Difference between revisions of "Part:BBa K5184033"

Revision as of 11:10, 27 September 2024

HxTx-Hv1h

In order to eliminate T.urticae of infested cultivations, spider venom peptide G1M5-HxTx-Hv1h-his is incorporated in our project with pesticidal means. HxTx-Hv1h is a small cysteine-rich venom peptide derived from Blue mountains funnel-web spiders Hadronyche versuta. In nature, utilized as predatory toxin, it carries the ability to cause paralysis and death in susceptible subjects by targeting both calcium ion channels and potassium ion channels of them. Though its strong activity on certain invertebrates, it is proven no harm to non-pest insects such as Dalotia coriaria, Orius insidiosus, and pollinating bees of genus Apis. Having both ion channels playing a fundamental role in the neuronal system, targets experience fast immobilization after envenomation, thus it serves as an effective pesticide. Due to the cysteine-rich nature of HxTx-Hv1h, expression strategy that exterminates inclusion bodies is required, thus a G1M5 secretion system is engineered with HxTx-Hv1h to achieve this. Considering future pesticidal control, G1M5-HxTx-Hv1h-his can provide future iGEM teams that dedicate in exterminating other destructive pests more choices of sustainable pesticide that could be expressed correctly in Escherichia Coli.

Usage and Biology

Paralysis and mortal effects of susceptible subjects are achieved via HxTx-Hv1h target on nicotinic Acetylcholine receptors (nAChRs), voltage-activated calcium ion channel (Cav) and calcium ion activated potassium ion channels (Kca) of targets. G1M5 is the mutated, less hydrophobic version of the secretion signal peptide of the G1 cyclomaltodextrin glucanotransferase (CGtase) of Bacillus sp., which allows the extracellular secretion of the bacterial enzyme. Conduction of proteins attached by G1M5 out of the cytosol is achieved by the Sec pathway, a very common secretion system seen in all three major domains of life: arachaea, prokaryote, and eukaryotes. Once the signal peptide, in this case G1M5 is synthesized, the protein chaperon SecB binds to the preprotein (that is attached to G1M5), and transfers the preprotein to the protein translocase SecA, of which binds to the membrane bound protein conducting channel SecYEG. Once bound to the membrane, SecA binds to a molecule of ATP, of which is hydrolyzed to conduct the protein through heterotrimer complex of SecYEG. A membrane bound SPaseI then, once enough of the preprotein had been conducted through the channel, will remove the SP and allow the preprotein to fold properly into the correct protein.

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]

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 <partinfo>BBa_K5184033 short</partinfo>
-HxTx-Hv1h is a small cysteine-rich venom peptide derived from Blue mountains funnel-web spiders Hadronyche versuta.  In nature, utilized as predatory toxin, it carries the ability to cause paralysis and death in susceptible subjects by targeting both calcium ion channels and potassium ion channels of susceptible targets. Though its strong activity on certain invertebrates, it is proven no harm to non-pest insects such as Dalotia coriaria, Orius insidiosus, and pollinating bees of genus Apis. In the context of our project, HxTx-Hv1h is utilized as a sustainable pesiticide to eliminate spider mites on infectious cultivations by targeting their ion channels. It is expressed via Escherichia.coli strand OrigamiB and injected into crickets to test mortal effects.
+In order to eliminate T.urticae of infested cultivations, spider venom peptide G1M5-HxTx-Hv1h-his is incorporated in our project with pesticidal means. HxTx-Hv1h is a small cysteine-rich venom peptide derived from Blue mountains funnel-web spiders Hadronyche versuta. In nature, utilized as predatory toxin, it carries the ability to cause paralysis and death in susceptible subjects by targeting both calcium ion channels and potassium ion channels of them. Though its strong activity on certain invertebrates, it is proven no harm to non-pest insects such as Dalotia coriaria, Orius insidiosus, and pollinating bees of genus Apis. Having both ion channels playing a fundamental role in the neuronal system, targets experience fast immobilization after envenomation, thus it serves as an effective pesticide. Due to the cysteine-rich nature of HxTx-Hv1h, expression strategy that exterminates inclusion bodies is required, thus a G1M5 secretion system is engineered with HxTx-Hv1h to achieve this. Considering future pesticidal control, G1M5-HxTx-Hv1h-his can provide future iGEM teams that dedicate in exterminating other destructive pests more choices of sustainable pesticide that could be expressed correctly in Escherichia Coli.
-<!-- Add more about the biology of this part here
 ===Usage and Biology===
+Paralysis and mortal effects of susceptible subjects are achieved via HxTx-Hv1h target on nicotinic Acetylcholine receptors (nAChRs), voltage-activated calcium ion channel (Cav) and calcium ion activated potassium ion channels (Kca) of targets. G1M5 is the mutated, less hydrophobic version of the secretion signal peptide of the G1 cyclomaltodextrin glucanotransferase (CGtase) of Bacillus sp., which allows the extracellular secretion of the bacterial enzyme. Conduction of proteins attached by G1M5 out of the cytosol is achieved by the Sec pathway, a very common secretion system seen in all three major domains of life: arachaea, prokaryote, and eukaryotes. Once the signal peptide, in this case G1M5 is synthesized, the protein chaperon SecB binds to the preprotein (that is attached to G1M5), and transfers the preprotein to the protein translocase SecA, of which binds to the membrane bound protein conducting channel SecYEG. Once bound to the membrane, SecA binds to a molecule of ATP, of which is hydrolyzed to conduct the protein through heterotrimer complex of SecYEG. A membrane bound SPaseI then, once enough of the preprotein had been conducted through the channel, will remove the SP and allow the preprotein to fold properly into the correct protein.
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