Appeal No. 2004-1505 Page 5
Application No. 09/016,743
Hölzer describes a complete antibody having heavy and light chains each with
an N-terminus and being capable of specifically binding to a tumor cell associated
antigen. See, e.g., column 3, lines 22-26. The complete antibody of Hölzer is coupled
to a chemokine, e.g., IL-8. Id. However, the chemokine of Hölzer is coupled to the C-
terminus of the complete antibody, not the N-terminus as required by claim 1 on appeal.
See, e.g., the third construct illustrated in Fig. 1 of Hölzer.
Hölzer states that the biological activity of IL-8 is associated with the N-terminal
portion of the molecule. Id., column 7, lines 41-51. Thus, in forming the chimeric
molecules of that invention, the question arose as to whether coupling the N-terminal
portion of the IL-8 molecule to the C-terminal portion of the complete antibody would
abrogate the biological activity of IL-8. Hölzer avoided the possibility of this problem by
providing linker peptides between the C-terminal of the complete antibody and the N-
terminal portion of the IL-8 molecule. Id.
Huston describes chimeric molecules formed of single-chain Fv antibody
fragments and proteins that are denominated as effector proteins. Huston, page 48.
The single-chain Fv fragment “forms the entire antibody combining site.” Id., page 47.
A fusion protein comprising a single-chain Fv fragment and an effector protein is of
interest in in vivo diagnostics and therapeutics. Id., page 48. Of particular interest is
Huston’s discovery that effector proteins can be attached to either the N-terminus or the
C-terminus of the single-chain Fv fragment with the resulting fusion protein retaining the
binding properties of the Fv antibody fragment. See, e.g., Figure 3 and page 57 of
Huston.
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