Analysis of the lipid composition of influenza virus–infected cells provides support for the membrane raft-based biogenesis model.

We document a new dimension of surface recognition in which communication is controlled through the collective behavior of lipids. Membrane cholesterol induces a tilt in glycolipid receptor headgroup, resulting in loss of access for ligand binding. This property appears to organize erythrocyte blood group presentation and glycolipid receptor function during the activation of sperm fertility, suggesting that lipid 'allostery' is a means to regulate membrane recognition processes.

The lung is a preferential (Gb(3)) "sink" for VT1, which explains the relatively slower clearance of VT2 and subsequent increased VT2 renal targeting and VT2 mortality in this animal model.

The glycosphingolipid globotriaosyl ceramide, (Galα1‐4Galß1‐4 glucosyl ceramide‐Gb3) also known as CD77 and the Pk blood group antigen, is bound by both verotoxins and by the HIV adhesin, gp120. Gb3 plays an important receptor role in VT induced hemolytic uremic syndrome (HUS) and HIV infection. The organization of glycolipids, including Gb3, into lipid rafts is central to both pathologies. The fatty acid heterogeneity within the Gb3 lipid moiety plays a central role in assembly within such ordered domains. Differential binding of verotoxins and gp120 to such Gb3 isoforms in model and cell membranes indicates a significant role in the eventual pathogenic outcome. HUS may provide the first example whereby membrane Gb3 organization provides a predictor for tissue selective in vivo pathology.