Difference between revisions of "Part:BBa K5184042"

 
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<partinfo>BBa_K5184042 short</partinfo>
 
<partinfo>BBa_K5184042 short</partinfo>
  
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PpVP1-S is the shorter version of a venom peptide from Phytoseiulus persimilis, a predatory mite mainly preys on  T. urticae. In our project, this protein's production is aimed to produce a more potent and specific venom peptide against the red spider mite, T. urticae. The coding sequence of this venom peptide is identified by gene alignment of NbSVP1(Bka:xxxxx) against the P. persimilis genome (GenBank: GCA_037576195.1). With the exons filtered out, the coding sequence is identified. With structure prediction results from Alphafold Server, the protein is modifed from PpVP2-F via truncation of ()aa on N-terminus and ()aa on the C-terminus ti achieve higher expression rate and possibly better toxicity.
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In our project we employ venom peptides to act as insecticidal agents against T. urticae a global ubiquitous pest. This part presents a mite venom peptide with higher specificity and potency against the spider mite comparing to spider venom peptides. This mite venom peptide may also aid future iGEM teams in identifying homologous venom peptide genes in the acari family that is, right now, currently almost completely unexplored.
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Abstract
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PpVP1S is the modified version of the venom peptide identified in the genome of the predatory mite Phytoseiulus persimilis. Via phylogenic analysis, we believe it achieves its paralyzing and insecticidal properties by interfering with voltage gated calcium channels whose affinity towards is illustrated by computer modelling.
  
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===Usage and Biology===
 
===Usage and Biology===
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Biology
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PpVP1S is the truncated version of the PpVP1F, composing of a total of 45 amino acids. It contains 8 cysteine residues to form 4 disulfide bridges that gives the peptide a unique geometry that allows it to achieve its toxicity. Comparing to the full-length PpVP1F all regions except from the core venomous domain had been truncated with matched core venom domain of known venom peptides as guidance, to enhance expression rate and solubility. It has the same set of cysteine network of C1xxxC2xxxC3C4xxxC5xC6xxxC7xC8, with disulfide bridges between C1C4, C2C5, C3C8, and C6C7, comparing to NbVP1 and therefore shares an almost congruent geometry, differing by only 3 amino acids.
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This venom peptide achieves its effects by interfering with voltage gated calcium channels and presumably nicotinic acetylcholine receptors (as proposed by [2]), and therefore blocks relay of neural impulse across synapses.
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The G1M5 tag is a secretion tag utilizing the Sec pathway, a common extracellular secretion system seen across all domains of life; it is fused with the venom peptide to allow extracellular secretion of the peptide, thus decreasing its production costs.
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Features
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Non-toxic to humans/mammals: Due to the venom peptide’s high specificity and the structural differences of its binding site in insect and mammal ion channels
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It shows higher toxicity against T. urticae, the two spotted spider mite that is a global pest against a huge range of host plants.
  
 
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Revision as of 11:23, 27 September 2024


PpVP1-S

In our project we employ venom peptides to act as insecticidal agents against T. urticae a global ubiquitous pest. This part presents a mite venom peptide with higher specificity and potency against the spider mite comparing to spider venom peptides. This mite venom peptide may also aid future iGEM teams in identifying homologous venom peptide genes in the acari family that is, right now, currently almost completely unexplored.

Abstract PpVP1S is the modified version of the venom peptide identified in the genome of the predatory mite Phytoseiulus persimilis. Via phylogenic analysis, we believe it achieves its paralyzing and insecticidal properties by interfering with voltage gated calcium channels whose affinity towards is illustrated by computer modelling.

Usage and Biology

Biology

PpVP1S is the truncated version of the PpVP1F, composing of a total of 45 amino acids. It contains 8 cysteine residues to form 4 disulfide bridges that gives the peptide a unique geometry that allows it to achieve its toxicity. Comparing to the full-length PpVP1F all regions except from the core venomous domain had been truncated with matched core venom domain of known venom peptides as guidance, to enhance expression rate and solubility. It has the same set of cysteine network of C1xxxC2xxxC3C4xxxC5xC6xxxC7xC8, with disulfide bridges between C1C4, C2C5, C3C8, and C6C7, comparing to NbVP1 and therefore shares an almost congruent geometry, differing by only 3 amino acids.

This venom peptide achieves its effects by interfering with voltage gated calcium channels and presumably nicotinic acetylcholine receptors (as proposed by [2]), and therefore blocks relay of neural impulse across synapses.

The G1M5 tag is a secretion tag utilizing the Sec pathway, a common extracellular secretion system seen across all domains of life; it is fused with the venom peptide to allow extracellular secretion of the peptide, thus decreasing its production costs.

Features

Non-toxic to humans/mammals: Due to the venom peptide’s high specificity and the structural differences of its binding site in insect and mammal ion channels It shows higher toxicity against T. urticae, the two spotted spider mite that is a global pest against a huge range of host plants.

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]