Herpes simplex virus-1 (HSV-1) is a ubiquitous virus which is implicated in diseases ranging from self-curing cold sores to life-threatening infections. The 2500 Å diameter herpes virion is composed of a glycoprotein spike containing, lipid envelope, enclosing a protein layer (the tegument) in which is embedded the capsid (which contains the dsDNA genome). The B-, and A- and C-capsids, representing different morphogenetic stages in HSV-1 infected cells, are composed of 7, and 5 structural proteins respectively. The three capsid types are organized in similar T=16 icosahedral shells with 12 pentons, 150 hexons, and 320 connecting triplexes. Our previous 3D structure study at 26 Å revealed domain features of all these structural components and suggested probable locations for the outer shell proteins, VP5, VP26, VP19c and VP23. VP5 makes up most of both pentons and hexons. VP26 appeared to bind to the VP5 subunit in hexon but not to that in penton.
Low‐fat fermented milk with a combination of fructo‐oligosaccharides and live Lactobacillus rhamnosus GG (ATCC 53103), Streptococcus thermophilus (Z57) and Lactobacillus bulgaricus (LB2), and defence against reactivation of Herpes simplex virus in the orolabial epithelia: evaluation of a health claim pursuant to Article 13(5) of Regulation (EC) No 1924/2006
