title: Galectin-1 binds to influenza virus and ameliorates influenza virus pathogenesis.
abstract: Innate immune response is important for viral clearance during influenza virus infection. Galectin-1, which belongs to S-type lectins, contains a conserved carbohydrate recognition domain that recognizes galactose-containing oligosaccharides. Since the envelope proteins of influenza virus are highly glycosylated, we studied the role of galectin-1 in influenza virus infection in vitro and in mice. We found that galectin-1 was upregulated in the lungs of mice during influenza virus infection. There was a positive correlation between galectin-1 levels and viral loads during the acute phase of viral infection. Cells treated with recombinant human galectin-1 generated lower viral yields after influenza virus infection. Galectin-1 could directly bind to the envelope glycoproteins of influenza A/WSN/33 virus and inhibit its hemagglutination activity and infectivity. It also bound to different subtypes of influenza A virus with micromolar dissociation constant (K(d)) values and protected cells against influenza virus-induced cell death. We used nanoparticle, surface plasmon resonance analysis and transmission electron microscopy to further demonstrate the direct binding of galectin-1 to influenza virus. More importantly, we show for the first time that intranasal treatment of galectin-1 could enhance survival of mice against lethal challenge with influenza virus by reducing viral load, inflammation, and apoptosis in the lung. Furthermore, galectin-1 knockout mice were more susceptible to influenza virus infection than wild-type mice. Collectively, our results indicate that galectin-1 has anti-influenza virus activity by binding to viral surface and inhibiting its infectivity. Thus, galectin-1 may be further explored as a novel therapeutic agent for influenza.
authors.affiliation: Institute of Basic Medical Science, National Cheng Kung University Medical College, Tainan, Taiwan.
authors.forename: Mei-Lin
authors.initials: ML
authors.lastname: Yang
authors.forename: Yu-Hung
authors.initials: YH
authors.lastname: Chen
authors.forename: Shainn-Wei
authors.initials: SW
authors.lastname: Wang
authors.forename: Yen-Jang
authors.initials: YJ
authors.lastname: Huang
authors.forename: Chia-Hsing
authors.initials: CH
authors.lastname: Leu
authors.forename: Nai-Chi
authors.initials: NC
authors.lastname: Yeh
authors.forename: Chun-Yen
authors.initials: CY
authors.lastname: Chu
authors.forename: Chia-Cheng
authors.initials: CC
authors.lastname: Lin
authors.forename: Gia-Shing
authors.initials: GS
authors.lastname: Shieh
authors.forename: Yuh-Ling
authors.initials: YL
authors.lastname: Chen
authors.forename: Jen-Ren
authors.initials: JR
authors.lastname: Wang
authors.forename: Ching-Ho
authors.initials: CH
authors.lastname: Wang
authors.forename: Chao-Liang
authors.initials: CL
authors.lastname: Wu
authors.forename: Ai-Li
authors.initials: AL
authors.lastname: Shiau
mesh_terms: D000818:Animals; D000998:Antiviral Agents / Q000378:metabolism* / Q000627:therapeutic use; D004195:Disease Models, Animal; D005260:Female; D037483:Galectin 1 / Q000378:metabolism* / Q000627:therapeutic use; D009980:Influenza A virus / Q000472:pathogenicity*; D007700:Kinetics; D008168:Lung / Q000473:pathology / Q000821:virology; D051379:Mice; D008810:Mice, Inbred C57BL; D046529:Microscopy, Electron, Transmission; D009976:Orthomyxoviridae Infections / Q000188:drug therapy / Q000473:pathology* / Q000821:virology*; D011485:Protein Binding; D012376:Rodent Diseases / Q000188:drug therapy / Q000473:pathology / Q000821:virology; D020349:Surface Plasmon Resonance; D016019:Survival Analysis; D019562:Viral Load
chemical_list: D000998:Antiviral Agents; D037483:Galectin 1