Author

A. Stevaert

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· 6

Signature Assays, Organisms & Methods

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Approach:experimental assay· 6 Research Focus:host-pathogen & immune response· 5 Organism:human· 4 Research Focus:drug response / drug discovery· 1 Assay:proteomics· 1 Organism:virus· 1

Frequent Co-Authors

M. Laporte· 3 shared V. Raeymaekers· 3 shared B. Provinciael· 2 shared D. Schols· 2 shared E. Vanhulle· 2 shared J. Stroobants· 2 shared K. Vermeire· 2 shared L. Naesens· 2 shared

Activity by Year

2019-2022 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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3 shared papersMicrobiology

M. Laporte

Mutual co-authors in cluster

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6 papers

Recent·Most cited

Cellular electrical impedance to profile SARS-CoV-2 fusion inhibitors and to assess the fusogenic potential of spike mutants

E. Vanhulle, J. Doijen, J. Stroobants, B. Provinciael, S. Noppen, D. Schols, A. Stevaert, K. Vermeire

This paper demonstrates the use of cellular electrical impedance to monitor SARS-CoV-2 spike-mediated cell-cell fusion and assess fusion inhibitors and spike mutants.

bioRxiv · Dec 13, 2022Microbiology

Carbohydrate-Binding Protein from Stinging Nettle as Fusion Inhibitor for SARS-CoV-2 Variants of Concern

E. Vanhulle, T. D'huys, B. Provinciael, J. Stroobants, A. Camps, S. Noppen, D. Schols, E. J. M. Van Damme, P. Maes, A. Stevaert, K. Vermeire

This paper shows that UDA, a protein from stinging nettle, inhibits SARS-CoV-2 and its variants by blocking viral entry and fusion, with nanomolar potency.

bioRxiv · Jul 8, 2022Microbiology

Effect of SARS-CoV-2 spike mutations on its activation by TMPRSS2 and TMPRSS13

A. Stevaert, R. Van Berwaer, V. Raeymaekers, M. Laporte, L. M. J. Naesens

This study investigates how mutations in the SARS-CoV-2 spike protein's S2 motif affect activation by TMPRSS2 and TMPRSS13 proteases, finding that K814 is dispensable for TMPRSS2 but not TMPRSS13.

bioRxiv · Jan 26, 2022 · PreprintMicrobiology

Betulonic acid derivatives inhibiting coronavirus replication in cell culture via the nsp15 endoribonuclease

B. Krasniqi, A. Stevaert, B. Van Loy, T. Nguyen, J. Thomas, J. Vandeput, D. Jochmans, V. Thiel, R. Dijkman, W. Dehaen, A. Voet, L. Naesens

This study identifies betulonic acid derivatives as inhibitors of coronavirus replication by targeting the nsp15 endoribonuclease, with EC50 of 0.6 M against 229E.

bioRxiv · Dec 10, 2020Microbiology

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

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