Macromolecular diffusion is essential to cell function but largely restricted by the viscosity of the cytosol and the dense meshwork of cytoskeletal filaments. The fusion process requires the actions of viral glycoproteins gH, gL, and gB for entry into epithelial cells and additionally requires gp42 for entry into B cells. Utilizing the dissociation reaction and varying the concentration of the ionized form of caprylate, a specific amount of the nonionized form of caprylate was maintained over a wide pH range. Herpes simplex virus type 1 (HSV-1) requires four glycoproteins-glycoprotein D (gD), glycoprotein B (gB), and a heterodimer of glycoprotein H and L (gH/gL)-to accomplish fusion. Moreover, CD59 and HHV-6 envelope glycoprotein B showed the same localization through the confocal microscope. In addition, the presence of full-length pUL36 results in weak density that extends the CVSC toward the penton, suggesting either that this extra density is formed directly by pUL36 or that pUL36 stabilizes other components of the vertex-tegument interface. If this mechanism proves to be correct, 1-docosanol may provide a broad spectrum activity against many different viruses, especially those with lipid-containing envelopes.
The combined results of SPR and ESR showed a marked difference between the mode of action of the HSV peptides and the HIV fusion peptide compared to melittin, suggesting that viral-derived membrane interacting peptides all act via a similar mechanism, which is substantially different from that of the non-cell selective lytic peptide melittin. The nucleic acid coat or capsid. So it is me and Dick talking about virus structure.