Author

J. Potempa

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 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 7 Organism:human· 6 Research Focus:host-pathogen & immune response· 5 Organism:mouse· 2 Assay:proteomics· 2 Research Focus:cancer & tumor microenvironment· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1

Frequent Co-Authors

A. Lesner· 2 shared C. Scavenius· 2 shared E. Bielecka· 2 shared G. Dubin· 2 shared J. J. Enghild· 2 shared K. Falkowski· 2 shared K. Pyrc· 2 shared M. Kalinska· 2 shared

Activity by Year

2019-2024 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 30 mutual co-author links

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2 shared papersBiochemistry

A. Lesner

Mutual co-authors in cluster

Author profile →

7 papers

Recent·Most cited

Inhibition of SARS-CoV-2 infection by Porphyromonas gingivalis and the oral microbiome

A. Bontempo, A. Chirino, A. Heidari, A. Lugo, S. Shindo, M. R. Pastore, S. Antonson, C. Godoy, F. Nichols, J. Potempa, M. Davey, T. Kawai, M. Cayabyab

This study shows that Porphyromonas gingivalis and other oral bacteria can inhibit SARS-CoV-2 infection through cytotoxicity and unknown mechanisms, with individual variation in oral microbiome activity.

bioRxiv · Feb 27, 2024 · PreprintMicrobiology

Acriflavine, a clinically aproved drug, inhibits SARS-CoV-2 and other betacoronaviruses

V. Napolitano, A. Dabrowska, K. Schorpp, A. Mourao, E. Barreto-Duran, M. Benedyk, P. Botwina, S. Brandner, M. Bostock, Y. Chykunova, A. Czarna, G. Dubin, T. Frohlich, M. Hoelscher, M. Jedrysik, , K. Pyrc

This study identifies acriflavine as a potent inhibitor of SARS-CoV-2 and other betacoronaviruses, effective in cellular models, in vivo, and ex vivo.

bioRxiv · Mar 20, 2021Microbiology

The essential Porphyromonas gingivalis type IX secretion system component PorZ delivers anionic-lipopolysaccharide to the PorU sortase for transpeptidase processing of cargos

M. Madej, Z. Nowakowska, M. Ksiazek, A. M. Lasica, D. Mizgalska, N. Magdalena, A. Jacula, C. Scavenius, J. J. Enghild, J. Aduse-Opoku, M. A. Curtis, F. X. Gomis-Rüth, J. Potempa

This paper identifies PorZ as a T9SS component that binds anionic lipopolysaccharide (A-LPS) and interacts with the PorU sortase to facilitate cargo protein anchoring to the outer membrane.

mBio · Feb 23, 2021Peer-reviewedMicrobiology

Kallikrein-related peptidase 14 activates zymogens of membrane type matrix metalloproteinases (MT-MMPs) - a CleavEx library-based analysis

K. Falkowski, E. Bielecka, I. B. Thogersen, O. Bochenska, K. Płaza, M. Kalinska, L. Sasiadek, M. Magoch, A. Pecak, M. Wisniewska, N. Gruba, M. Wysocka, A. Wojtysiak, M. Brzezinska-Bodal, K. Sychowska, , T. Kantyka

This study identifies KLK14 as a specific activator of proMT-MMPs using a CleavEx library-based approach, revealing its role in ECM remodeling and potential implications in cancer.

bioRxiv · Apr 23, 2020Biochemistry

Kallikrein 13: a new player in coronaviral infections.

A. Milewska, K. Falkowski, M. Kalinska, E. Bielecka, A. Naskalska, P. Mak, A. Lesner, M. Ochman, M. Urlik, J. Potempa, T. Kantyka, K. Pyrc

This study identifies KLK13 as a protease required for HCoV-HKU1 infection and shows it cleaves the viral S protein, determining tissue specificity and potential interspecies transmission.

bioRxiv · Mar 1, 2020 · PreprintMicrobiology

Intracellular Staphylococcus aureus employs the cysteine protease staphopain A to induce host cell death in epithelial cells

K. Stelzner, T. Hertlein, A. Sroka, A. Moldovan, K. Paprotka, D. Kessie, H. Mehling, J. Potempa, K. Ohlsen, M. Fraunholz, T. Rudel

This study identifies staphopain A as a cysteine protease used by intracellular Staphylococcus aureus to induce host cell death and enhance bacterial survival during infection.

bioRxiv · Feb 10, 2020Microbiology

Dynamic oligopeptide acquisition by the RagAB transporter from Porphyromonas gingivalis

M. Madej, J. White, Z. Nowakowska, S. Rawson, C. Scavenius, J. Enghild, G. Bereta, K. Pothula, U. Kleinekathoefer, A. Basle, N. Ranson, J. Potempa, B. van den Berg

This study identifies RagAB as the oligopeptide transporter in P. gingivalis, revealing its structure and mechanism for nutrient uptake from the extracellular environment.

bioRxiv · Sep 4, 2019Microbiology