Difference between revisions of "Part:BBa K5184039"

 
 
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<partinfo>BBa_K5184039 short</partinfo>
 
<partinfo>BBa_K5184039 short</partinfo>
  
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PpSVP2-F is a venom peptide from Phytoseiulus persimilis, a predatory mite whose main prey is  T. urticae. The coding sequence of this venom peptide is identified by gene alignment of NbSVP2(Bka:xxxxx) against the P. persimilis genome (GenBank: GCA_037576195.1). With the exons filtered out, the coding sequence is identified. 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.
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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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PpVP2F is a venom peptide identified in the genome of the predatory mite Phytoseiulus persimilis using BLAST. 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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PpVP2F is the full-length version of the P. persimilis venom peptide that is homologous to NbVP2F. It is composed of a total of 186 amino acids. It contains a total of 9 cysteine residues, 8 of which are involved in the 4 disulfide bridges that form the backbone of the peptide’s core venomous domain. Comparing its core venomous domain to that of the N. barkeri homolog, the P. persimilis venom peptide has the same set of cysteine network of C1xxxC2xxxC3C4xxxC5xC6xxxC7xC8, with disulfide bridges between C1C4, C2C5, C3C8, and C6C7, and therefore shares an almost congruent geometry, differing by only 5 amino acids.
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Via signal peptide prediction results using DeepLoc 2.1, we believe there is a signal peptide at its C-terminus and another at its N-terminus, targeting the peptide for extracellular secretion. The peptide is believed to block insect voltage gated calcium channels and presumably nicotinic acetylcholine receptors (as proposed by [2]) to interfere with the neuron’s normal function.
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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 extremely high toxicity against T. urticae comparing all other mite venom peptides."
 
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<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>

Latest revision as of 11:16, 27 September 2024


PpVP2-F

" 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 PpVP2F is a venom peptide identified in the genome of the predatory mite Phytoseiulus persimilis using BLAST. 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

PpVP2F is the full-length version of the P. persimilis venom peptide that is homologous to NbVP2F. It is composed of a total of 186 amino acids. It contains a total of 9 cysteine residues, 8 of which are involved in the 4 disulfide bridges that form the backbone of the peptide’s core venomous domain. Comparing its core venomous domain to that of the N. barkeri homolog, the P. persimilis venom peptide has the same set of cysteine network of C1xxxC2xxxC3C4xxxC5xC6xxxC7xC8, with disulfide bridges between C1C4, C2C5, C3C8, and C6C7, and therefore shares an almost congruent geometry, differing by only 5 amino acids.

Via signal peptide prediction results using DeepLoc 2.1, we believe there is a signal peptide at its C-terminus and another at its N-terminus, targeting the peptide for extracellular secretion. The peptide is believed to block insect voltage gated calcium channels and presumably nicotinic acetylcholine receptors (as proposed by [2]) to interfere with the neuron’s normal function.

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 extremely high toxicity against T. urticae comparing all other mite venom peptides." 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]