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PMID:24347545
| Citation |
Zhang, X, Guo, H, Jin, L, Czornyj, E, Hodes, A, Hui, WH, Nieh, AW, Miller, JF and Zhou, ZH (2013) A new topology of the HK97-like fold revealed in Bordetella bacteriophage by cryoEM at 3.5 A resolution. Elife 2:e01299 |
|---|---|
| Abstract |
Bacteriophage BPP-1 infects and kills Bordetella species that cause whooping cough. Its diversity-generating retroelement (DGR) provides a naturally occurring phage-display system, but engineering efforts are hampered without atomic structures. Here, we report a cryo electron microscopy structure of the BPP-1 head at 3.5 Å resolution. Our atomic model shows two of the three protein folds representing major viral lineages: jellyroll for its cement protein (CP) and HK97-like ('Johnson') for its major capsid protein (MCP). Strikingly, the fold topology of MCP is permuted non-circularly from the Johnson fold topology previously seen in viral and cellular proteins. We illustrate that the new topology is likely the only feasible alternative of the old topology. β-sheet augmentation and electrostatic interactions contribute to the formation of non-covalent chainmail in BPP-1, unlike covalent inter-protein linkages of the HK97 chainmail. Despite these complex interactions, the termini of both CP and MCP are ideally positioned for DGR-based phage-display engineering. DOI: http://dx.doi.org/10.7554/eLife.01299.001. |
| Links |
PubMed PMC3863775 Online version:10.7554/eLife.01299 |
| Keywords |
Amino Acid Sequence; Bacteriophages/chemistry; Bacteriophages/ultrastructure; Bordetella/virology; Cryoelectron Microscopy; Electrophoresis, Polyacrylamide Gel; Mass Spectrometry; Models, Molecular; Molecular Sequence Data; Protein Conformation; Viral Proteins/chemistry; Viral Proteins/ultrastructure |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0019012: virion |
ECO:0000314: |
C |
Figure 1 shows the results of mass spectrometry from the major band of a gel that was derived from whole phage particles. From the thick black line under part B on the top of the mass spectrometry, it is evident that Bbp16 is the second most abundant protein. Mass spectrometry confirmed that the sequence obtained from the second most abundant band corresponded to capsid protein. This is a virion component because whole phage components were run as a gel.The band migrating at 15.0 kD is around the size they expected based on the sequence of the capsid. |
complete | ||||
Notes
See also
References
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