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10.1038/icb.2010.113 http://scihub22266oqcxt.onion/10.1038/icb.2010.113 20938455!ä!20938455 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Immunol+Cell+Biol 2011 ; 89 (3): 482-91 Nephropedia Template TP {{tp|p=20938455|t=2011. Inhibition of lectin-mediated innate host defences in vivo modulates disease severity during influenza virus infection |pdf=|usr=}}{{20938455}} gab.com Text Inhibition of lectin-mediated innate host defences in vivo modulates disease severity during influenza virus infection JO: Immunol Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=20938455 #FOAvip Host-mediated recognition of mannose-rich glycans on the surface of pathogens represents an ancient mechanism of innate immune defence. In this study, we demonstrate that the virus strains that differ in the degree of N-linked glycosylation on the globular head of their hemagglutinin glycoprotein also differed in their (i) sensitivity to neutralization by a mannose-specific lectin in mouse lung fluids and (ii) ability to infect (and, therefore, to be destroyed) by airway macrophages. Virus strain BJx109 (H3N2), but not PR8 (H1N1), was sensitive to neutralization by mouse lung fluids and infected airway macrophages efficiently in vitro and these antiviral activities were blocked by mannan, a complex polymer of mannose residues. Although intranasal (i.n.) infection of mice with PR8 led to severe disease and mortality, mice infected with an equivalent dose of BJx109 displayed no signs of disease. However, i.n. treatment of BJx109-infected mice with mannan led to viral pneumonia, severe disease and death characterized by excessive virus replication, pulmonary inflammation, vascular leak and lung edema. Thus, when mannose-specific innate defences were inhibited in vivo, virus strain BJx109 induced severe viral pneumonia similar to that of PR8. Together, these findings highlight the importance of N-linked glycans as a target for recognition and destruction of influenza viruses by the innate immune system. Moreover, soluble and cell-associated lectins coordinate to modulate disease severity following influenza virus infection of mice. Twit Text FOAVip Inhibition of lectin-mediated innate host defences in vivo modulates disease severity during influenza virus infection ????Immunol Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=20938455 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=20938455 #FOAvip English Wikipedia <ref>{{Cite pmid|20938455}}</ref> Inhibition of lectin-mediated innate host defences in vivo modulates disease severity during influenza virus infection #MMPMID20938455 Tate MD; Brooks AG; Reading PC Immunol Cell Biol 2011[Mar]; 89 (3): 482-91 PMID20938455show ga Host-mediated recognition of mannose-rich glycans on the surface of pathogens represents an ancient mechanism of innate immune defence. In this study, we demonstrate that the virus strains that differ in the degree of N-linked glycosylation on the globular head of their hemagglutinin glycoprotein also differed in their (i) sensitivity to neutralization by a mannose-specific lectin in mouse lung fluids and (ii) ability to infect (and, therefore, to be destroyed) by airway macrophages. Virus strain BJx109 (H3N2), but not PR8 (H1N1), was sensitive to neutralization by mouse lung fluids and infected airway macrophages efficiently in vitro and these antiviral activities were blocked by mannan, a complex polymer of mannose residues. Although intranasal (i.n.) infection of mice with PR8 led to severe disease and mortality, mice infected with an equivalent dose of BJx109 displayed no signs of disease. However, i.n. treatment of BJx109-infected mice with mannan led to viral pneumonia, severe disease and death characterized by excessive virus replication, pulmonary inflammation, vascular leak and lung edema. Thus, when mannose-specific innate defences were inhibited in vivo, virus strain BJx109 induced severe viral pneumonia similar to that of PR8. Together, these findings highlight the importance of N-linked glycans as a target for recognition and destruction of influenza viruses by the innate immune system. Moreover, soluble and cell-associated lectins coordinate to modulate disease severity following influenza virus infection of mice. |Animals[MESH] |Antibodies, Neutralizing/immunology[MESH] |Cell Line[MESH] |Dogs[MESH] |Host-Pathogen Interactions[MESH] |Humans[MESH] |Immunity, Innate/*immunology[MESH] |Immunologic Factors/pharmacology[MESH] |Influenza A Virus, H1N1 Subtype/pathogenicity/*physiology[MESH] |Leukocytes/immunology[MESH] |Macrophages/immunology/virology[MESH] |Male[MESH] |Mannans/pharmacology[MESH] |Mannose-Binding Lectin/*immunology[MESH] |Mice[MESH] |Mice, Inbred C57BL[MESH] |Mice, Knockout[MESH] |Orthomyxoviridae Infections/*immunology/pathology/virology[MESH] |Pneumonia/chemically induced/pathology[MESH] |Pulmonary Edema/chemically induced/pathology[MESH] |Respiratory System/pathology/virology[MESH]Inhibition of lectin-mediated innate host defences in vivo modulates d(epmc).pdf DeepDyve Pubget Overpricing