IP Library Granted Patent US 12,630,636
Granted Patent B2
US 12,630,636 · App. 17/734,239 · Granted May 19, 2026

Anti-FcRH5 antibodies

Inventors: Allen J. Ebens (San Carlos, CA); Meredith C. Hazen (Belmont, CA); Jo-Anne Hongo (Redwood City, CA); Jennifer W. Johnston (San Francisco, CA); Teemu T. Junttila (San Mateo, CA); Ji Li (San Mateo, CA); Andrew G. Polson (San Francisco, CA)
Assignee: Genentech, Inc.
C07K16/283A61K39/395A61K39/3955A61K47/6849A61K47/6879A61K47/6889A61K51/1045C07K16/2896A61K2039/505C07K2317/24C07K2317/33C07K2317/56
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Quick Facts
Patent No.
US 12,630,636
App. No.
17/734,239
Granted
May 19, 2026
Kind
B2
Abstract

The invention provides anti-FcRH5 antibodies and immunoconjugates and methods of using the same.

Claims (78)

1 . A method of treating an individual having an FcRH5-positive cancer, the method comprising administering to the individual an effective amount of an isolated anti-FcRH5 antibody that binds an isoform c-specific region of the extracellular domain of FcRH5c, wherein the isoform c-specific region comprises amino acids 745-850 of SEQ ID NO:1, and wherein the antibody comprises:

(a) a heavy chain comprising an HVR-H1 comprising the amino acid sequence of SEQ ID NO:39, an HVR-H2 comprising the amino acid sequence of SEQ ID NO:63, and an HVR-H3 comprising the amino acid sequence of SEQ ID NO:87, and a light chain comprising an HVR-L1 comprising the amino acid sequence of SEQ ID NO:3, an HVR-L2 comprising the amino acid sequence of SEQ ID NO:15, and an HVR-L3 comprising the amino acid sequence of SEQ ID NO:27;

(b) a heavy chain comprising an HVR-H1 comprising the amino acid sequence of SEQ ID NO:38, an HVR-H2 comprising the amino acid sequence of SEQ ID NO:62, and an HVR-H3 comprising the amino acid sequence of SEQ ID NO:86, and a light chain comprising an HVR-L1 comprising the amino acid sequence of SEQ ID NO:2, an HVR-L2 comprising the amino acid sequence of SEQ ID NO:14, and an HVR-L3 comprising the amino acid sequence of SEQ ID NO:26;

(c) a heavy chain comprising an HVR-H1 comprising the amino acid sequence of SEQ ID NO:41, an HVR-H2 comprising the amino acid sequence of SEQ ID NO:65, and an HVR-H3 comprising the amino acid sequence of SEQ ID NO:89, and a light chain comprising an HVR-L1 comprising the amino acid sequence of SEQ ID NO:5, an HVR-L2 comprising the amino acid sequence of SEQ ID NO:17, and an HVR-L3 comprising the amino acid sequence of SEQ ID NO:29;

(d) a heavy chain comprising an HVR-H1 comprising the amino acid sequence of SEQ ID NO:42, an HVR-H2 comprising the amino acid sequence of SEQ ID NO:66, and an HVR-H3 comprising the amino acid sequence of SEQ ID NO:90, and a light chain comprising an HVR-L1 comprising the amino acid sequence of SEQ ID NO:6, an HVR-L2 comprising the amino acid sequence of SEQ ID NO:18, and an HVR-L3 comprising the amino acid sequence of SEQ ID NO:30;

(e) a heavy chain comprising an HVR-H1 comprising the amino acid sequence of SEQ ID NO:43, an HVR-H2 comprising the amino acid sequence of SEQ ID NO:67, and an HVR-H3 comprising the amino acid sequence of SEQ ID NO:91, and a light chain comprising an HVR-L1 comprising the amino acid sequence of SEQ ID NO:7, an HVR-L2 comprising the amino acid sequence of SEQ ID NO:19, and an HVR-L3 comprising the amino acid sequence of SEQ ID NO:31;

(f) a heavy chain comprising an HVR-H1 comprising the amino acid sequence of SEQ ID NO:44, an HVR-H2 comprising the amino acid sequence of SEQ ID NO:68, and an HVR-H3 comprising the amino acid sequence of SEQ ID NO:92, and a light chain comprising an HVR-L1 comprising the amino acid sequence of SEQ ID NO:8, an HVR-L2 comprising the amino acid sequence of SEQ ID NO:20, and an HVR-L3 comprising the amino acid sequence of SEQ ID NO:32;

(g) a heavy chain comprising an HVR-H1 comprising the amino acid sequence of SEQ ID NO:45, an HVR-H2 comprising the amino acid sequence of SEQ ID NO:69, and an HVR-H3 comprising the amino acid sequence of SEQ ID NO:93, and a light chain comprising an HVR-L1 comprising the amino acid sequence of SEQ ID NO:9, an HVR-L2 comprising the amino acid sequence of SEQ ID NO:21, and an HVR-L3 comprising the amino acid sequence of SEQ ID NO:33;

