Abstract：
:We characterized an anti-cancer fusion protein consisting of anthrax lethal factor (LF) and the catalytic domain of Pseudomonas exotoxin A by (i) mutating the N-terminal amino acids and by (ii) reductive methylation to dimethylate all lysines. Dimethylation of lysines was achieved quantitatively and specifically without affecting binding of the fusion protein to PA or decreasing the enzymatic activity of the catalytic moiety. Ubiquitination in vitro was drastically decreased for both the N-terminally mutated and dimethylated variants, and both appeared to be slightly more stable in the cytosol of treated cells. The dimethylated variant showed greatly reduced neutralization by antibodies to LF. The two described modifications offer unique advantages such as increased cytotoxic activity and diminished antibody recognition, and thus may be applicable to other therapeutic proteins that act in the cytosol of cells.
journal_name
Sci Repjournal_title
Scientific reportsauthors
Bachran C,Gupta PK,Bachran S,Leysath CE,Hoover B,Fattah RJ,Leppla SHdoi
10.1038/srep04754subject
Has Abstractpub_date
2014-04-23 00:00:00pages
4754issn
2045-2322pii
srep04754journal_volume
4pub_type
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