Endocytic function is critical for influenza A virus infection via DC-SIGN and L-SIGN
Gillespie, L Roosendahl, P Ng, W.C Brooks, A.G Reading, P.C Londrigan, S.L
Gillespie, L
Roosendahl, P
Brooks, A.G
Reading, P.C
Londrigan, S.L
Citations
Altmetric:
Alternative Title
Abstract
The ubiquitous presence of cell-surface sialic acid (SIA) has complicated efforts to identify specific transmembrane glycoproteins that function as bone fide entry receptors for influenza A virus (IAV) infection. The C-type lectin receptors (CLRs) DC-SIGN (CD209) and L-SIGN (CD209L) enhance IAV infection however it is not known if they act as attachment factors, passing virions to other unknown receptors for virus entry, or as authentic entry receptors for CLR-mediated virus uptake and infection. Sialic acid-deficient Lec2 Chinese Hamster Ovary (CHO) cell lines were resistant to IAV infection whereas expression of DC-SIGN/L-SIGN restored susceptibility of Lec2 cells to pH- and dynamin-dependent infection. Moreover, Lec2 cells expressing endocytosis-defective DC-SIGN/L-SIGN retained capacity to bind IAV but showed reduced susceptibility to infection. These studies confirm that DC-SIGN and L-SIGN are authentic endocytic receptors for IAV entry and infection.
Keywords
cell adhesion molecule, cell surface receptor, DC-specific ICAM-3 grabbing nonintegrin, dynamin, lectin, n acetylneuraminic acid, virus receptor, animal, cell line, chemistry, CHO cell line, Cricetulus, dog, endocytosis, gene expression, genetics, Influenza A virus, metabolism, mutation, pH, physiology, virus attachment, virus entry, Animals, Cell Adhesion Molecules, Cell Line, CHO Cells, Cricetulus, Dogs, Dynamins, Endocytosis, Gene Expression, Hydrogen-Ion Concentration, Influenza A virus, Lectins, C-Type, Mutation, N-Acetylneuraminic Acid, Receptors, Cell Surface, Receptors, Virus, Virus Attachment, Virus Internalization
Source Title
Scientific Reports
Publisher
Series/Report No.
Collections
Rights
Attribution 4.0 International
Date
2016
DOI
10.1038/srep19428
Type
Article