(h) a heavy chain comprising an HVR-H1 comprising the amino acid sequence of SEQ ID NO:46, an HVR-H2 comprising the amino acid sequence of SEQ ID NO:70, and an HVR-H3 comprising the amino acid sequence of SEQ ID NO:94, and a light chain comprising an HVR-L1 comprising the amino acid sequence of SEQ ID NO:10, an HVR-L2 comprising the amino acid sequence of SEQ ID NO:22, and an HVR-L3 comprising the amino acid sequence of SEQ ID NO:34;

(i) a heavy chain comprising an HVR-H1 comprising the amino acid sequence of SEQ ID NO:48, an HVR-H2 comprising the amino acid sequence of SEQ ID NO:72, and an HVR-H3 comprising the amino acid sequence of SEQ ID NO:96, and a light chain comprising an HVR-L1 comprising the amino acid sequence of SEQ ID NO:12, an HVR-L2 comprising the amino acid sequence of SEQ ID NO:24, and an HVR-L3 comprising the amino acid sequence of SEQ ID NO:36; or

(j) a heavy chain comprising an HVR-H1 comprising the amino acid sequence of SEQ ID NO:49, an HVR-H2 comprising the amino acid sequence of SEQ ID NO:73, and an HVR-H3 comprising the amino acid sequence of SEQ ID NO:97, and a light chain comprising an HVR-L1 comprising the amino acid sequence of SEQ ID NO:13, an HVR-L2 comprising the amino acid sequence of SEQ ID NO:25, and an HVR-L3 comprising the amino acid sequence of SEQ ID NO:37.

2 . The method of claim 1 , wherein the FcRH5-positive cancer is a B-cell proliferative disorder.

3 . The method of claim 1 , further comprising administering an additional therapeutic agent to the individual.

4 . A method of inhibiting proliferation of an FcRH5-positive cell, the method comprising exposing the cell to an isolated anti-FcRH5 antibody that binds an isoform c-specific region of the extracellular domain of FcRH5c under conditions permissive for binding of the antibody to FcRH5 on the surface of the cell, thereby inhibiting proliferation of the cell, wherein the isoform c-specific region comprises amino acids 745-850 of SEQ ID NO:1, and wherein the antibody comprises:

(a) a heavy chain comprising an HVR-H1 comprising the amino acid sequence of SEQ ID NO:39, an HVR-H2 comprising the amino acid sequence of SEQ ID NO:63, and an HVR-H3 comprising the amino acid sequence of SEQ ID NO:87, and a light chain comprising an HVR-L1 comprising the amino acid sequence of SEQ ID NO:3, an HVR-L2 comprising the amino acid sequence of SEQ ID NO:15, and an HVR-L3 comprising the amino acid sequence of SEQ ID NO:27;

(b) a heavy chain comprising an HVR-H1 comprising the amino acid sequence of SEQ ID NO:38, an HVR-H2 comprising the amino acid sequence of SEQ ID NO:62, and an HVR-H3 comprising the amino acid sequence of SEQ ID NO:86, and a light chain comprising an HVR-L1 comprising the amino acid sequence of SEQ ID NO:2, an HVR-L2 comprising the amino acid sequence of SEQ ID NO:14, and an HVR-L3 comprising the amino acid sequence of SEQ ID NO:26;

(c) a heavy chain comprising an HVR-H1 comprising the amino acid sequence of SEQ ID NO:41, an HVR-H2 comprising the amino acid sequence of SEQ ID NO:65, and an HVR-H3 comprising the amino acid sequence of SEQ ID NO:89, and a light chain comprising an HVR-L1 comprising the amino acid sequence of SEQ ID NO:5, an HVR-L2 comprising the amino acid sequence of SEQ ID NO:17, and an HVR-L3 comprising the amino acid sequence of SEQ ID NO:29;

(d) a heavy chain comprising an HVR-H1 comprising the amino acid sequence of SEQ ID NO:42, an HVR-H2 comprising the amino acid sequence of SEQ ID NO:66, and an HVR-H3 comprising the amino acid sequence of SEQ ID NO:90, and a light chain comprising an HVR-L1 comprising the amino acid sequence of SEQ ID NO:6, an HVR-L2 comprising the amino acid sequence of SEQ ID NO:18, and an HVR-L3 comprising the amino acid sequence of SEQ ID NO:30;

(e) a heavy chain comprising an HVR-H1 comprising the amino acid sequence of SEQ ID NO:43, an HVR-H2 comprising the amino acid sequence of SEQ ID NO:67, and an HVR-H3 comprising the amino acid sequence of SEQ ID NO:91, and a light chain comprising an HVR-L1 comprising the amino acid sequence of SEQ ID NO:7, an HVR-L2 comprising the amino acid sequence of SEQ ID NO:19, and an HVR-L3 comprising the amino acid sequence of SEQ ID NO:31;

(f) a heavy chain comprising an HVR-H1 comprising the amino acid sequence of SEQ ID NO:44, an HVR-H2 comprising the amino acid sequence of SEQ ID NO:68, and an HVR-H3 comprising the amino acid sequence of SEQ ID NO:92, and a light chain comprising an HVR-L1 comprising the amino acid sequence of SEQ ID NO:8, an HVR-L2 comprising the amino acid sequence of SEQ ID NO:20, and an HVR-L3 comprising the amino acid sequence of SEQ ID NO:32;

