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The N-Terminal Domain of Tailspike Depolymerases Affects the Replication Efficiency of Synthetic Klebsiella Phages. / Baykov, Ivan K.; Mikhaylova, Ekaterina E.; Miroshnikova, Anna V. et al.

In: International Journal of Molecular Sciences, Vol. 26, No. 23, 11297, 22.11.2025.

Research output: Contribution to journal › Article › peer-review

Harvard

Baykov, IK, Mikhaylova, EE, Miroshnikova, AV, Fedorets, VA, Markova, SA, Ushakova, TA, Morozova, VV & Tikunova, NV 2025, 'The N-Terminal Domain of Tailspike Depolymerases Affects the Replication Efficiency of Synthetic Klebsiella Phages', International Journal of Molecular Sciences, vol. 26, no. 23, 11297. https://doi.org/10.3390/ijms262311297

APA

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

Vancouver

Baykov IK, Mikhaylova EE, Miroshnikova AV, Fedorets VA, Markova SA, Ushakova TA et al. The N-Terminal Domain of Tailspike Depolymerases Affects the Replication Efficiency of Synthetic Klebsiella Phages. International Journal of Molecular Sciences. 2025 Nov 22;26(23):11297. doi: 10.3390/ijms262311297

Author

Baykov, Ivan K. ; Mikhaylova, Ekaterina E. ; Miroshnikova, Anna V. et al. / The N-Terminal Domain of Tailspike Depolymerases Affects the Replication Efficiency of Synthetic Klebsiella Phages. In: International Journal of Molecular Sciences. 2025 ; Vol. 26, No. 23.

BibTeX

@article{8266431dbf274e7ab3581ea366216cd6,
title = "The N-Terminal Domain of Tailspike Depolymerases Affects the Replication Efficiency of Synthetic Klebsiella Phages",
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.",
author = "Baykov, {Ivan K.} and Mikhaylova, {Ekaterina E.} and Miroshnikova, {Anna V.} and Fedorets, {Valeriya A.} and Markova, {Sofya A.} and Ushakova, {Tatyana A.} and Morozova, {Vera V.} and Tikunova, {Nina V.}",
note = "This research was funded by the Russian Science Foundation, grant number 24-24-00553.",
year = "2025",
month = nov,
day = "22",
doi = "10.3390/ijms262311297",
language = "English",
volume = "26",
journal = "International Journal of Molecular Sciences",
issn = "1661-6596",
publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
number = "23",

}

RIS

TY - JOUR

T1 - The N-Terminal Domain of Tailspike Depolymerases Affects the Replication Efficiency of Synthetic Klebsiella Phages

AU - Baykov, Ivan K.

AU - Mikhaylova, Ekaterina E.

AU - Miroshnikova, Anna V.

AU - Fedorets, Valeriya A.

AU - Markova, Sofya A.

AU - Ushakova, Tatyana A.

AU - Morozova, Vera V.

AU - Tikunova, Nina V.

N1 - This research was funded by the Russian Science Foundation, grant number 24-24-00553.

PY - 2025/11/22

Y1 - 2025/11/22

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/105024641236

UR - https://www.mendeley.com/catalogue/062bfc55-44ba-3375-ad26-d795e19ba1f7/

U2 - 10.3390/ijms262311297

DO - 10.3390/ijms262311297

M3 - Article

C2 - 41373458

VL - 26

JO - International Journal of Molecular Sciences

JF - International Journal of Molecular Sciences

SN - 1661-6596

IS - 23

M1 - 11297

ER -

ID: 72828544