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Posted:Jun 30, 2026 Research Highlights

Flexible motion of bacteriophage tail fibers modulates infection

In this study, as part of an international collaboration supported in part by the Bio-SPM Summer School and the Collaborative Research Program (2024–2025), a research team led by Associate Professor Hiroki Konno and Soma Yamamoto (master’s student in the Division of Life Science and Engineering and member of the WISE Program for Nano-Precision Medicine, Science, and Engineering) at the Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, together with Professor Noriyuki Kodera (WPI-NanoLSI), in collaboration with Assistant Professor Balint Kiss and Professor Miklos Kellermayer (Department of Biophysics and Radiation Biology, Semmelweis University, Hungary), has successfully elucidated a key dynamic mechanism utilized by bacteriophages in the process of recognizing the surface of their host (bacterial) cells.
This study focuses on the tail fibers of T7 bacteriophage (*1), which were expressed and purified at the Department of Biophysics and Radiation Biology, Semmelweis University (Budapest, Hungary). The fibers were subsequently imaged using high-speed atomic force microscopy (HS-AFM) at the Nano Life Science Institute (WPI-NanoLSI), Kanazawa University (Kanazawa, Japan).
This study highlights the crucial role of viral protein dynamics in the T7 bacteriophage infection process. HS-AFM observations reveal that T7 tail fibers exhibit both bending and torsional flexibility, suggesting that these mechanical properties are actively utilized by the phage during host cell surface exploration.

The results were published online as Open Access in Small (Wiley) on June 19, 2026.

【Background】
Bacteriophages—viruses that specifically infect bacteria—have attracted increasing attention in recent years due to their potential therapeutic applications in overcoming multidrug-resistant bacterial infections.
In this study, the team investigated the structural dynamics of the tail fibers of T7 bacteriophage. The T7 virion consists of an icosahedral capsid (*2) and a tail-fiber complex, which plays a critical role in bacterial target recognition and viral DNA injection. The virus possesses six L-shaped fibers, approximately 40 nm in length, attached to the tail tube. These fibers are believed to be essential for initial host recognition and may also facilitate surface exploration.
During the first step of infection, phages recognize and attach to the bacterial outer membrane via their tail fibers. This is followed by full phage immobilization through engagement of the tail tube. However, the precise sequence of events and the mechanisms triggering these binding processes remain unclear.

【Summary of the Research Findings】
Using high-speed atomic force microscopy (HS-AFM), molecular dynamics (MD) simulations, and small-angle X-ray scattering (SAXS), the team analyzed the molecular structure and dynamics of isolated tail fibers and tail-fiber complexes (Fig. 1).

Fig. 1. During host recognition, T7 bacteriophage fibers transition from a capsid-bound state to an extended conformation, a process that requires structural flexibility (left). HS-AFM observation demonstrates the fibers contain a molecular hinge and a torsionally compliant coiled-coil region (right).

The results reveal that the kink region separating the proximal and distal segments of the fiber functions as a molecular hinge, enabling large-scale bending motions. This flexibility may enable the phage to explore the host surface through a “walking-like” mechanism.
Additionally, partial unwinding and rewinding within the triple-helical coiled-coil structure (*3) of the proximal segment allow for rotational and torsional flexibility. These dynamic features enable rapid, large-scale flexing and extension of the fibers, facilitating an efficient topological search for anchoring sites on the host cell surface.
Because fiber-assisted topological search is likely a general mechanism of host recognition, its modulation may provide a means to fine-tune phage–bacterium interactions.

【Future Perspectives】

This study characterizes the large-scale motions of T7 tail fibers and suggests their functional role in host cell surface exploration. As a next step, the team aims to directly observe the movement of tail-fiber complexes on the surface of living bacteria using HS-AFM.
In addition, the team plans to investigate the nanomechanics of fiber–host binding using optical tweezers, thereby providing further insight into the physical forces underlying the infection process.

Glossary

*1 T7 Bacteriophage
A type of bacteriophage (a virus that infects bacteria) that infects Escherichia coli. It uses six tail fibers located at its tail to recognize and bind to the bacterial surface. It then injects its own DNA into the bacterium to initiate infection. T7 bacteriophage is widely used as a representative model phage for studying viral infection mechanisms.
*2 Capsid
A protein shell that encloses and protects the viral genetic material (DNA or RNA). The T7 bacteriophage has an icosahedral structure and stores viral DNA inside.
*3 Triple-Helical Coiled-Coil Structure
A structure formed by three protein strands winding around each other in a helical manner. It is both strong and flexible. In this study, this structure was shown to enable the twisting motion of the T7 bacteriophage tail fiber complex.

Article

Title
Large-Scale Structural Dynamics in the Tail Fiber Modulate the Infective Transition of the T7 Bacteriophage.
Author
Luca Elizabet Kosik, Miklós Cervenak, Dominik Sziklai, Andrea Balogh-Molnár, Negar Rahimi, Bence Fehér, Soma Yamamoto, Hiroki Konno, Noriyuki Kodera, Holger Flechsig, Romain Amyot, Heinz Amenitsch, Hedvig Tordai, Levente Herényi, Ana Cuervo, Miklós Kellermayer, Bálint Kiss.
Journal
Small
Publication date
Jun 19, 2026
DOI
10.1002/smll.74269
URL
https://onlinelibrary.wiley.com/doi/10.1002/smll.74269

Funder

Access to the TU Graz Austrian SAXS beamline at ELETTRA-Sincrotrone Trieste was provided by the CERIC-ERIC consortium and is gratefully acknowledged. This work was supported by the Hungarian National Research, Development and Innovation Office (NKFIH) (K143321 and 2020-2.1.1-ED-2024-00292/EUniWell to MK) and by HUN-REN-KUTT-2025 (02073). This work was partly supported by the World Premier International Research Center Initiative (WPI), MEXT, Japan, the NanoLSI Bio-SPM Collaborative Research program, and the Kanazawa University CHOZEN Project. Bálint Kiss was supported by the EKÖP-2025-328 university excellence scholarship program of the Hungarian Ministry for Culture and Innovation, funded by the National Research, Development and Innovation Fund. KIFÜ is gratefully acknowledged for providing access to CPU and GPU resources on the Komondor high-performance computing system, as well as for associated technical support. Support from the HUN-REN Welcome Home and Foreign Researcher Recruitment Programme 2023 is also acknowledged.