(g) a heavy chain comprising an HVR-H1 comprising the amino acid sequence of SEQ ID NO:45, an HVR-H2 comprising the amino acid sequence of SEQ ID NO:69, and an HVR-H3 comprising the amino acid sequence of SEQ ID NO:93, and a light chain comprising an HVR-L1 comprising the amino acid sequence of SEQ ID NO:9, an HVR-L2 comprising the amino acid sequence of SEQ ID NO:21, and an HVR-L3 comprising the amino acid sequence of SEQ ID NO:33;

(h) a heavy chain comprising an HVR-H1 comprising the amino acid sequence of SEQ ID NO:46, an HVR-H2 comprising the amino acid sequence of SEQ ID NO:70, and an HVR-H3 comprising the amino acid sequence of SEQ ID NO:94, and a light chain comprising an HVR-L1 comprising the amino acid sequence of SEQ ID NO:10, an HVR-L2 comprising the amino acid sequence of SEQ ID NO:22, and an HVR-L3 comprising the amino acid sequence of SEQ ID NO:34;

(i) a heavy chain comprising an HVR-H1 comprising the amino acid sequence of SEQ ID NO:48, an HVR-H2 comprising the amino acid sequence of SEQ ID NO:72, and an HVR-H3 comprising the amino acid sequence of SEQ ID NO:96, and a light chain comprising an HVR-L1 comprising the amino acid sequence of SEQ ID NO:12, an HVR-L2 comprising the amino acid sequence of SEQ ID NO:24, and an HVR-L3 comprising the amino acid sequence of SEQ ID NO:36; or

(j) a heavy chain comprising an HVR-H1 comprising the amino acid sequence of SEQ ID NO:49, an HVR-H2 comprising the amino acid sequence of SEQ ID NO:73, and an HVR-H3 comprising the amino acid sequence of SEQ ID NO:97, and a light chain comprising an HVR-L1 comprising the amino acid sequence of SEQ ID NO:13, an HVR-L2 comprising the amino acid sequence of SEQ ID NO:25, and an HVR-L3 comprising the amino acid sequence of SEQ ID NO:37.

5 . The method of claim 4 , wherein the cell is a B-cell.

6 . The method of claim 1 , wherein:

(a) in part (a), the heavy chain comprises a VH sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:113 and/or the light chain comprises a VL sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:112;

(b) in part (b), the heavy chain comprises a VH sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:111 and/or the light chain comprises a VL sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO: 110;

(c) in part (c), the heavy chain comprises a VH sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:117 and/or the light chain comprises a VL sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:116;

(d) in part (d), the heavy chain comprises a VH sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:119 and/or the light chain comprises a VL sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:118;

(e) in part (e), the heavy chain comprises a VH sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:121 and/or the light chain comprises a VL sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:120;

(f) in part (f), the heavy chain comprises a VH sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:123 and/or the light chain comprises a VL sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:122;

(g) in part (g), the heavy chain comprises a VH sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:125 and/or the light chain comprises a VL sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:124;

(h) in part (h), the heavy chain comprises a VH sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:127 and/or the light chain comprises a VL sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO: 126;

(i) in part (i), the heavy chain comprises a VH sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:131 and/or the light chain comprises a VL sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:130;

(j) in part (j), the heavy chain comprises a VH sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:133 and/or the light chain comprises a VL sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:132; or

(k) in part (a), the heavy chain comprises a VH sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:135 and/or the light chain comprises a VL sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:134.

7 . The method of claim 6 , wherein:

(a) in part (a), the heavy chain comprises a VH sequence of SEQ ID NO:113 and/or the light chain comprises a VL sequence of SEQ ID NO:112;

(b) in part (b), the heavy chain comprises a VH sequence of SEQ ID NO:111 and/or the light chain comprises a VL sequence of SEQ ID NO:110;

(c) in part (c), the heavy chain comprises a VH sequence of SEQ ID NO:117 and/or the light chain comprises a VL sequence of SEQ ID NO:116;

(d) in part (d), the heavy chain comprises a VH sequence of SEQ ID NO:119 and/or the light chain comprises a VL sequence of SEQ ID NO:118;

(e) in part (e), the heavy chain comprises a VH sequence of SEQ ID NO:121 and/or the light chain comprises a VL sequence of SEQ ID NO:120;

(f) in part (f), the heavy chain comprises a VH sequence of SEQ ID NO:123 and/or the light chain comprises a VL sequence of SEQ ID NO:122;

(g) in part (g), the heavy chain comprises a VH sequence of SEQ ID NO:125 and/or the light chain comprises a VL sequence of SEQ ID NO:124;

(h) in part (h), the heavy chain comprises a VH sequence of SEQ ID NO:127 and/or the light chain comprises a VL sequence of SEQ ID NO:126;

(i) in part (i), the heavy chain comprises a VH sequence of SEQ ID NO:131 and/or the light chain comprises a VL sequence of SEQ ID NO:130;

(j) in part (j), the heavy chain comprises a VH sequence of SEQ ID NO:133 and/or the light chain comprises a VL sequence of SEQ ID NO:132; or

(k) in part (a), the heavy chain comprises a VH sequence of SEQ ID NO:135 and/or the light chain comprises a VL sequence of SEQ ID NO:134.

8 . The method of claim 1 , wherein the antibody is a monoclonal antibody.

9 . The method of claim 1 , wherein the antibody is a human, humanized, or chimeric antibody.

