Giuseppe
Emeritus
Macrophage Receptors for Influenza A Virus: Role of the Macrophage Galactose-type Lectin and Mannose Receptor in Viral Entry. (J Virol., abstract, edited)
13. J Virol. 2010 Jan 27. [Epub ahead of print]
Macrophage Receptors for Influenza A Virus: Role of the Macrophage Galactose-type Lectin and Mannose Receptor in Viral Entry.
Upham JP, Pickett D, Irimura T, Anders EM, Reading PC. - Department of Microbiology & Immunology, University of Melbourne, Victoria 3010, Australia; Laboratory of Cancer Biology and Molecular Immunology, Graduate School of Pharmaceutical Sciences, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan; WHO Collaborating Centre for Reference and Research on Influenza, Victorian Infectious Diseases Reference Laboratory, North Melbourne, Victoria 3051, Australia.
Although sialic acid has long been recognised as the primary receptor determinant for attachment of influenza virus to host cells, the specific receptor molecules that mediate viral entry are not known for any cell type. For the infection of murine macrophages by influenza virus, our earlier study indicated involvement of a C-type lectin, the macrophage mannose receptor (MMR), in this process. Here, we have used direct binding techniques to confirm and characterize the interaction of influenza virus with the MMR and to seek additional macrophage surface molecules that may have potential as receptors for viral entry. We identified the macrophage galactose-type lectin (MGL) as a second macrophage membrane C-type lectin that binds influenza virus and is known to be endocytic. Binding of influenza virus to MMR and MGL occurred independently of sialic acid through Ca(2+)-dependent recognition of viral glycans by the carbohydrate-recognition domains of the two lectins; influenza virus also bound to the sialic acid on MMR. Multivalent ligands of MMR and MGL inhibited influenza virus infection of macrophages in a manner that correlated with expression of these receptors on different macrophage populations. Influenza virus strain A/PR/8/34, which is poorly glycosylated and infects macrophages poorly, was not recognized by the C-type lectin activity of either MMR or MGL. We conclude that lectin-mediated interactions of influenza virus with MMR or MGL are required for endocytic uptake of the virus into macrophages and these lectins can thus be considered secondary or co-receptors with sialic acid for infection of this cell type.
PMID: 20106926 [PubMed - as supplied by publisher]
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13. J Virol. 2010 Jan 27. [Epub ahead of print]
Macrophage Receptors for Influenza A Virus: Role of the Macrophage Galactose-type Lectin and Mannose Receptor in Viral Entry.
Upham JP, Pickett D, Irimura T, Anders EM, Reading PC. - Department of Microbiology & Immunology, University of Melbourne, Victoria 3010, Australia; Laboratory of Cancer Biology and Molecular Immunology, Graduate School of Pharmaceutical Sciences, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan; WHO Collaborating Centre for Reference and Research on Influenza, Victorian Infectious Diseases Reference Laboratory, North Melbourne, Victoria 3051, Australia.
Although sialic acid has long been recognised as the primary receptor determinant for attachment of influenza virus to host cells, the specific receptor molecules that mediate viral entry are not known for any cell type. For the infection of murine macrophages by influenza virus, our earlier study indicated involvement of a C-type lectin, the macrophage mannose receptor (MMR), in this process. Here, we have used direct binding techniques to confirm and characterize the interaction of influenza virus with the MMR and to seek additional macrophage surface molecules that may have potential as receptors for viral entry. We identified the macrophage galactose-type lectin (MGL) as a second macrophage membrane C-type lectin that binds influenza virus and is known to be endocytic. Binding of influenza virus to MMR and MGL occurred independently of sialic acid through Ca(2+)-dependent recognition of viral glycans by the carbohydrate-recognition domains of the two lectins; influenza virus also bound to the sialic acid on MMR. Multivalent ligands of MMR and MGL inhibited influenza virus infection of macrophages in a manner that correlated with expression of these receptors on different macrophage populations. Influenza virus strain A/PR/8/34, which is poorly glycosylated and infects macrophages poorly, was not recognized by the C-type lectin activity of either MMR or MGL. We conclude that lectin-mediated interactions of influenza virus with MMR or MGL are required for endocytic uptake of the virus into macrophages and these lectins can thus be considered secondary or co-receptors with sialic acid for infection of this cell type.
PMID: 20106926 [PubMed - as supplied by publisher]
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