Glycosylated VEGF decoy receptor fusion protein

1. A VEGF decoy fusion polypeptide that synchronously binds to VEGF polypeptide and placenta growth factor (PIGF) polypeptide, comprising parental VEGFR1 second and third immunoglobulin (Ig)-like domains, wherein at least one positive amino acid residue in the third domain of VEGFR1 is mutated to a negatively charged residue so as to comprise a glycosylation site.

2. The polypeptide according to claim 1 , which is linked to a multimerizing component.

3. The polypeptide according to claim 1 , wherein the amino acid residue is on the β1-β2 loop, which comprises amino acid residues that are expressed from nucleic acid positions 397 to 432 of SEQ ID NO:1 corresponding to amino acid residues 133 to 144 of SEQ ID NO: 2, or β3-β4 loop, which comprises amino acid residues that are expressed from nucleic acid positions 490 to 522 of SEQ ID NO:1 corresponding to amino acid residues 164 to 174 of SEQ ID NO: 2.

4. The polypeptide according to claim 3 , wherein the residue to be mutated is R135 residue on the β1-β2 loop, K138 residue on the β1-β2 loop, or R172 residue on the β3-β4 loop on the third domain.

5. The polypeptide according to claim 4 , wherein the residue to be mutated is R135 residue on the β1-β2 loop and K138 residue on the β1-β2 loop on the third domain.

6. The polypeptide according to claim 4 , wherein the residue to be mutated is R135 residue on the β1-β2 loop, K138 residue on the β1-β2 loop, and R172 residue on the β3-β4 loop on the third domain.

7. The polypeptide according to claim 1 , wherein the polypeptide is glycosylated.

8. The polypeptide according to claim 1 , wherein the polypeptide is sialylated.

9. The polypeptide according to claim 1 , wherein the polypeptide exhibits a decrease in net pI of the polypeptide compared to that which has not been mutated.