US 11,939,368 B2
QTY Fc fusion receptor proteins
Shuguang Zhang, Cambridge, MA (US); David Jin, Staten Island, NY (US); Rui Qing, Somerville, MA (US); and Uwe Sleytr, Vienna (AT)
Assigned to Massachusetts Institute of Technology, Cambridge, MA (US); and Avalon GloboCare Corp., Freehold, NJ (US)
Filed by Massachusetts Institute of Technology, Cambridge, MA (US); and Avalon GloboCare Corp., Freehold, NJ (US)
Filed on Jul. 29, 2022, as Appl. No. 17/877,091.
Application 17/877,091 is a continuation of application No. 17/210,878, filed on Mar. 24, 2021, granted, now 11,401,320.
Claims priority of provisional application 63/048,730, filed on Jul. 7, 2020.
Claims priority of provisional application 63/002,666, filed on Mar. 31, 2020.
Prior Publication US 2023/0124436 A1, Apr. 20, 2023
This patent is subject to a terminal disclaimer.
Int. Cl. C07K 14/715 (2006.01); A61K 38/17 (2006.01); A61K 45/06 (2006.01); A61K 38/00 (2006.01)
CPC C07K 14/7158 (2013.01) [A61K 38/177 (2013.01); A61K 45/06 (2013.01); A61K 38/00 (2013.01); C07K 2319/03 (2013.01); C07K 2319/30 (2013.01)] 4 Claims
 
1. A Fc fusion QTY CCR9 variant receptor protein comprising a Fc domain and a QTY CCR9 variant receptor domain; wherein the QTY CCR9 variant receptor domain comprises a QTY transmembrane region characterized by an alpha helix: and wherein all of the leucines (L) in a transmembrane domain of a wild type CCR9 sequence are replaced with glutamines (Q) and all of the valines (V) in the transmembrane domain of the wild type sequence are replaced with threonines (T) and all of the isoleucines (I) in the transmembrane domain of the wild type sequence are replaced with threonines (T) and all of the phenylalanines (F) in the transmembrane domain of the wild type sequence are replaced with tyrosines (Y).