Newcastle disease virus neuraminidase primes neutrophils for stimulation by galectin-3 and formyl-Met-Leu-Phe.
Human neutrophils are activated by the beta-galactoside-binding lectin galectin-3, provided that the cells are primed by in vivo extravasation or by in vitro preactivation with, for example, LPS. Removal of terminal sialic acid can change neutrophil functionality and responsiveness due to exposure of underlying glycoconjugate receptors or change in surface charge. Here, we investigated whether such alteration of the cell surface carbohydrate composition can alter the responsiveness of the cells to galectin-3. Neutrophils were treated with neuraminidases (NA) of different origins: Clostridium perfringens (CP), Salmonella typhimurium, Vibrio cholerae, and Newcastle disease virus (NDV). In the presence of NDV-NA, but no other NA, the otherwise non-responding neutrophils responded readily to galectin-3 by activation of the NADPH-oxidase. The galectin-3 priming effect was inhibited by the sialidase inhibitor 2,3-dehydro-2-deoxy-N-acetyl-neuraminic acid. Earlier studies have shown that priming of the neutrophil response to galectin-3 with, for example, LPS is paralleled by degranulation of intracellular vesicles and granules and upregulation of potential galectin-3 receptors. Also, NDV-NA (but not CP-NA) treatment induced degranulation, shown as an upregulation of complement receptor 3. Since not only the galectin response but also the response to the chemoattractant fMLF was primed, NDV-NA appears to induce a general priming phenomenon, possibly due to receptor upregulation by degranulation.
Almkvist
Jenny
J
The Phagocyte Research Laboratory, Department of Rheumatology and Inflammation Research, Göteborg University, Sweden.
Dahlgren
Claes
C
Leffler
Hakon
H
Karlsson
Anna
A
D015550:Cell Degranulation / Q000187:drug effects / Q000276:immunology / Q000502:physiology; D002634:Chemotaxis, Leukocyte / Q000276:immunology; D004791:Enzyme Inhibitors / Q000494:pharmacology; D037502:Galectin 3 / Q000276:immunology* / Q000378:metabolism; D006801:Humans; D008562:Membrane Glycoproteins / Q000187:drug effects / Q000276:immunology; D019158:N-Acetylneuraminic Acid / Q000378:metabolism; D009240:N-Formylmethionine Leucyl-Phenylalanine / Q000276:immunology* / Q000378:metabolism; D019255:NADPH Oxidases / Q000378:metabolism; D009439:Neuraminidase / Q000037:antagonists & inhibitors / Q000276:immunology* / Q000378:metabolism / Q000494:pharmacology; D018375:Neutrophil Activation / Q000276:immunology*; D009504:Neutrophils / Q000187:drug effects / Q000276:immunology* / Q000821:virology; D009522:Newcastle disease virus / Q000201:enzymology* / Q000276:immunology; D011956:Receptors, Cell Surface / Q000187:drug effects / Q000276:immunology; D011951:Receptors, Complement / Q000187:drug effects / Q000276:immunology; D016897:Respiratory Burst / Q000187:drug effects / Q000276:immunology / Q000502:physiology; D022142:Secretory Vesicles / Q000187:drug effects / Q000378:metabolism; D013696:Temperature; D015854:Up-Regulation / Q000187:drug effects / Q000276:immunology; D014764:Viral Proteins / Q000276:immunology
D004791:Enzyme Inhibitors; D037502:Galectin 3; D008562:Membrane Glycoproteins; D011956:Receptors, Cell Surface; D011951:Receptors, Complement; D014764:Viral Proteins; D009240:N-Formylmethionine Leucyl-Phenylalanine; D019255:NADPH Oxidases; D009439:Neuraminidase; D019158:N-Acetylneuraminic Acid