tetano
Editor, Senior Moderator
J Virol. 2013 Nov 20. [Epub ahead of print]
The Macrophage Galactose-Type Lectin Can Function as an Attachment and Entry Receptor for Influenza Virus.
Ng WC, Liong S, Tate MD, Irimura T, Denda-Nagai K, Brooks AG, Londrigan SL, Reading PC.
Source
Department of Microbiology and Immunology, University of Melbourne, Victoria, 3010, Australia.
Abstract
Specific protein receptors that mediate internalization and entry of influenza A virus (IAV) have not been identified for any cell type. Sialic acid (SIA), the primary attachment factor for IAV hemagglutinin, is expressed by numerous cell-surface glycoproteins and glycolipids, confounding efforts to identify specific receptors involved in virus infection. Lec1 Chinese hamster ovary (CHO) epithelial cells express cell-surface SIA and bind IAV, yet are largely resistant to infection. Herein, we demonstrate that expression of the murine macrophage galactose-type lectin (MGL)-1 by Lec1 cells enhanced Ca2+-dependent IAV binding and restored permissivity to infection. Lec1 cells expressing MGL1 were infected in the presence or absence of cell-surface SIA, indicating that MGL1 can act as a primary receptor or as a co-receptor with SIA. Lec1 cells expressing endocytosis-deficient MGL1 mediated Ca2+-dependent IAV binding, but were less sensitive to IAV infection, indicating that direct internalization via MGL1 can result in cellular infection. Together, these studies identify MGL1 as a cell-surface glycoprotein that can act as an authentic receptor for both attachment and infectious entry of IAV.
PMID:
24257596
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24257596
The Macrophage Galactose-Type Lectin Can Function as an Attachment and Entry Receptor for Influenza Virus.
Ng WC, Liong S, Tate MD, Irimura T, Denda-Nagai K, Brooks AG, Londrigan SL, Reading PC.
Source
Department of Microbiology and Immunology, University of Melbourne, Victoria, 3010, Australia.
Abstract
Specific protein receptors that mediate internalization and entry of influenza A virus (IAV) have not been identified for any cell type. Sialic acid (SIA), the primary attachment factor for IAV hemagglutinin, is expressed by numerous cell-surface glycoproteins and glycolipids, confounding efforts to identify specific receptors involved in virus infection. Lec1 Chinese hamster ovary (CHO) epithelial cells express cell-surface SIA and bind IAV, yet are largely resistant to infection. Herein, we demonstrate that expression of the murine macrophage galactose-type lectin (MGL)-1 by Lec1 cells enhanced Ca2+-dependent IAV binding and restored permissivity to infection. Lec1 cells expressing MGL1 were infected in the presence or absence of cell-surface SIA, indicating that MGL1 can act as a primary receptor or as a co-receptor with SIA. Lec1 cells expressing endocytosis-deficient MGL1 mediated Ca2+-dependent IAV binding, but were less sensitive to IAV infection, indicating that direct internalization via MGL1 can result in cellular infection. Together, these studies identify MGL1 as a cell-surface glycoprotein that can act as an authentic receptor for both attachment and infectious entry of IAV.
PMID:
24257596
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24257596