The O-specific polysaccharide lyase from the phage LKA1 tailspike reduces Pseudomonas virulence

Tomasz Olszak, Mikhail M. Shneider, Agnieszka Latka, Barbara Maciejewska, Christopher Browning, Lada V. Sycheva, Anneleen Cornelissen, Katarzyna Danis-Wlodarczyk, Sofya N. Senchenkova, Alexander S. Shashkov, Grzegorz Gula, Michal Arabski, Slawomir Wasik, Konstantin A. Miroshnikov, Rob Lavigne, Petr Leiman, Yuriy A. Knirel, Zuzanna Drulis-Kawa

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Abstract

Pseudomonas phage LKA1 of the subfamily Autographivirinae encodes a tailspike protein (LKA1gp49) which binds and cleaves B-band LPS (O-specific antigen, OSA) of Pseudomonas aeruginosa PAO1. The crystal structure of LKA1gp49 catalytic domain consists of a beta-helix, an insertion domain and a C-terminal discoidin-like domain. The putative substrate binding and processing site is located on the face of the beta-helix whereas the C-terminal domain is likely involved in carbohydrates binding. NMR spectroscopy and mass spectrometry analyses of degraded LPS (OSA) fragments show an O5 serotype-specific polysaccharide lyase specificity. LKA1gp49 reduces virulence in an in vivo Galleria mellonella infection model and sensitizes P. aeruginosa to serum complement activity. This enzyme causes biofilm degradation and does not affect the activity of ciprofloxacin and gentamicin. This is the first comprehensive report on LPS-degrading lyase derived from a Pseudomonas phage. Biological properties reveal a potential towards its applications in antimicrobial design and as a microbiological or biotechnological tool.

Original languageEnglish (US)
Article number16302
JournalScientific Reports
Volume7
Issue number1
DOIs
StatePublished - Dec 1 2017

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Polysaccharide-Lyases
Pseudomonas Phages
O Antigens
Pseudomonas
Bacteriophages
Pseudomonas aeruginosa
Virulence
Lyases
Ciprofloxacin
Biofilms
Gentamicins
Mass Spectrometry
Catalytic Domain
Magnetic Resonance Spectroscopy
Binding Sites
Carbohydrates
Enzymes
Infection
Serum
Proteins

ASJC Scopus subject areas

  • General

Cite this

Olszak, T., Shneider, M. M., Latka, A., Maciejewska, B., Browning, C., Sycheva, L. V., ... Drulis-Kawa, Z. (2017). The O-specific polysaccharide lyase from the phage LKA1 tailspike reduces Pseudomonas virulence. Scientific Reports, 7(1), [16302]. https://doi.org/10.1038/s41598-017-16411-4

The O-specific polysaccharide lyase from the phage LKA1 tailspike reduces Pseudomonas virulence. / Olszak, Tomasz; Shneider, Mikhail M.; Latka, Agnieszka; Maciejewska, Barbara; Browning, Christopher; Sycheva, Lada V.; Cornelissen, Anneleen; Danis-Wlodarczyk, Katarzyna; Senchenkova, Sofya N.; Shashkov, Alexander S.; Gula, Grzegorz; Arabski, Michal; Wasik, Slawomir; Miroshnikov, Konstantin A.; Lavigne, Rob; Leiman, Petr; Knirel, Yuriy A.; Drulis-Kawa, Zuzanna.

In: Scientific Reports, Vol. 7, No. 1, 16302, 01.12.2017.

Research output: Contribution to journalArticle

Olszak, T, Shneider, MM, Latka, A, Maciejewska, B, Browning, C, Sycheva, LV, Cornelissen, A, Danis-Wlodarczyk, K, Senchenkova, SN, Shashkov, AS, Gula, G, Arabski, M, Wasik, S, Miroshnikov, KA, Lavigne, R, Leiman, P, Knirel, YA & Drulis-Kawa, Z 2017, 'The O-specific polysaccharide lyase from the phage LKA1 tailspike reduces Pseudomonas virulence', Scientific Reports, vol. 7, no. 1, 16302. https://doi.org/10.1038/s41598-017-16411-4
Olszak T, Shneider MM, Latka A, Maciejewska B, Browning C, Sycheva LV et al. The O-specific polysaccharide lyase from the phage LKA1 tailspike reduces Pseudomonas virulence. Scientific Reports. 2017 Dec 1;7(1). 16302. https://doi.org/10.1038/s41598-017-16411-4
Olszak, Tomasz ; Shneider, Mikhail M. ; Latka, Agnieszka ; Maciejewska, Barbara ; Browning, Christopher ; Sycheva, Lada V. ; Cornelissen, Anneleen ; Danis-Wlodarczyk, Katarzyna ; Senchenkova, Sofya N. ; Shashkov, Alexander S. ; Gula, Grzegorz ; Arabski, Michal ; Wasik, Slawomir ; Miroshnikov, Konstantin A. ; Lavigne, Rob ; Leiman, Petr ; Knirel, Yuriy A. ; Drulis-Kawa, Zuzanna. / The O-specific polysaccharide lyase from the phage LKA1 tailspike reduces Pseudomonas virulence. In: Scientific Reports. 2017 ; Vol. 7, No. 1.
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