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Influenza A virus up‐regulates neutrophil adhesion molecules and adhesion to biological surfaces
Author(s) -
Hartshorn Kevan L.,
White Mitchell R.
Publication year - 1999
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1002/jlb.65.5.614
Subject(s) - integrin , cell adhesion molecule , biology , microbiology and biotechnology , selectin , adhesion , elastase , influenza a virus , integrin alpha m , cell adhesion , glycoprotein , cd11c , immunology , chemistry , virus , biochemistry , immune system , receptor , cell , enzyme , phenotype , organic chemistry , gene
Influenza A virus (IAV) binds to sialylated neutrophil surface components (e.g., CD43 and sialyl Lewis x antigen) and induces both activation and functional depression of neutrophils. We report that IAV enhanced neutrophil adhesion to surfaces coated with serum or serum components, but not to uncoated plastic. IAV up‐regulated expression of integrins (CD11b and CD11c) and carcinoembryonic‐related antigens on neutrophils, while reducing expression of CD43, L‐selectin, and P‐selectin glycoprotein ligand (PSGL). Although treatment of neutrophils with elastase or O ‐sialoglycoprotease decreased surface CD43 and PSGL, they did not reduce binding of IAV to neutrophils, implying that IAV can bind to alternate binding sites in the absence of CD43. Pretreatment of neutrophils with elastase also did not prevent IAV from increasing expression of integrins and enhancing adhesion. Up‐regulation of adhesion molecules and adhesion are important, previously unrecognized, features of neutrophil activation by IAV. Further studies will be needed to clarify the mechanism of these effects. J. Leukoc. Biol. 65: 614–622; 1999.