title: Herpes simplex virus type 1 infection increases the carbohydrate binding activity and the secretion of cellular galectin-3.
abstract: Galectin-3 binds beta-galactoside-containing sugars and is a chemoattractant for monocytes, macrophages, and neutrophils. Galectin-3 was identified by mass spectrometry from an anti-gI affinity column; however, we determined that galectin-3 did not bind gI, but rather that HSV-1 infection increased galectin-3 binding to carbohydrate residues on IgG. Our conclusions are based on the following observations: (1) galectin-3 from cells infected with a gI-deleted HSV-1 mutant virus bound anti-gI IgG; (2) galectin-3 from wild-type HSV-1 infected cells bound nonimmune IgG; (3) more galectin-3 from infected than uninfected cells bound IgG; and (4) binding to IgG was blocked by lactose, a competitive inhibitor of galectin-3 carbohydrate binding. HSV-1 infection did not increase galectin-3 expression, but did increase its secretion. We propose that increased carbohydrate binding and secretion of galectin-3 contribute to an early pro-inflammatory innate immune response to HSV-1 infection.
authors.affiliation: University of Pennsylvania, Philadelphia, 19104-6073, USA. rdking@mail.med.upenn.edu
authors.forename: Ryan D
authors.initials: RD
authors.lastname: King
authors.forename: John M
authors.initials: JM
authors.lastname: Lubinski
authors.forename: Harvey M
authors.initials: HM
authors.lastname: Friedman
mesh_terms: D000818:Animals; D050260:Carbohydrate Metabolism; D002460:Cell Line; D037502:Galectin 3 / Q000276:immunology / Q000378:metabolism*; D006561:Herpes Simplex / Q000276:immunology* / Q000821:virology*; D018259:Herpesvirus 1, Human / Q000276:immunology*; D006801:Humans; D007074:Immunoglobulin G / Q000378:metabolism; D011485:Protein Binding
chemical_list: D037502:Galectin 3; D007074:Immunoglobulin G