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10.1016/j.immuni.2017.06.019

http://scihub22266oqcxt.onion/10.1016/j.immuni.2017.06.019
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C5568648!5568648!28723548
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suck abstract from ncbi


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pmid28723548      Immunity 2017 ; 47 (1): 159-170.e10
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  • The Fc domain of immunoglobulin is sufficient to bridge NK cells with virally infected cells #MMPMID28723548
  • Dai HS(; Griffin N; Bolyard C; Mao HC; Zhang J; Cripe TP; Suenaga T; Arase H; Nakano I; Chiocca EA; Kaur B; Yu J; Caligiuri MA
  • Immunity 2017[Jul]; 47 (1): 159-170.e10 PMID28723548show ga
  • Clearance of pathogens or tumor cells by antibodies traditionally requires both Fab and Fc domains of IgG. Here we show the Fc domain of IgG alone mediates recognition and clearance of herpes simplex virus (HSV1) infected cells. The human natural killer (NK) cell surface is naturally coated with IgG bound by its Fc domain to the Fc? receptor CD16a. NK cells utilize the Fc domain of bound IgG to recognize gE, an HSV1-encoded glycoprotein that also binds the Fc domain of IgG but at a site distinct from CD16a. The bridge formed by Fc domain between the HSV1-infected cell and the NK cell results in NK cell activation and lysis of the HSV1-infected cell in the absence of HSV1-specific antibody in vitro, and prevents fatal HSV1 infection in vivo. This mechanism also explains how bacterial IgG-binding proteins regulate NK cell function, and may be broadly applicable to Fc? receptor-bearing cells.
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