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Bordetella dermonecrotic toxin binds to target cells via the N‐terminal 30 amino acids
Author(s) -
FukuiMiyazaki Aya,
Ohnishi Shinya,
Kamitani Shigeki,
Abe Hiroyuki,
Horiguchi Yasuhiko
Publication year - 2011
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.2010.00300.x
Subject(s) - furin , cleavage (geology) , biology , toxin , amino acid , biochemistry , anthrax toxin , cytoplasm , binding domain , binding site , protease , recombinant dna , fusion protein , gene , paleontology , fracture (geology) , enzyme
Bordetella dermonecrotic toxin (DNT) affects the biological function of host cells by activating intracellular Rho GTPases. The toxin binds to unidentified receptor(s) via 54 N‐terminal amino acids, undergoes intramolecular cleavage on the C‐terminal side of Arg 44 by furin or furin‐like protease, and eventually enters the cytoplasm where the Rho GTPases reside. The binding to the receptor(s) and intramolecular cleavage are essential for DNT to intoxicate cells, and the 54 amino‐acid binding domain encompasses the cleavage site, however, it is unclear whether these two events are related. In this study, we could narrow down the cell‐binding domain to the N‐terminal amino acids 2–30. The region does not contain the furin‐recognition site, indicating that the cell binding and the intramolecular cleavage are independent events.