10 . The method of claim 1 , wherein the antibody is an antibody fragment that binds FcRH5.

11 . The method of claim 1 , wherein the antibody is an IgG1, IgG2a or IgG2b antibody.

12 . The method of claim 1 , wherein the antibody has one or more of the following characteristics: a) cross reactivity with full length human and cyno FcRH5, b) binds to endogenous FcRH5, c) does not cross react with FcRH5a, and d) does not cross react with another Ig-like domain of FcRH5.

13 . The method of claim 4 , wherein:

(a) in part (a), the heavy chain comprises a VH sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:113 and/or the light chain comprises a VL sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:112;

(b) in part (b), the heavy chain comprises a VH sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:111 and/or the light chain comprises a VL sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO: 110;

(c) in part (c), the heavy chain comprises a VH sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:117 and/or the light chain comprises a VL sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:116;

(d) in part (d), the heavy chain comprises a VH sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:119 and/or the light chain comprises a VL sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:118;

(e) in part (e), the heavy chain comprises a VH sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:121 and/or the light chain comprises a VL sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:120;

(f) in part (f), the heavy chain comprises a VH sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:123 and/or the light chain comprises a VL sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:122;

(g) in part (g), the heavy chain comprises a VH sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:125 and/or the light chain comprises a VL sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:124;

(h) in part (h), the heavy chain comprises a VH sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:127 and/or the light chain comprises a VL sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO: 126;

(i) in part (i), the heavy chain comprises a VH sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:131 and/or the light chain comprises a VL sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:130;

(j) in part (j), the heavy chain comprises a VH sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:133 and/or the light chain comprises a VL sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:132; or

(k) in part (a), the heavy chain comprises a VH sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:135 and/or the light chain comprises a VL sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO:134.

14 . The method of claim 13 , wherein:

(a) in part (a), the heavy chain comprises a VH sequence of SEQ ID NO:113 and/or the light chain comprises a VL sequence of SEQ ID NO:112;

(b) in part (b), the heavy chain comprises a VH sequence of SEQ ID NO:111 and/or the light chain comprises a VL sequence of SEQ ID NO:110;

(c) in part (c), the heavy chain comprises a VH sequence of SEQ ID NO:117 and/or the light chain comprises a VL sequence of SEQ ID NO:116;

(d) in part (d), the heavy chain comprises a VH sequence of SEQ ID NO:119 and/or the light chain comprises a VL sequence of SEQ ID NO:118;

(e) in part (e), the heavy chain comprises a VH sequence of SEQ ID NO:121 and/or the light chain comprises a VL sequence of SEQ ID NO:120;

(f) in part (f), the heavy chain comprises a VH sequence of SEQ ID NO:123 and/or the light chain comprises a VL sequence of SEQ ID NO:122;

(g) in part (g), the heavy chain comprises a VH sequence of SEQ ID NO:125 and/or the light chain comprises a VL sequence of SEQ ID NO:124;

(h) in part (h), the heavy chain comprises a VH sequence of SEQ ID NO:127 and/or the light chain comprises a VL sequence of SEQ ID NO:126;

(i) in part (i), the heavy chain comprises a VH sequence of SEQ ID NO:131 and/or the light chain comprises a VL sequence of SEQ ID NO:130;

(j) in part (j), the heavy chain comprises a VH sequence of SEQ ID NO:133 and/or the light chain comprises a VL sequence of SEQ ID NO:132; or

(k) in part (a), the heavy chain comprises a VH sequence of SEQ ID NO:135 and/or the light chain comprises a VL sequence of SEQ ID NO:134.

