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Determination of the three-dimensional structure of bacteriophage Mu(-) tail fiber and its characterization
Yukina Mori1, Eiki Yamashita2, Atsushi Nakagawa2
1Faculty of Science and Technology, Division of Molecular Science, Gunma University, 1-5-1 Tenjin-cho, Kiryu, Gunma, 376-8515, Japan.
Abstract:
Bacteriophage Mu is a temperate phage known to infect various species of Enterobacteria, playing a role in bacterial mutation induction and horizontal gene transfer. The phage possesses two types of tail fibers important for host recognition, which enable it to expand its range of hosts. The alternate tail fibers are formed through the action of genes 49-50 or 52-51, allowing the Mu phage to recognize different surfaces of host cells. In a previous study, we presented the X-ray crystal structure of the C-terminal lipopolysaccharide (LPS)-binding domain of gene product (gp) 49, one of the subunits comprising the Mu tail fiber. In this study, we have determined the structure of the alternative tail fiber subunit, gp52, and compared it with other tail fibers. The results revealed that Mu phage employs different structural motifs for two individual tail fibers for recognizing different hosts.
Insights
Bacteriophage Mu uses distinct tail fiber structures to recognize and infect different bacterial hosts. This study determined the structure of an alternative tail fiber subunit, revealing unique motifs for host recognition.
Area of Science:
- Microbiology
- Structural Biology
- Virology
Background:
- Bacteriophage Mu is a temperate phage infecting Enterobacteria, contributing to bacterial mutation and gene transfer.
- Phage host recognition relies on tail fibers, with Bacteriophage Mu utilizing two types for host range expansion.
- Previous work elucidated the structure of the gp49 tail fiber subunit.
Purpose of the Study:
- To determine the structure of the alternative tail fiber subunit, gp52, of Bacteriophage Mu.
- To compare the structural motifs of gp52 with other tail fibers.
- To understand the molecular basis of host recognition by Bacteriophage Mu.
Main Methods:
- X-ray crystallography was used to determine the three-dimensional structure of gp52.
- Bioinformatic tools were employed for structural comparisons.
Main Results:
- The crystal structure of the alternative tail fiber subunit, gp52, was successfully determined.
- gp52 exhibits distinct structural motifs compared to other characterized tail fibers.
- These structural differences are crucial for recognizing diverse host cell surfaces.
Conclusions:
- Bacteriophage Mu employs structurally divergent tail fibers for host specificity.
- The distinct motifs in gp52 and gp49 facilitate recognition of different bacterial hosts.
- Understanding these structures provides insights into phage-host interactions and evolution.
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