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10.1073/pnas.2101497118

http://scihub22266oqcxt.onion/10.1073/pnas.2101497118
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34183391!8271757!34183391
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suck abstract from ncbi

pmid34183391      Proc+Natl+Acad+Sci+U+S+A 2021 ; 118 (27): ä
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  • IgA potentiates NETosis in response to viral infection #MMPMID34183391
  • Stacey HD; Golubeva D; Posca A; Ang JC; Novakowski KE; Zahoor MA; Kaushic C; Cairns E; Bowdish DME; Mullarkey CE; Miller MS
  • Proc Natl Acad Sci U S A 2021[Jul]; 118 (27): ä PMID34183391show ga
  • IgA is the second most abundant antibody present in circulation and is enriched at mucosal surfaces. As such, IgA plays a key role in protection against a variety of mucosal pathogens including viruses. In addition to neutralizing viruses directly, IgA can also stimulate Fc-dependent effector functions via engagement of Fc alpha receptors (Fc-alphaRI) expressed on the surface of certain immune effector cells. Neutrophils are the most abundant leukocyte, express Fc-alphaRI, and are often the first to respond to sites of injury and infection. Here, we describe a function for IgA-virus immune complexes (ICs) during viral infections. We show that IgA-virus ICs potentiate NETosis-the programmed cell-death pathway through which neutrophils release neutrophil extracellular traps (NETs). Mechanistically, IgA-virus ICs potentiated a suicidal NETosis pathway via engagement of Fc-alphaRI on neutrophils through a toll-like receptor-independent, NADPH oxidase complex-dependent pathway. NETs also were capable of trapping and inactivating viruses, consistent with an antiviral function.
  • |Alphainfluenzavirus/immunology[MESH]
  • |Antigen-Antibody Complex/immunology[MESH]
  • |Antigens, CD/metabolism[MESH]
  • |Extracellular Traps/*immunology/virology[MESH]
  • |Humans[MESH]
  • |Immunoglobulin A/*immunology[MESH]
  • |NADPH Oxidases/metabolism[MESH]
  • |Neutrophils/*immunology/pathology/virology[MESH]
  • |Receptors, Fc/metabolism[MESH]
  • |SARS-CoV-2/immunology[MESH]
  • |Signal Transduction[MESH]
  • |Virion[MESH]


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