Continuity (4)
Division 16583584 · Sep 26, 2019
Division 14313822 · Jun 24, 2014
Provisional Application 61838534 · Jun 24, 2013
Related Publication 20230096941A1 · Mar 30, 2023
References Cited (180)
US 4975278A · Senter et al. · 1990 [cited by applicant]
US 5767237A · Sakakibara et al. · 1998 [cited by applicant]
US 6124431A · Sakakibara et al. · 2000 [cited by applicant]
US 6248564B1 · Walter et al. · 2001 [cited by applicant]
US 7105149B1 · Dalla-Favera · 2006 [cited by examiner]
US 7375078B2 · Feng · 2008 [cited by applicant]
US 7491529B2 · Goddard et al. · 2009 [cited by applicant]
US 7498298B2 · Doronina et al. · 2009 [cited by applicant]
US 7745394B2 · Doronina et al. · 2010 [cited by applicant]
US 7858330B2 · Hongo et al. · 2010 [cited by applicant]
US 7863424B2 · Dalla-Favera · 2011 [cited by applicant]
US 7888478B2 · Chang et al. · 2011 [cited by applicant]
US 7947839B2 · Gazzard et al. · 2011 [cited by applicant]
US 7964566B2 · Doronina et al. · 2011 [cited by applicant]
US 7964567B2 · Doronina et al. · 2011 [cited by applicant]
US 7994135B2 · Doronina et al. · 2011 [cited by applicant]
US 7999077B2 · Pastan et al. · 2011 [cited by applicant]
US 8142784B2 · Ebens, Jr. et al. · 2012 [cited by applicant]
US 8362213B2 · Elkins et al. · 2013 [cited by applicant]
US 8388973B2 · Chang et al. · 2013 [cited by applicant]
US 8466260B2 · Elkins et al. · 2013 [cited by applicant]
US 8617559B2 · Elkins et al. · 2013 [cited by applicant]
US 9017951B2 · Elkins et al. · 2015 [cited by applicant]
US 9360484B2 · Elkins et al. · 2016 [cited by applicant]
US 20030165496A1 · Basi et al. · 2003 [cited by applicant]
US 20040018194A1 · Francisco et al. · 2004 [cited by applicant]
US 20040253233A1 · Del Rio et al. · 2004 [cited by applicant]
US 20050226869A1 · Chang et al. · 2005 [cited by applicant]
US 20050238649A1 · Doronina et al. · 2005 [cited by applicant]
US 20060182751A1 · Gazzard et al. · 2006 [cited by applicant]
US 20060216232A1 · Chang et al. · 2006 [cited by applicant]
US 20060251662A1 · Chang et al. · 2006 [cited by applicant]
US 20070092940A1 · Eigenbrot et al. · 2007 [cited by applicant]
US 20070134243A1 · Gazzard et al. · 2007 [cited by applicant]
US 20070148176A1 · Dalla-Favera · 2007 [cited by applicant]
US 20080226657A1 · Doronina et al. · 2008 [cited by applicant]
US 20080247944A1 · Graziano et al. · 2008 [cited by applicant]
US 20080248051A1 · Doronina et al. · 2008 [cited by applicant]
US 20080248053A1 · Doronina et al. · 2008 [cited by applicant]
US 20080292632A1 · Pastan et al. · 2008 [cited by applicant]
US 20090047296A1 · Doronina et al. · 2009 [cited by applicant]
US 20090202536A1 · Ebens, Jr. et al. · 2009 [cited by applicant]
US 20100260748A1 · Elkins et al. · 2010 [cited by applicant]
US 20110076287A1 · Cohen et al. · 2011 [cited by applicant]
US 20110110951A1 · Dalla-Favera · 2011 [cited by applicant]
US 20110256157A1 · Howard et al. · 2011 [cited by applicant]
US 20110268657A1 · Chang et al. · 2011 [cited by applicant]
US 20120003247A1 · Doronina et al. · 2012 [cited by applicant]
US 20120003248A1 · Doronina et al. · 2012 [cited by applicant]
US 20120027783A1 · Doronina et al. · 2012 [cited by applicant]
US 20120027784A1 · Doronina et al. · 2012 [cited by applicant]
US 20120034246A1 · Doronina et al. · 2012 [cited by applicant]
US 20120034247A1 · Doronina et al. · 2012 [cited by applicant]
US 20120141508A1 · Doronina et al. · 2012 [cited by applicant]
US 20120141509A1 · Doronina et al. · 2012 [cited by applicant]
US 20120141510A1 · Doronina et al. · 2012 [cited by applicant]
US 20120148608A1 · Doronina et al. · 2012 [cited by applicant]
US 20120148610A1 · Doronina et al. · 2012 [cited by applicant]
US 20130089555A1 · Elkins et al. · 2013 [cited by applicant]
US 20150166661A1 · Chen et al. · 2015 [cited by applicant]
US 20160368985A1 · Hotzel et al. · 2016 [cited by applicant]
CN 102973947A · 2013 [cited by applicant]
EP 1391213A1 · 2004 [cited by applicant]
JP 2005536439A · 2005 [cited by applicant]
JP 2011528360A · 2011 [cited by applicant]
JP 2012522513A · 2012 [cited by applicant]
JP 2013523895A · 2013 [cited by applicant]
RU 2539112C2 · 2015 [cited by applicant]
TW 201039846A · 2010 [cited by applicant]
TW 201508008A · 2015 [cited by applicant]
WO WO0138490A2 · 2001 [cited by applicant]
WO WO02088172A2 · 2002 [cited by applicant]
WO WO02102972A2 · 2002 [cited by applicant]
WO WO03024392A2 · 2003 [cited by applicant]
WO WO03043583A2 · 2003 [cited by applicant]
WO WO03077836A2 · 2003 [cited by applicant]
WO WO2004032828A2 · 2004 [cited by applicant]
WO WO2005063299A2 · 2005 [cited by applicant]
WO WO2005081711A2 · 2005 [cited by applicant]
WO WO2005117986A2 · 2005 [cited by applicant]
WO WO2006034488A2 · 2006 [cited by applicant]
WO WO2006039238A2 · 2006 [cited by applicant]
WO WO2006076691A2 · 2006 [cited by applicant]
WO WO2007001851A2 · 2007 [cited by applicant]
