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Interaction of virions with membrane glycolipids

Marta Bally (Institutionen för teknisk fysik, Biologisk fysik) ; Kristian Dimitrievski (Institutionen för teknisk fysik, Kemisk fysik) ; Göran Larson ; Vladimir P. Zhdanov (Institutionen för teknisk fysik, Kemisk fysik) ; Fredrik Höök (Institutionen för teknisk fysik, Biologisk fysik)
Physical Biology (1478-3967). Vol. 9 (2012), 2, p. Article Number: 026011.
[Artikel, refereegranskad vetenskaplig]

Cellular membranes contain various lipids including glycolipids (GLs). The hydrophilic head groups of GLs extend from the membrane into the aqueous environment outside the cell where they act as recognition sites for specific interactions. The first steps of interaction of virions with cells often include contacts with GLs. To clarify the details of such contacts, we have used the total internal reflection fluorescence microscopy to explore the interaction of individual unlabelled virus-like particles (or, more specifically, norovirus protein capsids), which are firmly bound to a lipid bilayer, and fluorescent vesicles containing glycosphingolipids (these lipids form a subclass of GLs). The corresponding binding kinetics were earlier found to be kinetically limited, while the detachment kinetics were logarithmic over a wide range of time. Here, the detachment rate is observed to dramatically decrease with increasing concentration of glycosphingolipids from 1% to 8%. This effect has been analytically explained by using a generic model describing the statistics of bonds in the contact area between a virion and a lipid membrane. Among other factors, the model takes the formation of GL domains into account. Our analysis indicates that in the system under consideration, such domains, if present, have a characteristic size smaller than the contact area between the vesicle and the virus-like particle.

Nyckelord: intracellular viral kinetics, lipid rafts, infection pathway, enveloped, viruses, norwalk virus, single virus, monte-carlo, cell, entry, model

Denna post skapades 2012-05-24. Senast ändrad 2013-01-09.
CPL Pubid: 158005


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Institutioner (Chalmers)

Institutionen för teknisk fysik, Biologisk fysik (2007-2015)
Institutionen för teknisk fysik, Kemisk fysik (1900-2015)
Institutionen för biomedicin, avdelningen för klinisk kemi och transfusionsmedicin (GU)


Biofysikalisk kemi
Klinisk virologi
Klinisk laboratoriemedicin

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