Difference between revisions of "Part:BBa K4960016"
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===Usage and Biology=== | ===Usage and Biology=== | ||
| − | PVCs are eCISs produced by members of the genus Photorhabdus, which exist as endosymbionts within entomopathogenic nematodes. As a toxin, PVC targets the host insect, delivering the PVC payload Pdp1 and Pnf to kill the insect[1]. The toxin is responsible for the cytotoxicity towardsthe eukaryotic cells on the basis of its dNTP pyrophosphataseactivity. [2] | + | PVCs are eCISs produced by members of the genus Photorhabdus, which exist as endosymbionts within entomopathogenic nematodes. As a toxin, PVC targets the host insect, delivering the PVC payload Pdp1 and Pnf to kill the insect[1].<br> |
| − | Pdp1(Photorhabdus dNTP pyrophosphatase 1) is a widespread dual-localized pyrophosphatase toxin ,containing a predicted N-terminal packaging domain. The N-terminal domain (NTD) of Pdp1 is likely disordered as it exhibits a low pLDDT score in AlphaFold (it appears as a long disordered extension in the protein’s predicted structure) as well as a high PONDR VSL2 score49. This N-terminal disordered region could serve as a “packaging domain”—a molecular identifier to assist the PVCs loading machinery in identifying and loading the proper payloads [3]. | + | The toxin is responsible for the cytotoxicity towardsthe eukaryotic cells on the basis of its dNTP pyrophosphataseactivity. [2]<br> |
| − | N-terminal packaging domains of Pdp1 and Pnf are necessary and sufficient for loading of these proteins into a PVC particle. | + | Pdp1(Photorhabdus dNTP pyrophosphatase 1) is a widespread dual-localized pyrophosphatase toxin ,containing a predicted N-terminal packaging domain. The N-terminal domain (NTD) of Pdp1 is likely disordered as it exhibits a low pLDDT score in AlphaFold (it appears as a long disordered extension in the protein’s predicted structure) as well as a high PONDR VSL2 score49. This N-terminal disordered region could serve as a “packaging domain”—a molecular identifier to assist the PVCs loading machinery in identifying and loading the proper payloads [3].<br> |
| + | N-terminal packaging domains of Pdp1 and Pnf are necessary and sufficient for loading of these proteins into a PVC particle.<br> | ||
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===Sequencing=== | ===Sequencing=== | ||
Revision as of 18:49, 10 October 2023
Pdp1-NTD
N-peptide that guides payload loading
Usage and Biology
PVCs are eCISs produced by members of the genus Photorhabdus, which exist as endosymbionts within entomopathogenic nematodes. As a toxin, PVC targets the host insect, delivering the PVC payload Pdp1 and Pnf to kill the insect[1].
The toxin is responsible for the cytotoxicity towardsthe eukaryotic cells on the basis of its dNTP pyrophosphataseactivity. [2]
Pdp1(Photorhabdus dNTP pyrophosphatase 1) is a widespread dual-localized pyrophosphatase toxin ,containing a predicted N-terminal packaging domain. The N-terminal domain (NTD) of Pdp1 is likely disordered as it exhibits a low pLDDT score in AlphaFold (it appears as a long disordered extension in the protein’s predicted structure) as well as a high PONDR VSL2 score49. This N-terminal disordered region could serve as a “packaging domain”—a molecular identifier to assist the PVCs loading machinery in identifying and loading the proper payloads [3].
N-terminal packaging domains of Pdp1 and Pnf are necessary and sufficient for loading of these proteins into a PVC particle.
Sequencing
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
References
[1] Yang, G., Dowling, A. J., Gerike, U., ffrench-Constant, R. H. & Waterfield, N. R.
Photorhabdus virulence cassettes confer injectable insecticidal activity against the wax
moth. J. Bacteriol. 188, 2254–2261 (2006).
[2] Wang X, Cheng J, Shen J, Liu L, Li N, Gao N, Jiang F, Jin Q. Characterization of Photorhabdus Virulence Cassette as a causative agent in the emerging pathogen Photorhabdus asymbiotica. Sci China Life Sci. 2022 Mar;65(3):618-630.
[3] Kreitz, J., Friedrich, M.J., Guru, A. et al. Programmable protein delivery with a bacterial contractile injection system. Nature 616, 357–364 (2023).