WO WO2008109533A2 · 2008 [cited by applicant]
WO WO2010009124A2 · 2010 [cited by applicant]
WO WO2010114940A1 · 2010 [cited by applicant]
WO WO2010120561A1 · 2010 [cited by applicant]
WO WO2011028945A1 · 2011 [cited by applicant]
WO WO2011130598A1 · 2011 [cited by applicant]
WO WO2014210064A1 · 2014 [cited by applicant]
WO WO2016205520A1 · 2016 [cited by applicant]
Janeway et al., Immunology Third Edition, Garland Publishing Inc. 1997, Chapter 3, Structure of the Antibody Molecule and Immunoglobulin Genes, pp. 3:1-3:11. (Year: 1997). [cited by examiner]
Edwards et al. J. Mol. Biol., 2003, 334:103-118. (Year: 2003). [cited by examiner]
Kanyavuz et al. Nature Review Immunology, 2019, 19: 355-368. (Year: 2019). [cited by examiner]
Goel et al. The Journal of Immunology, 2004, 173:7358-7367. (Year: 2004). [cited by examiner]
Bargou et al., “Tumor regression in cancer patients by very low doses of a T cell-engaging antibody,” Science. 321(5891):974-7 (2008) (5 pages). [cited by applicant]
Bendayan, “Possibilities of false immunocytochemical results generated by the use of monoclonal antibodies: the example of the anti-proinsulin antibody,” J Histochem Cytochem. 43(9):881-6 (1995). [cited by applicant]
Bendig, “Humanization of rodent monoclonal antibodies by CDR grafting,” Methods: A Companion to Methods in Enzymology. 8:83-93 (1995). [cited by applicant]
Bernhard et al., “Cysteine analogs of recombinant barley ribosome inactivating protein form antibody conjugates with enhanced stability and potency in vitro,” Bioconjug Chem. 5(2):126-32 (1994). [cited by applicant]
Better et al., “Gelonin analogs with engineered cysteine residues form antibody immunoconjugates with unique properties,” J Biol Chem. 269(13):9644-50 (1994). [cited by applicant]
Bhaskar et al., “E-selectin up-regulation allows for targeted drug delivery in prostate cancer,” Cancer Res. 63(19):6387-94 (2003). [cited by applicant]
Boring et al., “Cancer statistics, 1993,” CA Cancer J Clin. 43(1):7-26 (1993). [cited by applicant]
Bost et al., “Antibodies against a peptide sequence within the HIV envelope protein crossreacts with human interleukin-2,” Immunol Invest. 17(6-7):577-86 (1988). [cited by applicant]
Burns et al., “A high molecular weight-melanoma associated antigen-specific chimeric antigen receptor redirects lymphocytes to target human melanomas,” available in PMC Dec. 23, 2011, published in final edited form as: … [cited by applicant]
Carter et al., “Humanization of an anti-p185 [cited by applicant]
Chen et al., “Generation and analysis of random point mutations in an antibody CDR2 sequence: many mutated antibodies lose their ability to bind antigen,” J Exp Med. 176(3):855-66 (1992). [cited by applicant]
Chmura et al., “Antibodies with infinite affinity,” Proc Natl Acad Sci U S A. 98(15):8480-4 (2001). [cited by applicant]
Colman, “Effects of amino acid sequence changes on antibody-antigen interactions,” Res Immunol. 145(1):33-6 (1994). [cited by applicant]
Davis et al., “Identification of a family of Fc receptor homologs with preferential B cell expression,” Proc Natl Acad Sci U S A. 98(17):9772-7 (2001). [cited by applicant]
Dement-Brown et al., “Fc receptor-like 5 promotes B cell proliferation and drives the development of cells displaying switched isotypes,” J Leukoc Biol. 91(1):59-67 (2012) (10 pages). [cited by applicant]
Doronina et al., “Development of potent monoclonal antibody auristatin conjugates for cancer therapy,” Nat Biotechnol. 21(7):778-84 (2003) (9 pages). [cited by applicant]
Dreier et al., “Extremely potent, rapid and costimulation-independent cytotoxic T-cell response against lymphoma cells catalyzed by a single-chain bispecific antibody,” Int J Cancer. 100(6):690-7 (2002). [cited by applicant]
Elkins et al., “FcRL5 as a target of antibody-drug conjugates for the treatment of multiple myeloma,” Mol Cancer Ther. 11(10):2222-32 (2012). [cited by applicant]
Francisco et al., “cAC10-vcMMAE, an anti-CD30-monomethyl auristatin E conjugate with potent and selective antitumor activity,” Blood. 102(4):1458-65 (2003). [cited by applicant]
Greenspan et al., “Defining epitopes: It's not as easy as it seems,” Nat Biotechnol. 17(10):936-7 (1999). [cited by applicant]
Greenwood et al., “Engineering multiple-domain forms of the therapeutic antibody CAMPATH-1H: effects on complement lysis,” Ther Immunol. 1(5):247-55 (1994). [cited by applicant]
Güssow et al., “Humanization of monoclonal antibodies,” Methods Enzymol. 203:99-121 (1991). [cited by applicant]
Hatzivassiliou et al., “IRTA1 and IRTA2, novel immunoglobulin superfamily receptors expressed in B cells and involved in chromosome 1q21 abnormalities in B cell malignancy,” Immunity. 14(3):277-89 (2001). [cited by applicant]
Hinman et al., “Preparation and characterization of monoclonal antibody conjugates of the calicheamicins: a novel and potent family of antitumor antibiotics,” Cancer Res. 53(14):3336-42 (1993). [cited by applicant]
