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Interaction of Virus-Like Particles with Vesicles Containing Glycolipids: Kinetics of Detachment

Waqas Nasir ; Marta Bally (Institutionen för teknisk fysik, Biologisk fysik) ; Vladimir P. Zhdanov (Institutionen för teknisk fysik, Biologisk fysik) ; Göran Larson ; Fredrik Höök (Institutionen för teknisk fysik, Biologisk fysik)
The Journal of Physical Chemistry B (1520-6106). Vol. 119 (2015), 35, p. 11466-11472.
[Artikel, refereegranskad vetenskaplig]

Many viruses interact with their host cells via glycosphingolipids (GSLs) and/or glycoproteins present on the outer cell membrane. This highly specific interaction includes virion attachment and detachment. The residence time determined by the detachment is particularly interesting, since it is directly related to internalization and infection as well as to virion egress and spreading. In an attempt to deepen the understanding of virion detachment kinetics, we have used total internal reflection fluorescence (TIRF) microscopy to probe the interaction between individual fluorescently labeled GSL-containing lipid vesicles and surface-bound virus-like particles (VLPs) of a norovirus genotype II.4 strain. The distribution of the VLP-vesicle residence time was investigated for seven naturally occurring GSLs, all of which are candidates for the not yet identified receptor(s) mediating norovirus entry into host cells. As expected for interactions involving multiple GSL binding sites at a viral capsid, the detachment kinetics displayed features typical for a broad activation-energy distribution for all GSLs. Detailed inspection of these distributions revealed significant differences among the different GSLs. The results are discussed in terms of strength of the interaction, vesicle size, as well as spatial distribution and clustering of GSLs in the vesicle membrane. (Figure Presented).

Denna post skapades 2015-09-28. Senast ändrad 2015-10-21.
CPL Pubid: 223289


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Institutioner (Chalmers)

Institutionen för biomedicin, avdelningen för klinisk kemi och transfusionsmedicin (GU)
Institutionen för teknisk fysik, Biologisk fysik (2007-2015)



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