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10.1074/jbc.M110.125567 http://scihub22266oqcxt.onion/10.1074/jbc.M110.125567 C3039347!3039347!21123169     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=21123169&cmd=llinks): Failed to open stream: HTTP request failed! 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Surfactant Protein A (SP-A)-mediated Clearance of Staphylococcus aureus Involves Binding of SP-A to the Staphylococcal Adhesin Eap and the Macrophage Receptors SP-A Receptor 210 and Scavenger Receptor Class A* |pdf=|usr=}}{{21123169}} gab.com Text Surfactant Protein A (SP-A)-mediated Clearance of Staphylococcus aureus Involves Binding of SP-A to the Staphylococcal Adhesin Eap and the Macrophage Receptors SP-A Receptor 210 and Scavenger Receptor Class A* JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=21123169 #FOAvip Staphylococcus aureus causes life-threatening pneumonia in hospitals and deadly superinfection during viral influenza. The current study investigated the role of surfactant protein A (SP-A) in opsonization and clearance of S. aureus. Previous studies showed that SP-A mediates phagocytosis via the SP-A receptor 210 (SP-R210). Here, we show that SP-R210 mediates binding and control of SP-A-opsonized S. aureus by macrophages. We determined that SP-A binds S. aureus through the extracellular adhesin Eap. Consequently, SP-A enhanced macrophage uptake of Eap-expressing (Eap+) but not Eap-deficient (Eap?) S. aureus. In a reciprocal fashion, SP-A failed to enhance uptake of Eap+S. aureus in peritoneal Raw264.7 macrophages with a dominant negative mutation (SP-R210(DN)) blocking surface expression of SP-R210. Accordingly, WT mice cleared infection with Eap+ but succumbed to sublethal infection with Eap- S. aureus. However, SP-R210(DN) cells compensated by increasing non-opsonic phagocytosis of Eap+S. aureus via the scavenger receptor scavenger receptor class A (SR-A), while non-opsonic uptake of Eap?S. aureus was impaired. Macrophages express two isoforms: SP-R210L and SP-R210S. The results show that WT alveolar macrophages are distinguished by expression of SP-R210L, whereas SR-A?/? alveolar macrophages are deficient in SP-R210L expressing only SP-R210S. Accordingly, SR-A?/? mice were highly susceptible to both Eap+ and Eap?S. aureus. The lungs of susceptible mice generated abnormal inflammatory responses that were associated with impaired killing and persistence of S. aureus infection in the lung. In conclusion, alveolar macrophage SP-R210L mediates recognition and killing of SP-A-opsonized S. aureus in vivo, coordinating inflammatory responses and resolution of S. aureus pneumonia through interaction with SR-A. Twit Text FOAVip Surfactant Protein A (SP-A)-mediated Clearance of Staphylococcus aureus Involves Binding of SP-A to the Staphylococcal Adhesin Eap and the Macrophage Receptors SP-A Receptor 210 and Scavenger Receptor Class A* ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=21123169 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=21123169 #FOAvip English Wikipedia <ref>{{Cite pmid|21123169}}</ref> Surfactant Protein A (SP-A)-mediated Clearance of Staphylococcus aureus Involves Binding of SP-A to the Staphylococcal Adhesin Eap and the Macrophage Receptors SP-A Receptor 210 and Scavenger Receptor Class A* #MMPMID21123169 Sever-Chroneos Z; Krupa A; Davis J; Hasan M; Yang CH; Szeliga J; Herrmann M; Hussain M; Geisbrecht BV; Kobzik L; Chroneos ZC J Biol Chem 2011[Feb]; 286 (6): 4854-70 PMID21123169show ga Staphylococcus aureus causes life-threatening pneumonia in hospitals and deadly superinfection during viral influenza. The current study investigated the role of surfactant protein A (SP-A) in opsonization and clearance of S. aureus. Previous studies showed that SP-A mediates phagocytosis via the SP-A receptor 210 (SP-R210). Here, we show that SP-R210 mediates binding and control of SP-A-opsonized S. aureus by macrophages. We determined that SP-A binds S. aureus through the extracellular adhesin Eap. Consequently, SP-A enhanced macrophage uptake of Eap-expressing (Eap+) but not Eap-deficient (Eap?) S. aureus. In a reciprocal fashion, SP-A failed to enhance uptake of Eap+S. aureus in peritoneal Raw264.7 macrophages with a dominant negative mutation (SP-R210(DN)) blocking surface expression of SP-R210. Accordingly, WT mice cleared infection with Eap+ but succumbed to sublethal infection with Eap- S. aureus. However, SP-R210(DN) cells compensated by increasing non-opsonic phagocytosis of Eap+S. aureus via the scavenger receptor scavenger receptor class A (SR-A), while non-opsonic uptake of Eap?S. aureus was impaired. Macrophages express two isoforms: SP-R210L and SP-R210S. The results show that WT alveolar macrophages are distinguished by expression of SP-R210L, whereas SR-A?/? alveolar macrophages are deficient in SP-R210L expressing only SP-R210S. Accordingly, SR-A?/? mice were highly susceptible to both Eap+ and Eap?S. aureus. The lungs of susceptible mice generated abnormal inflammatory responses that were associated with impaired killing and persistence of S. aureus infection in the lung. In conclusion, alveolar macrophage SP-R210L mediates recognition and killing of SP-A-opsonized S. aureus in vivo, coordinating inflammatory responses and resolution of S. aureus pneumonia through interaction with SR-A. �Surfactant Protein A (SP-A)-mediated Clearance of Staphylococcus aureu(epmc).pdf DeepDyve Pubget Overpricing