# NAIST researchers resolve how phage protein SglPP7 blocks bacterial lipid transporter MurJ

- Published: 2026-11-10 12:31 UTC
- Section: Life & Health › Biology & biochemistry
- Tags: MurJ lipid transporter, phage lysis protein, SglPP7, cryo-electron microscopy, drug-resistant bacteria, bacterial cell wall, convergent evolution, Nara Institute of Science and Technology
- URL: https://realtech.media/news/rt-9026aeac9fbe54aac0ec8e4c_naist_researchers_resolve/

**Cryo-EM structure shows how the phage protein SglPP7 locks MurJ, a bacterial lipid transporter. The work is basic research relevant to the search for new antibacterials.**

![NAIST researchers resolve how phage protein SglPP7 blocks bacterial lipid transporter MurJ](https://realtech.media/media/2026/11/37c36c28e3c77381.webp)
*ua.news*

Researchers at the Nara Institute of Science and Technology (NAIST), Japan, have determined how the bacteriophage protein SglPP7 inhibits MurJ, a bacterial protein that transports lipids needed to build the cell wall. The study, led by Assistant Professor Hidetaka Kohga, was published in PLOS Biology on October 27, 2026, according to news-medical.net [1]. The authors describe the work as basic research [1].

Drug-resistant bacteria are becoming more common worldwide, and new antibiotics require new cellular targets. Bacteriophages infect bacteria and hijack their cellular machinery to replicate. Some of them inject small proteins that shut down specific bacterial processes and ultimately kill the cell. MurJ is one such target. Several phage proteins that inhibit MurJ are known, but their amino acid sequences vary considerably, so it was unclear whether they use the same molecular strategy [1].

## Structure of the MurJ–SglPP7 complex

The team used cryo-electron microscopy, which resolves biological molecules at near-atomic resolution, to determine the structure of the MurJ–SglPP7 complex. They also carried out targeted protein mutations, bacterial cell lysis experiments and computer simulations to examine how the interaction with SglPP7 affects MurJ's behavior [1].

SglPP7 lies along a lipid-binding groove in MurJ and inserts its short C-terminal tail into a deep internal cavity. This holds MurJ in an outward-facing conformation and prevents the back-and-forth structural changes required to transport lipid [1].

## Comparison with other phage proteins

The authors compared SglPP7 with two other known phage proteins, LysM and SglCJ3. All three stabilize a similar conformation of MurJ, although they bind to it in different ways. "These findings suggest convergent evolution toward a common target through diverse inhibitory mechanisms," Kohga said [1].

According to the researchers, understanding these interactions could help in designing new drugs and engineering artificial phage proteins with targeted antibacterial activity. Kohga said the study provides a foundation for drug discovery targeting this transporter and that the findings could contribute to new antibacterial agents against drug-resistant bacteria, while noting that the work remains at the basic research stage [1].

Co-authors from NAIST are Kaito Hosoda, Sixian Wu, Hiroyuki Tanaka, Hideki Shigematsu, Ryoji Miyazaki, Min Fey Chek and Tomoya Tsukazaki [1].

## Sources

1. [news-medical.net](https://www.news-medical.net/news/20261109/Phage-protein-study-opens-new-path-for-future-antibiotics.aspx)
2. [ua.news](https://ua.news/en/dovkolo-svitu/iaponski-naukovtsi-pokazali-iak-fagovii-bilok-blokuie-murj-news-medical)

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Source: RealTech, realtech.media — https://realtech.media/news/rt-9026aeac9fbe54aac0ec8e4c_naist_researchers_resolve/