DC-SIGN and Influenza Hemagglutinin Dynamics in Plasma Membrane Microdomains Are Markedly Different

DC-SIGN, a Ca2+-dependent transmembrane lectin, is found assembled in microdomains on the plasma membranes of dendritic cells. These microdomains bind a large variety of pathogens and facilitate their uptake for subsequent antigen presentation. In this study, DC-SIGN dynamics in microdomains were ex...

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Bibliographic Details
Published in:Biophysical journal 2011-06, Vol.100 (11), p.2662-2670
Main Authors: Itano, Michelle S., Neumann, Aaron K., Liu, Ping, Zhang, Feng, Gratton, Enrico, Parak, Wolfgang J., Thompson, Nancy L., Jacobson, Ken
Format: Article
Language:English
Subjects:
Antigen presentation
Antigens
Cell Adhesion Molecules - chemistry
Cell Adhesion Molecules - metabolism
Clathrin - metabolism
dendritic cells
Endocytosis
fluorescence
fluorescence microscopy
Hemagglutinin Glycoproteins, Influenza Virus - chemistry
Hemagglutinin Glycoproteins, Influenza Virus - metabolism
hemagglutinins
image analysis
Influenza
lectins
Lectins, C-Type - chemistry
Lectins, C-Type - metabolism
Lipids
Mannose-Binding Lectins - metabolism
Membrane
Membrane Microdomains - metabolism
Membrane Proteins - metabolism
Membranes
Movement
Nerve Tissue Proteins - metabolism
Pathogens
photobleaching
Plasma
plasma membrane
Protein Transport
Proteins
Quantum Dots
Receptors, Cell Surface - chemistry
Receptors, Cell Surface - metabolism
spectroscopy
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Summary:DC-SIGN, a Ca2+-dependent transmembrane lectin, is found assembled in microdomains on the plasma membranes of dendritic cells. These microdomains bind a large variety of pathogens and facilitate their uptake for subsequent antigen presentation. In this study, DC-SIGN dynamics in microdomains were explored with several fluorescence microscopy methods and compared with dynamics for influenza hemagglutinin (HA), which is also found in plasma membrane microdomains. Fluorescence imaging indicated that DC-SIGN microdomains may contain other C-type lectins and that the DC-SIGN cytoplasmic region is not required for microdomain formation. Fluorescence recovery after photobleaching measurements showed that neither full-length nor cytoplasmically truncated DC-SIGN in microdomains appreciably exchanged with like molecules in other microdomains and the membrane surround, whereas HA in microdomains exchanged almost completely. Line-scan fluorescence correlation spectroscopy indicated an essentially undetectable lateral mobility for DC-SIGN but an appreciable mobility for HA within their respective domains. Single-particle tracking with defined-valency quantum dots confirmed that HA has significant mobility within microdomains, whereas DC-SIGN does not. By contrast, fluorescence recovery after photobleaching indicated that inner leaflet lipids are able to move through DC-SIGN microdomains. The surprising stability of DC-SIGN microdomains may reflect structural features that enhance pathogen uptake either by providing high-avidity platforms and/or by protecting against rapid microdomain endocytosis.
ISSN:0006-3495
1542-0086
DOI:10.1016/j.bpj.2011.04.044