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Volume 26
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10.3390/ijms262311297
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This is an early access version, the complete PDF, HTML, and XML versions will be available soon.
Article

The N-Terminal Domain of Tailspike Depolymerases Affects the Replication Efficiency of Synthetic Klebsiella Phages

by
Ivan K. Baykov
1,2,*,
Ekaterina E. Mikhaylova
1,3,
Anna V. Miroshnikova
1,3,
Valeriya A. Fedorets
1,
Sofya A. Markova
3,
Tatyana A. Ushakova
1,
Vera V. Morozova
1 and
Nina V. Tikunova
1,*
1
Laboratory of Molecular Microbiology, Institute of Chemical Biology and Fundamental Medicine of the Siberian Branch of the Russian Academy of Sciences, Novosibirsk 630090, Russia
2
Shared Research Facility “Siberian Circular Photon Source” (SRF “SKIF”), Boreskov Institute of Catalysis of the Siberian Branch of the Russian Academy of Sciences, Novosibirsk 630090, Russia
3
Faculty of Natural Sciences, Novosibirsk State University, Novosibirsk 630090, Russia
*
Authors to whom correspondence should be addressed.
Int. J. Mol. Sci. 2025, 26(23), 11297; https://doi.org/10.3390/ijms262311297 (registering DOI)
Submission received: 30 September 2025 / Revised: 13 November 2025 / Accepted: 19 November 2025 / Published: 22 November 2025
(This article belongs to the Special Issue Exploring Phage–Host Interactions: Novel Findings and Perspectives)
Review Reports Versions Notes

Abstract

Bacteriophage receptor-binding proteins are often attached to the tail via a conserved N-terminal adapter/anchor domain, presumed to function independently from the distal receptor-binding/catalytic domain. Using synthetic phage technology, we demonstrated that the N-terminal domain in Przondovirus phages KP192 and KP195 substantially modulates the receptor-binding and hydrolytic activities of their type A tailspikes. A bioinformatics analysis of related proteins revealed a high correlation between the N-terminal domain and the distal receptor-binding region. Furthermore, it was shown that an imperfect structural fit between the N-terminal domain and the adjacent tail proteins (gatekeeper and nozzle proteins) can reduce virion assembly efficiency, thereby impairing phage fitness. These results underscore the importance of selecting an appropriate N-terminal domain of receptor-binding proteins when engineering bacteriophages with altered host specificity.
Keywords: bacteriophage; Klebsiella; tailspike depolymerase; receptor-binding protein; anchor domain; adapter domain; synthetic biology; genome assembly; transformation-associated recombination cloning bacteriophage; Klebsiella; tailspike depolymerase; receptor-binding protein; anchor domain; adapter domain; synthetic biology; genome assembly; transformation-associated recombination cloning

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MDPI and ACS Style

Baykov, I.K.; Mikhaylova, E.E.; Miroshnikova, A.V.; Fedorets, V.A.; Markova, S.A.; Ushakova, T.A.; Morozova, V.V.; Tikunova, N.V. The N-Terminal Domain of Tailspike Depolymerases Affects the Replication Efficiency of Synthetic Klebsiella Phages. Int. J. Mol. Sci. 2025, 26, 11297. https://doi.org/10.3390/ijms262311297

AMA Style

Baykov IK, Mikhaylova EE, Miroshnikova AV, Fedorets VA, Markova SA, Ushakova TA, Morozova VV, Tikunova NV. The N-Terminal Domain of Tailspike Depolymerases Affects the Replication Efficiency of Synthetic Klebsiella Phages. International Journal of Molecular Sciences. 2025; 26(23):11297. https://doi.org/10.3390/ijms262311297

Chicago/Turabian Style

Baykov, Ivan K., Ekaterina E. Mikhaylova, Anna V. Miroshnikova, Valeriya A. Fedorets, Sofya A. Markova, Tatyana A. Ushakova, Vera V. Morozova, and Nina V. Tikunova. 2025. "The N-Terminal Domain of Tailspike Depolymerases Affects the Replication Efficiency of Synthetic Klebsiella Phages" International Journal of Molecular Sciences 26, no. 23: 11297. https://doi.org/10.3390/ijms262311297

APA Style

Baykov, I. K., Mikhaylova, E. E., Miroshnikova, A. V., Fedorets, V. A., Markova, S. A., Ushakova, T. A., Morozova, V. V., & Tikunova, N. V. (2025). The N-Terminal Domain of Tailspike Depolymerases Affects the Replication Efficiency of Synthetic Klebsiella Phages. International Journal of Molecular Sciences, 26(23), 11297. https://doi.org/10.3390/ijms262311297

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