptation when passaged on human lung cells.

bioRxiv · Aug 10, 2020Microbiology

Structural Basis for Potent Neutralization of Betacoronaviruses by Single-domain Camelid Antibodies

D. Wrapp, D. De Vlieger, K. S. Corbett, G. M. Torres, W. Van Breedam, K. Roose, L. van Schie, VIB-CMB COVID-19 Response Team, M. Hoffmann, S. Pöhlmann, B. S. Graham, N. Callewaert, B. Schepens, X. Saelens, J. S. McLellan

This study isolates and characterizes VHH antibodies that neutralize MERS-CoV, SARS-CoV-1, and SARS-CoV-2 by blocking receptor binding, with structural insights into their epitopes and cross-reactivity.

bioRxiv · Mar 26, 2020Microbiology

Evidence for influenza B virus hemagglutinin adaptation to the human host: high cleavability, acid-stability and preference for cool temperature

M. Laporte, A. Stevaert, V. Raeymaekers, T. Boogaerts, I. Nehlmeier, W. Chiu, M. Benkheil, B. Vanaudenaerde, S. Pöhlmann, L. M. Naesens

This study compares influenza B virus (IBV) and influenza A virus (IAV) hemagglutinin (HA) adaptation to human airways, finding IBV HA is more cleavable, acid-stable, and temperature-preferred for human upper airways.

bioRxiv · Aug 23, 2019 · PreprintMicrobiology