Decay-accelerating factor binding determines the entry route of echovirus 11 in polarized epithelial cells

Autor: Amanda D. Stuart, Laura Rubbia-Brandt, Komla Sobo, Thomas Alexander Mckee, T. D. K. Brown
Rok vydání: 2011
Předmět:
media_common.quotation_subject
Immunoblotting
Immunology
Mutant
Epithelial Cells/virology
Fluorescent Antibody Technique
Beta-Cyclodextrins
Plasma protein binding
ddc:616.07
Biology
Virus Replication
Microbiology
Enterovirus B
Human/drug effects/metabolism/pathogenicity
Tight Junctions
03 medical and health sciences
Virology
Cell polarity
Enterovirus Infections
Humans
Internalization
Decay-accelerating factor
Cholesterol/deficiency
030304 developmental biology
media_common
0303 health sciences
CD55 Antigens
Tight junction
beta-Cyclodextrins
030302 biochemistry & molecular biology
Beta-Cyclodextrins/pharmacology
Cell Polarity
Epithelial Cells
Virus Internalization
Apical membrane
Molecular biology
Virus-Cell Interactions
Enterovirus B
Human
3. Good health
Cell biology
Virus Internalization/drug effects
Cholesterol
Enterovirus Infections/metabolism/virology
Insect Science
Antigens
CD55/metabolism
Tight Junctions/metabolism
Caco-2 Cells
Protein Binding
Zdroj: Journal of virology
Journal of Virology, Vol. 85, No 23 (2011) pp. 12376-86
ISSN: 0022-538X
DOI: 10.1128/JVI.00016-11
Popis: The interaction between echovirus 11 strain 207 (EV11-207) and decay-accelerating factor (DAF or CD55) at the apical surface of polarized Caco-2 cells results in rapid transport of the virus to tight junctions and in its subsequent uptake. A virus mutant (EV11-207R) which differs at 6 amino acids and whose affinity for DAF is apparently significantly lower remains at the apical surface, from where its uptake occurs. Binding of EV11-207 to DAF and its transport to tight junctions result in a loss of function of the junctions. In contrast, the mutant virus EV11-207R is not transferred to tight junctions, nor does it impair the integrity of these junctions. Cholesterol depletion from the apical membrane leads to DAF aggregation and, presumably, internalization and inhibits infection by EV11-207. However, infection by EV11-207R is significantly less sensitive to cholesterol depletion than infection by EV11-207, confirming the DAF requirement for EV11-207, but not EV11-207R, to infect cells. These data strongly indicate that in the case of infection of polarized epithelial cells by echovirus 11, DAF binding appears be a key determinant in the choice of entry pathway, at least in cell culture.
Databáze: OpenAIRE
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