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J. Biol. Chem., Vol. 268, Issue 5, 3334-3341, Feb, 1993
N Arora and SH Leppla
Anthrax lethal toxin is a complex of protective antigen (PA, 735 amino
acids) and lethal factor (LF, 776 amino acids) that lyses certain
eukaryotic cells. LF interacts with PA to gain access to the cytosol to
assert its toxicity. The internalization of LF requires that PA bind to a
specific membrane receptor and be cleaved by a cell-surface protease
(probably furin), so as to expose a site on PA to which LF binds with high
affinity. To localize LF functional domains, amino, carboxyl, and internal
deletions of LF were made. Toxicity was eliminated by deletion of 40 and 47
residues from the amino and carboxyl termini, respectively. Similarly,
deleting the first of the four imperfect repeats of 19 amino acids located
at residues 308-383 made LF non- toxic, showing that this region is also
essential for activity. To identify the minimum region of LF which is
required for binding to PA, varying amino-terminal portions of LF were
fused to the ADP- ribosylation domain of Pseudomonas exotoxin A. Fusion
proteins containing residues 1-254 of LF were toxic when administered with
PA, while those having only residues 1-198 of LF were inactive, showing
that the PA-binding domain of LF lies within residues 1-254.
Residues 1-254 of anthrax toxin lethal factor are sufficient to cause cellular uptake of fused polypeptides
Laboratory of Microbial Ecology, National Institute of Dental Research, National Institutes of Health, Bethesda, Maryland 20892.
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