Holm et al., “Functional mapping and single chain construction of the anti-cytokeratin 8 monoclonal antibody TS1,” Mol Immunol. 44(6):1075-84 (2007). [cited by applicant]
Inoue et al., “Overexpression of PDZK1 within the 1q12-q22 amplicon is likely to be associated with drug-resistance phenotype in multiple myeloma,” Am J Pathol. 165(1):71-81 (2004). [cited by applicant]
Ise et al., “Elevation of soluble CD307 (IRTA2/FcRH5) protein in the blood and expression on malignant cells of patients with multiple myeloma, chronic lymphocytic leukemia, and mantle cell lymphoma,” Leukemia. 21(1):16… [cited by applicant]
Ise et al., “Immunoglobulin superfamily receptor translocation associated 2 protein on lymphoma cell lines and hairy cell leukemia cells detected by novel monoclonal antibodies,” Clin Cancer Res. 11(1):87-96 (2005). [cited by applicant]
Janeway et al., Chapter 3: Structure of the Antibody Molecule and Immunoglobulin Genes, [cited by applicant]
Junutula et al., “Rapid identification of reactive cysteine residues for site-specific labeling of antibody-Fabs,” J Immunol Methods. 332(1-2):41-52 (2008). [cited by applicant]
Junutula et al., “Site-specific conjugation of a cytotoxic drug to an antibody improves the therapeutic index,” Nat Biotechnol. 26(8):925-32 (2008). [cited by applicant]
Kanno et al., “Assembling of engineered IgG-binding protein on gold surface for highly oriented antibody immobilization,” J Biotechnol. 76(2-3):207-14 (2000). [cited by applicant]
Krishnan et al., “Role of antibody paratope conformational flexibility in the manifestation of molecular mimicry,” Biophys J. 94(4):1367-76 (2008). [cited by applicant]
Lambert, “Drug-conjugated monoclonal antibodies for the treatment of cancer,” Curr Opin Pharmacol. 5(5):543-9 (2005). [cited by applicant]
Liu et al., “Eradication of large colon tumor xenografts by targeted delivery of maytansinoids,” Proc Natl Acad Sci U S A. 93(16):8618-23 (1996). [cited by applicant]
Liu et al., “Heteroantibody duplexes target cells for lysis by cytotoxic T lymphocytes,” Proc Natl Acad Sci U S A. 82(24):8648-52 (1985). [cited by applicant]
Lode et al., “Targeted therapy with a novel enediyene antibiotic calicheamicin theta(I)1 effectively suppresses growth and dissemination of liver metastases in a syngeneic model of murine neuroblastoma,” Cancer Res. 58(… [cited by applicant]
Maccallum et al., “Antibody-antigen interactions: contact analysis and binding site topography,” J Mol Biol. 262(5):732-45 (1996) (14 pages). [cited by applicant]
Mandler et al., “Immunoconjugates of geldanamycin and anti-HER2 monoclonal antibodies: antiproliferative activity on human breast carcinoma cell lines,” J Natl Cancer Inst. 92(19):1573-81 (2000). [cited by applicant]
Mandler et al., “Modifications in synthesis strategy improve the yield and efficacy of geldanamycin-herceptin immunoconjugates,” Bioconjug Chem. 13(4):786-91 (2002). [cited by applicant]
Mandler et al., “Synthesis and evaluation of antiproliferative activity of a geldanamycin-Herceptin(TM) immunoconjugate,” Bioorg Med Chem Lett. 10(10):1025-8 (2000). [cited by applicant]
Mao et al., “EphB2 as a therapeutic antibody drug target for the treatment of colorectal cancer,” Cancer Res. 64(3):781-8 (2004). [cited by applicant]
Mariuzza et al., “The structural basis of antigen-antibody recognition,” Annu Rev Biophys Biophys Chem. 16:139-59 (1987). [cited by applicant]
Miller et al., “IRTAs: a new family of immunoglobulinlike receptors differentially expressed in B cells,” Blood. 99(8):2662-9 (2002) (9 pages). [cited by applicant]
Nakayama et al., “Altered gene expression upon BCR cross-linking in Burkitt's lymphoma B cell line,” Biochem Biophys Res Commun. 277(1):124-7 (2000). [cited by applicant]
Ohno et al., “Antigen-binding specificities of antibodies are primarily determined by seven residues of VH,” Proc Natl Acad Sci USA. 82(9):2945-9 (1985). [cited by applicant]
Paul, Chapter 9: Structure and Function of Immunoglobulins, [cited by applicant]
Payne, “Progress in immunoconjugate cancer therapeutics,” Cancer Cell. 3(3):207-12 (2003). [cited by applicant]
Polson et al., “Expression pattern of the human FcRH/IRTA receptors in normal tissue and in B-chronic lymphocytic leukemia,” Int Immunol. 18(9):1363-73 (2006). [cited by applicant]
Rowland et al., “Drug localisation and growth inhibition studies of vindesine-monoclonal anti-CEA conjugates in a human tumour xenograft,” Cancer Immunol Immunother. 21(3):183-7 (1986). [cited by applicant]
Rudikoff et al., “Single amino acid substitution altering antigen-binding specificity,” Proc Natl Acad Sci U S A. 79(6):1979-83 (1982). [cited by applicant]
Senter et al., “Immunoconjugates comprised of drugs with impaired cellular permeability: A new approach to targeted therapy,” Proc Amer Assoc Cancer Res. 45:144 Abstract 623 (2004) (1 page). [cited by applicant]
