Publications by authors named "Karlygash G Aimanova"

Bacillus thuringiensis subsp. israelensis (Bti) is widely used for the biological control of mosquito populations. However, the mechanism of Bti toxins is still not fully understood.

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Cadherin plays an important role in the toxicity of Bacillus thuringiensis Cry proteins. We previously cloned a full-length cadherin from Aedes aegypti larvae and reported this protein binds Cry11Aa toxin from B. thuringiensis subsp.

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Article Synopsis
  • The Cry11Aa protein, produced by Bacillus thuringiensis israelensis, effectively targets Aedes aegypti larvae by binding to specific receptors in the larvae's midgut.
  • The aminopeptidase N protein, AaeAPN2, was identified as a key binding partner for Cry11Aa, showing a high affinity for the toxin and localizing in the larvae's epithelial cells.
  • Experiments demonstrated that AaeAPN2 enhances the toxicity of Cry11Aa in larval bioassays, confirming its role as a critical binding protein in the Cry11Aa mechanism of action.
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After anautogenous mosquitoes ingest the required blood meal, proteins in it are rapidly cleaved, yielding a large pool of amino acids. Transport of these amino acids into gut epithelial cells and their subsequent translocation into other tissues is critical for oogenesis and other physiological processes. We have identified a proton amino acid transporter (PAT) in Aedes aegypti (AaePAT1, AAEL007191) which facilitates this transport and is expressed in epithelial cell membranes of larval caecae and the adult midgut.

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Cry11Aa of Bacillus thuringiensis subsp. israelensis is the most active toxin to Aedes aegypti in this strain. We previously reported that, in addition to a 65 kDa GPI (glycosylphosphatidylinositol)-anchored ALP (alkaline phosphatase), the toxin also binds a 250 kDa membrane protein.

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Article Synopsis
  • Bacillus thuringiensis subsp. israelensis produces toxins, like Cry11Aa, to control Aedes aegypti larvae by targeting their gut cells during sporulation.
  • In a study, a specific protein called AaeAPN1, which interacts with Cry11Aa, was isolated from Aedes larvae midgut membranes and identified as an aminopeptidase N.
  • The full-length AaeAPN1 was successfully expressed in two different systems; while one version was enzymatically active, it didn't bind Cry11Aa, whereas a truncated version did bind with high affinity.
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Using a Cry11Ba toxin model, predicted loops in domain II were analyzed for their role in receptor binding and toxicity. Peptides corresponding to loops alpha8, 1 and 3, but not loop 2, competed with toxin binding to Aedes midgut membranes. Mutagenesis data reveal loops alpha8, 1 and 3 are involved in toxicity.

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Following a blood meal, the mosquito Aedes aegypti will have acquired an enormous sodium load that must be rapidly excreted to restore ion homeostasis. It is a process that demands robust sodium and fluid transport capabilities. Even though the identities of the components involved in this ion transport across the mosquito Malpighian tubule epithelia have not been completely determined, electrophysiological studies suggest the contribution of a Na(+)/H(+) exchanger extruding cations into the lumen driven secondarily by the proton gradient created by the V-type H(+)-ATPase in the tubules' apical membrane.

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Cadherin-like proteins have been identified as putative receptors for the Bacillus thuringiensis Cry1A proteins in Heliothis virescens and Manduca sexta. Immunohistochemistry showed the cadherin-like proteins are present in the insect midgut apical membrane, which is the target site of Cry toxins. This subcellular localization is distinct from that of classical cadherins, which are usually present in cell-cell junctions.

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Article Synopsis
  • A 65 kDa GPI-anchored alkaline phosphatase (ALP) was identified as a functional receptor for the Cry11Aa toxin in Aedes aegypti (mosquito) midgut cells.
  • Two GPI-anchored proteins that interact with the Cry11Aa toxin were extracted and the 65 kDa protein was further purified, revealing its ALP activity.
  • The distribution of GPI-ALP in the midgut was mapped, showing it predominantly in the posterior region, where it competes with the Cry11Aa toxin, affecting the toxin's effectiveness on mosquito larvae.
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