Herpes simplex virus type-1 structural proteins were solubilized in formic acid and purified by reverse-phase high performance liquid chromatography. D., Mancini, P., Davis, F. In addition, several tegument proteins were found in high-molecular-weight complexes, including VP22, UL36, and UL37. The dileucine motifs were also required for proper cytoplasmic localization of VP22 itself and for optimal expression of viral proteins VP16, VP22, ICP0, UL41, and glycoprotein B. Nelson, D. In fact, this region of VP22 is sufficient to bind to gE in the absence of additional viral proteins. Further dissociation occurred within the axons and the cytosol as the capsids moved to the nucleus, resulting in the release of free tegument proteins, especially VP16, VP22, pUL37, and some pUL36, into the cytosol.
For example, if the current year is 2008 and a journal has a 5 year moving wall, articles from the year 2002 are available. In contrast, there are large gaps in the corresponding region of the procapsid, implying that formation of the floor involves extensive remodeling. While the site of final tegument and envelope assembly has been controversial Enquist et al., 1998 and Mettenleiter, 2002, recent genetic, biochemical, and ultrastructural data suggest that Herpes simplex virus type 1 (HSV-1) capsids acquire their final envelope and tegument layer by budding into the trans-Golgi network (TGN) or endosomes Browne et al., 1996a, Brunetti et al., 1998, Whiteley et al., 1999, Harley et al., 2001, Skepper et al., 2001, McMillan and Johnson, 2001 and Miranda-Saksena et al., 2002. Eisenberg, R.