Biophysical Reviews

, Volume 10, Issue 2, pp 641–658 | Cite as

Artificial bio-nanomachines based on protein needles derived from bacteriophage T4

  • Hiroshi Inaba
  • Takafumi Ueno


Bacteriophage T4 is a natural bio-nanomachine which achieves efficient infection of host cells via cooperative motion of specific three-dimensional protein architectures. The relationships between the protein structures and their dynamic functions have recently been clarified. In this review we summarize the design principles for fabrication of nanomachines using the component proteins of bacteriophage T4 based on these recent advances. We focus on the protein needle known as gp5, which is located at the center of the baseplate at the end of the contractile tail of bacteriophage T4. This protein needle plays a critical role in directly puncturing host cells, and analysis has revealed that it contains a common motif used for cell puncture in other known injection systems, such as T6SS. Our artificial needle based on the β-helical domain of gp5 retains the ability to penetrate cells and can be engineered to deliver various cargos into living cells. Thus, the unique components of bacteriophage T4 and other natural nanomachines have great potential for use as molecular scaffolds in efforts to fabricate new bio-nanomachines.


Bacteriophage T4 Gp5 β-Helix Protein needle Cell penetration 



This work was supported by a Research Fellowship for Young Scientists of JSPS for H.I. (No. 4240) and by JSPS KAKENHI grant nos. JP13F03343, JP16H04177, JP16K13095, JP23350080, and JP26102513 and from Mochida Memorial Foundation for Medical and Pharmaceutical Research for T.U.

Compliance with ethical standards

Conflict of interest

Hiroshi Inaba declares that he has no conflict of interest. Takafumi Ueno declares that he has no conflict of interest.

Ethical approval

This article does not contain any studies with human participants or animals performed by the authors.


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© International Union for Pure and Applied Biophysics (IUPAB) and Springer-Verlag GmbH Germany, part of Springer Nature 2017

Authors and Affiliations

  1. 1.Department of Chemistry and Biotechnology, Graduate School of EngineeringTottori UniversityTottoriJapan
  2. 2.School of Life Science and TechnologyTokyo Institute of TechnologyYokohamaJapan

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