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Galectin-1 Binds to Influenza Virus and Ameliorates Influenza Virus Pathogenesis

Galectin-1 Binds to Influenza Virus and Ameliorates Influenza Virus Pathogenesis Galectin-1 Binds to Influenza Virus and Ameliorates Influenza Virus Pathogenesis ▿ Mei-Lin Yang 1 , † , Yu-Hung Chen 2 , † , Shainn-Wei Wang 3 , † , Yen-Jang Huang 1 , Chia-Hsing Leu 1 , Nai-Chi Yeh 4 , Chun-Yen Chu 5 , Chia-Cheng Lin 6 , Gia-Shing Shieh 7 , Yuh-Ling Chen 8 , Jen-Ren Wang 9 , Ching-Ho Wang 10 , Chao-Liang Wu 1 , 2 , * and Ai-Li Shiau 1 , 4 , * 1 Institute of Basic Medical Sciences 2 Department of Biochemistry and Molecular Biology 3 Institute of Molecular Medicine 4 Department of Microbiology and Immunology 8 Institute of Oral Medicine 9 Department of Medical Laboratory Science and Biotechnology, National Cheng Kung University Medical College, Tainan, Taiwan 5 Graduate Institute of Animal Vaccine Technology, National Pingtung University of Science and Technology, Pingtung, Taiwan 6 Department of Pathology 7 Department of Urology, Tainan Hospital 10 Department of Health, Executive Yuan, Taiwan; and School of Veterinary Medicine, National Taiwan University, Taipei, Taiwan 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Virology American Society For Microbiology

Galectin-1 Binds to Influenza Virus and Ameliorates Influenza Virus Pathogenesis

Journal of Virology , Volume 85 (19): 10010 – Oct 1, 2011

Abstract

Galectin-1 Binds to Influenza Virus and Ameliorates Influenza Virus Pathogenesis ▿ Mei-Lin Yang 1 , † , Yu-Hung Chen 2 , † , Shainn-Wei Wang 3 , † , Yen-Jang Huang 1 , Chia-Hsing Leu 1 , Nai-Chi Yeh 4 , Chun-Yen Chu 5 , Chia-Cheng Lin 6 , Gia-Shing Shieh 7 , Yuh-Ling Chen 8 , Jen-Ren Wang 9 , Ching-Ho Wang 10 , Chao-Liang Wu 1 , 2 , * and Ai-Li Shiau 1 , 4 , * 1 Institute of Basic Medical Sciences 2 Department of Biochemistry and Molecular Biology 3 Institute of Molecular Medicine 4 Department of Microbiology and Immunology 8 Institute of Oral Medicine 9 Department of Medical Laboratory Science and Biotechnology, National Cheng Kung University Medical College, Tainan, Taiwan 5 Graduate Institute of Animal Vaccine Technology, National Pingtung University of Science and Technology, Pingtung, Taiwan 6 Department of Pathology 7 Department of Urology, Tainan Hospital 10 Department of Health, Executive Yuan, Taiwan; and School of Veterinary Medicine, National Taiwan University, Taipei, Taiwan 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.

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Publisher
American Society For Microbiology
Copyright
Copyright © 2011 by the American society for Microbiology.
ISSN
0022-538X
eISSN
1098-5514
DOI
10.1128/JVI.00301-11
pmid
21795357
Publisher site
See Article on Publisher Site

Abstract

Galectin-1 Binds to Influenza Virus and Ameliorates Influenza Virus Pathogenesis ▿ Mei-Lin Yang 1 , † , Yu-Hung Chen 2 , † , Shainn-Wei Wang 3 , † , Yen-Jang Huang 1 , Chia-Hsing Leu 1 , Nai-Chi Yeh 4 , Chun-Yen Chu 5 , Chia-Cheng Lin 6 , Gia-Shing Shieh 7 , Yuh-Ling Chen 8 , Jen-Ren Wang 9 , Ching-Ho Wang 10 , Chao-Liang Wu 1 , 2 , * and Ai-Li Shiau 1 , 4 , * 1 Institute of Basic Medical Sciences 2 Department of Biochemistry and Molecular Biology 3 Institute of Molecular Medicine 4 Department of Microbiology and Immunology 8 Institute of Oral Medicine 9 Department of Medical Laboratory Science and Biotechnology, National Cheng Kung University Medical College, Tainan, Taiwan 5 Graduate Institute of Animal Vaccine Technology, National Pingtung University of Science and Technology, Pingtung, Taiwan 6 Department of Pathology 7 Department of Urology, Tainan Hospital 10 Department of Health, Executive Yuan, Taiwan; and School of Veterinary Medicine, National Taiwan University, Taipei, Taiwan 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.

Journal

Journal of VirologyAmerican Society For Microbiology

Published: Oct 1, 2011

References