High-precision phage 3D blueprint is drawn to provide reference for future screening work

An international research team led by the University of Otago in New Zealand has drawn a high-precision three-dimensional structure "blueprint" of a bacteriophage (a virus that infects bacteria), providing new scientific basis for using viruses to fight multi-drug-resistant "superbugs". The researchers say this result not only helps screen for phages more suitable for treatment, but also reveals ancient connections in the evolutionary history of viruses.

James Hodgkinson-Bean, first author of the paper and PhD in the Department of Microbiology and Immunology at the University of Otago, pointed out that as the threat of antimicrobial resistance continues to escalate, phages are gaining increasing attention as an alternative to traditional antibiotics. He introduced that phages are harmless to multicellular organisms, including humans, but can highly selectively recognize and kill specific bacteria. Therefore, they are increasingly being used in so-called "phage therapy" to treat highly drug-resistant bacterial infections.

In his view, bacteriophages are "extremely sophisticated viruses" whose infection process relies on a huge machine-like structure - the "tail". This study used high-resolution structural biology technology to conduct a detailed molecular analysis of a phage called Bas63 that hosts E. coli, focusing on revealing how its tail functions during the infection process. Relevant results were published in the journal Science Advances.

The work was carried out by scientists from the University of Otago and Okinawa Institute of Science and Technology. Hodgkinson-Bean pointed out that such structural studies are crucial to understanding the differences in infection behavior displayed by different phages in experiments, and also provide an important reference for how to select the "most suitable" phage clinically.

Mihnea Bostina, corresponding author of the paper and associate professor in the Department of Microbiology and Immunology at the University of Otago, said that phages are becoming increasingly important in the context of increasing global antibiotic resistance and plant diseases continuing to threaten food security. He emphasized that this detailed "blueprint" of phage structure will promote more rationally designed applications in medical, agricultural and industrial fields, such as treating drug-resistant infections and clearing biofilms in food processing and water supply systems.

Research shows that the three-dimensional structure of the virus contains rare "whisker-collar" connection structures, hexameric decorative proteins, and diverse tail fibers. Bostina pointed out that in addition to scientific value, these fine three-dimensional data may also bring creative inspiration to artists, animation practitioners and popular science educators.

Hodgkinson-Bean also emphasized that studying the structure of viruses can also help trace the ancient evolutionary history of viruses. He pointed out that for humans, DNA is usually the best "fingerprint" for tracing evolutionary relationships, but in the world of viruses, three-dimensional structures can often reveal deeper relationships with distantly related viruses. In this study, the team discovered some structural features that had previously been observed only in distant viruses, thus revealing previously unrecognized evolutionary connections.

Through structural studies, scientists already know that bacteriophages are related to herpes viruses, a relationship thought to date back to geological time billions of years before the emergence of multicellular life. Hodgkinson-Bean said that in this sense, when we observe the structure of phages, we are actually "appreciating living fossils, primitive ancient life forms," which "has a unique beauty in itself."

The virus structure announced this time is the second major achievement of its kind achieved by this research team in this field. They have previously analyzed the structure of a virus that causes potato diseases, and related work has recently been published in academic journals. The latest paper titled "Cryo-EM structure of bacteriophage Bas63 reveals structural conservation and diversity in the Felixounavirus genus" was published in Science Advances on November 12, 2025.

As antibiotics gradually lose their "control" over some pathogens, this high-resolution "blueprint" of phage structures brings new hope for the future development of more precise and efficient phage therapies to deal with superbugs.