Adenoviral-mediated cell targeting commanded by the adenovirus penton base protein
AssigneeGenVec, Inc.
InventorsThomas J. Wickham, Imre Kovesdi, Petrus W. Roelvink, Douglas E. Brough, Duncan L. McVey, Joseph T. Bruder
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Abstract
A method of introducing an adenovirus into a cell that comprises a particular cell surface binding site, as well as a chimeric adenovirus penton base protein and recombinant adenoviral vector comprising the chimeric adenovirus penton base protein for use in the method, are provided.
Claims52
A method of introducing an adenovirus into a cell in vitro, said cell comprising a particular cell surface binding site, which method comprises:
- (a) contacting said adenovirus with a bispecific molecule comprising (i) a first component that selectively binds a binding domain of the penton base protein of said adenovirus, and (ii) a second component that selectively binds said particular cell surface binding site, to form a complex of said adenovirus and said bispecific molecule, and
- (b) contacting said cell with said complex such that cell entry of said adenovirus is effected.
A method of introducing an adenovirus into a cell in vitro, said cell comprising a particular cell surface binding site, which method comprises:
- (a) abrogating the binding of the fiber protein of said adenovirus to any cell surface molecule to which the fiber protein of said adenovirus can bind to effect cell entry of said adenovirus, and
- (b) contacting said cell with said adenovirus such that the penton base protein of said adenovirus binds said particular cell surface binding site and cell entry of said adenovirus is effected.
A chimeric adenovirus penton base protein comprising a binding domain that differs from the binding domain of a wild-type adenovirus penton base protein.
A vector comprising a chimeric adenovirus penton base protein that comprises a binding domain that differs from the binding domain of a wild-type adenovirus penton base protein, wherein said adenovirus further comprises a chimeric adenovirus fiber protein that comprises a protease cleavage site.
Dependencies are inferred from the claim text.