Author

Barbara Maciejewska

University of WrocławORCID 0000-0002-4876-8743Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

Click to filter author papers

Signature Assays, Organisms & Methods

Click to filter · or open tag

Assay:proteomics· 3 Organism:bacteria (other)· 2 Research Focus:cell type annotation· 2 Approach:statistical model· 2 Research Focus:clustering· 1 Approach:deep learning· 1 Research Focus:drug response / drug discovery· 1 Approach:experimental assay· 1

Frequent Co-Authors

Zuzanna Drulis‐KawaiD· 3 shared Aleksandra OtwinowskaiD· 2 shared Janusz KoszuckiiD· 2 shared Rafal J. MostowyiD· 2 shared Sebastian OlejniczakiD· 2 shared Vyshakh R. Panicker· 2 shared Agnieszka KwiatekiD· 1 shared Agnieszka ŁątkaiD· 1 shared

Activity by Year

2025-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 35 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

3 shared papersMicrobiology

Zuzanna Drulis‐KawaORCID

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Identification and characterization of the antigonococcal prophage-encoded endolysin Phi1gp518

Magdalena Krzysztofik - Pelka, Barbara Maciejewska, Zuzanna Drulis‐Kawa, Agnieszka Kwiatek, Monika Adamczyk-Popławska

This study identifies and characterizes Phi1gp518, a prophage-encoded endolysin with broad antigonococcal activity and potential therapeutic applications against drug-resistant Neisseria gonorrhoeae.

bioRxiv · Jul 13, 2026 · PreprintMicrobiology

Capsular specificity in temperate phages of Klebsiella pneumoniae is driven by diverse receptor-binding enzymes

Aleksandra Otwinowska, Janusz Koszucki, Vyshakh R. Panicker, Jade Leconte, Sebastian Olejniczak, Kathryn E. Holt, Edward J. Feil, Eduardo P. C. Rocha, Bogna J. Smug, Barbara Maciejewska, Zuzanna Drulis‐Kawa, Rafal J. Mostowy

This study identifies prophage-encoded receptor-binding proteins (RBPs) mediating capsule specificity in Klebsiella pneumoniae, revealing structural diversity and functional activity beyond classical depolymerases.

PLoS Biology · Apr 28, 2026Peer-reviewedMicrobiology

DepoCatalog: Mapping the Diversity of 105 Recombinant Klebsiella Phage Depolymerases Across Sequence, Structure, and Substrate Specificity

Aleksandra Otwinowska, Sebastian Olejniczak, Agnieszka Łątka, Maria Pozniak, Grażyna Majkowska-Skrobek, Barbara Maciejewska, Janusz Koszucki, Vyshakh R. Panicker, Sara Jabłońska, Mathilde Hulsens, Joachim J. Bugert, Régis Tournebize, Stan J. J. Brouns, Flavia Squeglia, Rita Berisio, , Zuzanna Drulis‐Kawa

The paper catalogs 105 recombinant Klebsiella phage depolymerases, classifying them by sequence, structure, and substrate specificity, revealing diverse enzyme functions and evolutionary patterns.

bioRxiv · Sep 9, 2025 · PreprintMicrobiology