Difference between revisions of "Part:BBa K5184045"

 
 
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G1M5-NbVP2F-His is a fusion protein of venom peptide that is identified in the transcriptome of the predatory mite Neoseiulus barkeri in [1] and the secretion signal peptide G1M5. 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."
 
G1M5-NbVP2F-His is a fusion protein of venom peptide that is identified in the transcriptome of the predatory mite Neoseiulus barkeri in [1] and the secretion signal peptide G1M5. 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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NbVP2F is the full-length version of the N. barkeri venom peptide 2, composing 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. The cysteine network of the peptide has the structure of C1xxxC2xxxC3C4xxxC5xC6xxxC7xC8, with disulfide bridges between C1C4, C2C5, C3C8, and C6C7.
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Via signal peptide prediction results using DeepLoc 2.1, it is believed that there is a signal peptide at its C-terminus, and one at the 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 moderate toxicity against T. urticae, the two spotted spider mite that is a global pest against a huge range of host plants, as shown in the paper that first describes the peptide [1]"
 
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<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>

Latest revision as of 07:49, 27 September 2024


G1M5-NbVP2F-His

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

G1M5-NbVP2F-His is a fusion protein of venom peptide that is identified in the transcriptome of the predatory mite Neoseiulus barkeri in [1] and the secretion signal peptide G1M5. 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

NbVP2F is the full-length version of the N. barkeri venom peptide 2, composing 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. The cysteine network of the peptide has the structure of C1xxxC2xxxC3C4xxxC5xC6xxxC7xC8, with disulfide bridges between C1C4, C2C5, C3C8, and C6C7.

Via signal peptide prediction results using DeepLoc 2.1, it is believed that there is a signal peptide at its C-terminus, and one at the 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 moderate toxicity against T. urticae, the two spotted spider mite that is a global pest against a huge range of host plants, as shown in the paper that first describes the peptide [1]" 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]