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Structural Basis for Cell-Wall Recognition by Bacteriophage PBC5 Endolysin.
Ko On Lee1, Minsuk Kong2, Iktae Kim2
1Department of Agricultural Biotechnology and Research Institute of Agriculture and Life Sciences, Seoul National University, Seoul 08826, South Korea; Protein Structure Research Team, Korea Basic Science Institute, 162 Yeongudanji-Ro, Ochang-Eup, Cheongju-Si, Chungcheongbuk-Do 28119, South Korea.
Structure (London, England : 1993)
|July 30, 2019
Summary
Phage endolysins like LysPBC5 target bacterial cell walls. This study reveals how LysPBC5’s cell-wall binding domain specifically recognizes Bacillus cereus peptidoglycan structure for effective lysis.
Area of Science:
- Microbiology
- Structural Biology
- Biochemistry
Background:
- Phage endolysins are enzymes that degrade bacterial cell walls, offering potential antimicrobial applications.
- Bacillus cereus is a significant foodborne pathogen.
- Understanding endolysin-peptidoglycan interactions is key to developing novel antibacterial strategies.
Purpose of the Study:
- To elucidate the molecular mechanism of interaction between the endolysin LysPBC5 and the peptidoglycan of Bacillus cereus.
- To characterize the structure and function of the LysPBC5 cell-wall binding domain (CBD).
Main Methods:
- Isolation of bacteriophage PBC5 targeting Bacillus cereus.
- Structural analysis of LysPBC5 CBD using X-ray crystallography and solution scattering.
- Biochemical assays to determine binding interactions with peptidoglycan.
Main Results:
- LysPBC5 possesses an N-terminal glycoside hydrolase domain and a C-terminal CBD.
- The CBD features tandem SH3b domains that bind peptidoglycan via distal β sheet motifs in a bidentate manner.
- Binding specificity is attributed to interactions with the peptidoglycan glycan strand, not peptide cross-links.
Conclusions:
- The structure of the LysPBC5 CBD explains its high affinity and host specificity for Bacillus cereus.
- Endolysin recognition of bacterial peptidoglycan tertiary structure, specifically the glycan strand, is crucial for lysis.
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