TY - JOUR
T1 - Integrin B1 promotes the interaction of murine IgG3 with effector cells
AU - Hawk, Carolyn Saylor
AU - Coelho, Carolina
AU - Lima de Oliveira, Diane Sthefany
AU - Paredes, Verenice
AU - Albuquerque, Patrícia
AU - Bocca, Anamélia Lorenzetti
AU - Correa dos Santos, Ananésia
AU - Rusakova, Victoria
AU - Holemon, Heather
AU - Silva-Pereira, Ildinete
AU - Soares Felipe, Maria Sueli
AU - Yagita, Hideo
AU - Nicola, André Moraes
AU - Casadevall, Arturo
N1 - Funding Information:
This work was supported by National Institutes of Health (NIH) Grants 5R01A1033774, 5R37AI033142, and 5T32A107506 (to A.C.) and Clinical and Translational Science Award Grants 1 ULI TR001073-01, 1 TLI 1 TR001072-01,
Funding Information:
This work was supported by National Institutes of Health (NIH) Grants 5R01A1033774, 5R37AI033142, and 5T32A107506 (to A.C.) and Clinical and Translational Science Award Grants 1 ULI TR001073-01, 1 TLI 1 TR001072-01, and 1 KL2 TR001071 from the National Center for Advancing Translational Sciences (to A.C.). Facilities were supported by the Center for AIDS research at Albert Einstein College of Medicine. C.C. was partially supported by Ph.D. Grant SFRH/ BD/33471/2008 from the Fundação Ciência e Tecnologia. C.S.H. was supported by NIH Grant T32 AI07506. A.M.N. was partially supported by a Reuni scholarship (Ministério da Educação-Brasil) and is currently supported by grants from Con-selho Nacional de Desenvolvimento Científico e Tecnológico (CNPq), Fundação de Apoio a Pesquisa do Distrito Federal and Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (Capes). D.S.L.d.O., V.P., and A.C.d.S. were supported by scholarships from CNPq and Capes. We would like to acknowledge Dr. Jinghang Zhang from the Albert Einstein College of Medicine flow cytometry core facility and Dr. Hao Zhang from the Bloomberg Flow Cytometry and Immunology Core at Johns Hopkins University for technical assistance.
Funding Information:
and 1 KL2 TR001071 from the National Center for Advancing Translational Sciences (to A.C.). Facilities were supported by the Center for AIDS research at Albert Einstein College of Medicine. C.C. was partially supported by Ph.D. Grant SFRH/ BD/33471/2008 from the Fundac¸ão Ciência e Tecnologia. C.S.H. was supported by NIH Grant T32 AI07506. A.M.N. was partially supported by a Reuni scholarship (Ministério da Educac¸ão-Brasil) and is currently supported by grants from Con-selho Nacional de Desenvolvimento Científico e Tecnológico (CNPq), Fundac¸ão de Apoio a Pesquisa do Distrito Federal and Coordenac¸ão de Aperfeic¸oamento de Pessoal de Nível Superior (Capes). D.S.L.d.O., V.P., and A.C.d.S. were supported by scholarships from CNPq and Capes.
Publisher Copyright:
Copyright Ó 2019 by The American Association of Immunologists, Inc.
PY - 2019/5/1
Y1 - 2019/5/1
N2 - Abs exert several of their effector functions by binding to cell surface receptors. For murine IgG3 (mIgG3), the identity of its receptors (and the very existence of a receptor) is still under debate, as not all mIgG3 functions can be explained by interaction with FcgRI. This implies the existence of an alternate receptor, whose identity we sought to pinpoint. We found that blockage of integrin b1 selectively hampered binding of mIgG3 to macrophages and mIgG3-mediated phagocytosis. Manganese, an integrin activator, increased mIgG3 binding to macrophages. Blockage of FcgRI or Itgb1 inhibited binding of different mIgG3 Abs to variable extents. Our results are consistent with the notion that Itgb1 functions as part of an IgG receptor complex. Given the more ancient origin of integrins in comparison with FcgR, this observation could have far-ranging implications for our understanding of the evolution of Ab-mediated immunity as well as in immunity to microorganisms, pathogenesis of autoimmune diseases, and Ab engineering.
AB - Abs exert several of their effector functions by binding to cell surface receptors. For murine IgG3 (mIgG3), the identity of its receptors (and the very existence of a receptor) is still under debate, as not all mIgG3 functions can be explained by interaction with FcgRI. This implies the existence of an alternate receptor, whose identity we sought to pinpoint. We found that blockage of integrin b1 selectively hampered binding of mIgG3 to macrophages and mIgG3-mediated phagocytosis. Manganese, an integrin activator, increased mIgG3 binding to macrophages. Blockage of FcgRI or Itgb1 inhibited binding of different mIgG3 Abs to variable extents. Our results are consistent with the notion that Itgb1 functions as part of an IgG receptor complex. Given the more ancient origin of integrins in comparison with FcgR, this observation could have far-ranging implications for our understanding of the evolution of Ab-mediated immunity as well as in immunity to microorganisms, pathogenesis of autoimmune diseases, and Ab engineering.
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U2 - 10.4049/jimmunol.1701795
DO - 10.4049/jimmunol.1701795
M3 - Article
C2 - 30894426
AN - SCOPUS:85065107626
SN - 0022-1767
VL - 202
SP - 2782
EP - 2794
JO - Journal of Immunology
JF - Journal of Immunology
IS - 9
ER -