Abstract
Pasteurella multocida toxin (PMT) is the causative agent of progressive atrophic rhinitis in swine. The 146 kDa single-chain toxin harbours discrete domains important for receptor binding, internalisation and biological activity. The molecular basis of the toxin's activity is the deamidation of a specific glutamine residue in the α-subunit of heterotrimeric G proteins. This results in an inhibition of the inherent GTPase activity leading to a constitutively active phenotype of the G protein. Due to the ability of the toxin to act on various families of heterotrimeric G proteins, a large subset of signal transduction pathways is stimulated.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Animals
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Bacterial Proteins / chemistry*
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism
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Bacterial Toxins / chemistry*
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Bacterial Toxins / genetics
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Bacterial Toxins / metabolism
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Glutamine / genetics
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Glutamine / metabolism
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Heterotrimeric GTP-Binding Proteins / chemistry
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Heterotrimeric GTP-Binding Proteins / genetics
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Heterotrimeric GTP-Binding Proteins / metabolism*
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Humans
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Models, Molecular
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Pasteurella Infections / genetics
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Pasteurella Infections / metabolism*
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Pasteurella Infections / microbiology
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Pasteurella multocida / genetics*
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Pasteurella multocida / metabolism
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Protein Binding
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Protein Structure, Tertiary
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Rhinitis, Atrophic / genetics
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Rhinitis, Atrophic / metabolism*
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Rhinitis, Atrophic / microbiology
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Signal Transduction / genetics
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Swine
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Up-Regulation
Substances
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Bacterial Proteins
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Bacterial Toxins
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Pasteurella multocida toxin
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Glutamine
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Heterotrimeric GTP-Binding Proteins