Difference between revisions of "Part:BBa K5184040"

 
 
Line 3: Line 3:
 
<partinfo>BBa_K5184040 short</partinfo>
 
<partinfo>BBa_K5184040 short</partinfo>
  
−
"NbSVP1-S is a venom peptide identified in Neoseiulus barkeri, a predatory mite. It is first identified in this paper [1], where it shows lethality against T. cinnabarinus, a synoym of 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.
+
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.
−
With structure prediction using Alphafold Server, we identified the highly conserved core domain that is responsible for the peptide's toxicity, and removed all other domains, to achieve higher expression rates."
+
 
 +
Abstract
 +
 
 +
G1M5-NbVP1S-His is the fusion protein of modified version of the venom peptide first identified in the transcriptome of the predatory mite Neoseiulus barkeri[] and the G1M5 secretion signal peptide. 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.
  
−
<!-- Add more about the biology of this part here
 
 
===Usage and Biology===
 
===Usage and Biology===
 +
"
 +
Biology
 +
 +
NbVP1S is the truncated version of the N. barkeri venom peptide 1, 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. The cysteine network of the peptide has the structure of C1xxxC2xxxC3C4xxxC5xC6xxxC7xC8, with disulfide bridges between C1C4, C2C5, C3C8, and C6C7.
 +
 +
Comparing to the full-length NbVP1F, 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. 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 should show higher toxicity against T. urticae, the two spotted spider mite that is a global pest against a huge range of host plants, comparing to NbVP1F since only the venomous domain is left out."
 
<!-- -->
 
<!-- -->
 
<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>

Latest revision as of 11:20, 27 September 2024


NbVP1-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

G1M5-NbVP1S-His is the fusion protein of modified version of the venom peptide first identified in the transcriptome of the predatory mite Neoseiulus barkeri[] and the G1M5 secretion signal peptide. 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

NbVP1S is the truncated version of the N. barkeri venom peptide 1, 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. The cysteine network of the peptide has the structure of C1xxxC2xxxC3C4xxxC5xC6xxxC7xC8, with disulfide bridges between C1C4, C2C5, C3C8, and C6C7.

Comparing to the full-length NbVP1F, 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. 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 should show higher toxicity against T. urticae, the two spotted spider mite that is a global pest against a huge range of host plants, comparing to NbVP1F since only the venomous domain is left out." 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]