Shalaby et al., “Development of humanized bispecific antibodies reactive with cytotoxic lymphocytes and tumor cells overexpressing the HER2 protooncogene,” J Exp Med. 175(1):217-25 (1992). [cited by applicant]
Springer et al., “Antibody-directed enzyme prodrug therapy (ADEPT): a review,” Adv Drug Deliv Rev. 26(2-3):151-172 (1997). [cited by applicant]
Syrigos et al., “Antibody directed enzyme prodrug therapy (ADEPT): a review of the experimental and clinical considerations,” Anticancer Res. 19(1A):605-13 (1999). [cited by applicant]
Tu et al., “Protein footprinting at cysteines: probing ATP-modulated contacts in cysteine-substitution mutants of yeast DNA topoisomerase II,” Proc Natl Acad Sci U S A. 96(9):4862-7 (1999). [cited by applicant]
Vajdos et al., “Comprehensive functional maps of the antigen-binding site of an anti-ErbB2 antibody obtained with shotgun scanning mutagenesis,” J Mol Biol. 320(2):415-28 (2002). [cited by applicant]
Wu et al., “Arming antibodies: prospects and challenges for immunoconjugates,” Nat Biotechnol. 23(9):1137-46 (2005). [cited by applicant]
Zhang et al., “Complete disulfide bond assignment of a recombinant immunoglobulin G4 monoclonal antibody,” Anal Biochem. 311(1):1-9 (2002). [cited by applicant]
Zhu et al., “Engineering high affinity humanized anti-p185HER2/anti-CD3 bispecific F(ab′)2 for efficient lysis of p185HER2 overexpressing tumor cells,” Int J Cancer. 62(3):319-24 (1995). [cited by applicant]
Communication pursuant to Article 94(3) EPC for European Patent Application No. 17198415.6, dated Jul. 12, 2019 (4 pages). [cited by applicant]
Decision to Grant for Russian Patent Application No. 2016101965, dated Feb. 1, 2019 (45 pages). [cited by applicant]
Decision of The Intellectual Property Office for Taiwanese Patent Application No. 103121621, dated Sep. 19, 2019 (12 pages). [cited by applicant]
English Translation of Decision of Final Rejection for Chinese Patent Application No. 201480045475.0, dated Apr. 2, 2020 (13 pages). [cited by applicant]
English Translation of Office Action for Chinese Patent Application No. 201480045475.0, dated Oct. 9, 2018 (9 pages). [cited by applicant]
English Translation of Search Report for Chinese Patent Application No. 201480045475.0, dated Sep. 27, 2018 (2 pages). [cited by applicant]
English Translation of the Second Office Action for Chinese Patent Application No. 201480045475.0, issued Sep. 3, 2019 (9 pages). [cited by applicant]
Examination Report for Australian Patent Application No. 2014302617, dated Dec. 18, 2018 (3 pages). [cited by applicant]
Examination Report for Gulf Cooperation Council Patent Application No. 2014-36569, dated for Mar. 5, 2020 (4 pages). [cited by applicant]
Examination Report for Gulf Cooperation Council Patent Application No. GC 2014-36569, dated Jun. 30, 2019 (4 pages). [cited by applicant]
International Preliminary Report on Patentability issued Dec. 19, 2017, for Hotzel et al., “Humanized and Affinity Matured Antibodies to FCRH5 and Methods of Use,” International Patent Application No. PCT/US2016/037879,… [cited by applicant]
International Search Report and Written Opinion for International Patent Application No. PCT/US2010/029516, mailed Aug. 23, 2010 (18 pages). [cited by applicant]
International Search Report and Written Opinion for International Patent Application No. PCT/US2010/029521, mailed Jul. 20, 2010 (16 pages). [cited by applicant]
International Search Report and Written Opinion for International Patent Application No. PCT/US2014/043952, mailed Oct. 7, 2014 (13 pages). [cited by applicant]
Notice of Preliminary Rejection for Korean Patent Application No. 10-2011-7025864, mailed Nov. 21, 2016 (19 pages). [cited by applicant]
Notice of Preliminary Rejection for Korean Patent Application No. 10-2016-7001897, dated Sep. 10, 2020 (15 pages). [cited by applicant]
Notice of Reasons for Rejection for Japanese Patent Application No. 2016-521907, issued Jun. 12, 2018 (16 pages). [cited by applicant]
Objection filed by Asociación Industrial de Laboratorios Farmacéuticos AG against Chilean Patent Application No. 2417-2011, dated Mar. 30, 2012 (6 pages). [cited by applicant]
Office Action and Search Report for Taiwanese Application No. 103121621, dated Feb. 11, 2019 (16 pages). [cited by applicant]
Office Action for Canadian Patent Application No. 2,915,480, dated Jun. 1, 2020 (6 pages). [cited by applicant]
Official Action for Mexican Patent Application No. MX/a/2015/017331, dated Aug. 20, 2019 (4 pages). [cited by applicant]
Office Action for Russian Patent Application No. 2016101965, dated Dec. 4, 2017 (6 pages). [cited by applicant]
Search Report for Singaporean Patent Application No. 11201510653Y, dated Nov. 9, 2016 (3 pages). [cited by applicant]
Written Opinion for Singaporean Patent Application No. 11201510653Y, dated Dec. 12, 2016 (7 pages). [cited by applicant]