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10.1371/journal.ppat.1006461 http://scihub22266oqcxt.onion/10.1371/journal.ppat.1006461 C5589267!5589267!28880920     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       PLoS+Pathog 2017 ; 13 (9): ä Nephropedia Template TP {{tp|p=28880920|t=2017. The Staphylococcus aureus superantigen SElX is a bifunctional toxin that inhibits neutrophil function |pdf=|usr=}}{{28880920}} gab.com Text The Staphylococcus aureus superantigen SElX is a bifunctional toxin that inhibits neutrophil function JO: PLoS Pathog http://www.kidney.de/pget.php?&tw=1&pmid=28880920 #FOAvip Bacterial superantigens (SAgs) cause V?-dependent T-cell proliferation leading to immune dysregulation associated with the pathogenesis of life-threatening infections such as toxic shock syndrome, and necrotizing pneumonia. Previously, we demonstrated that staphylococcal enterotoxin-like toxin X (SElX) from Staphylococcus aureus is a classical superantigen that exhibits T-cell activation in a V?-specific manner, and contributes to the pathogenesis of necrotizing pneumonia. Here, we discovered that SElX can also bind to neutrophils from human and other mammalian species and disrupt IgG-mediated phagocytosis. Site-directed mutagenesis of the conserved sialic acid-binding motif of SElX abolished neutrophil binding and phagocytic killing, and revealed multiple glycosylated neutrophil receptors for SElX binding. Furthermore, the neutrophil binding-deficient mutant of SElX retained its capacity for T-cell activation demonstrating that SElX exhibits mechanistically independent activities on distinct cell populations associated with acquired and innate immunity, respectively. Finally, we demonstrated that the neutrophil-binding activity rather than superantigenicity is responsible for the SElX-dependent virulence observed in a necrotizing pneumonia rabbit model of infection. Taken together, we report the first example of a SAg, that can manipulate both the innate and adaptive arms of the human immune system during S. aureus pathogenesis. Twit Text FOAVip The Staphylococcus aureus superantigen SElX is a bifunctional toxin that inhibits neutrophil function ????PLoS Pathog http://www.kidney.de/pget.php?&tw=1&pmid=28880920 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28880920 #FOAvip English Wikipedia <ref>{{Cite pmid|28880920}}</ref> The Staphylococcus aureus superantigen SElX is a bifunctional toxin that inhibits neutrophil function #MMPMID28880920 Tuffs SW; James DBA; Bestebroer J; Richards AC; Goncheva MI; O?Shea M; Wee BA; Seo KS; Schlievert PM; Lengeling A; van Strijp JA; Torres VJ; Fitzgerald JR PLoS Pathog 2017[Sep]; 13 (9): ä PMID28880920show ga Bacterial superantigens (SAgs) cause V?-dependent T-cell proliferation leading to immune dysregulation associated with the pathogenesis of life-threatening infections such as toxic shock syndrome, and necrotizing pneumonia. Previously, we demonstrated that staphylococcal enterotoxin-like toxin X (SElX) from Staphylococcus aureus is a classical superantigen that exhibits T-cell activation in a V?-specific manner, and contributes to the pathogenesis of necrotizing pneumonia. Here, we discovered that SElX can also bind to neutrophils from human and other mammalian species and disrupt IgG-mediated phagocytosis. Site-directed mutagenesis of the conserved sialic acid-binding motif of SElX abolished neutrophil binding and phagocytic killing, and revealed multiple glycosylated neutrophil receptors for SElX binding. Furthermore, the neutrophil binding-deficient mutant of SElX retained its capacity for T-cell activation demonstrating that SElX exhibits mechanistically independent activities on distinct cell populations associated with acquired and innate immunity, respectively. Finally, we demonstrated that the neutrophil-binding activity rather than superantigenicity is responsible for the SElX-dependent virulence observed in a necrotizing pneumonia rabbit model of infection. Taken together, we report the first example of a SAg, that can manipulate both the innate and adaptive arms of the human immune system during S. aureus pathogenesis. äThe Staphylococcus aureus superantigen SElX is a bifunctional toxin th(epmc).pdf DeepDyve Pubget Overpricing