HSV Mosaic protein (aa 140 - 170, 32 - 62) [GST], recombinant protein from E. coli
Recombinant HSV protein fused with a GST tag containing the C-terminal immunodominant regions from ORF65 140-170 a.a. and N-terminal regions from ORF8 32-62 a.a was expressed in E. coli and purified by proprietary chromatographic technique.
100mM NaCl, 0.1% SDS and 50% glycerol.
2-8°C short term, -20°C long term
Entry of HSV into the host cell involves interactions of several viral glycoproteins with cell surface receptors. The virus particle is covered by an envelope which, when bound to specific receptors on the cell surface, will fuse with the cell membrane and create an opening, or pore, through which the virus enters the host cell. The sequential stages of HSV entry are analagous to those of other viruses. At first, complementary receptors on the virus and cell surface bring the two membranes into proximity. In an intermediate state, the two membranes begin to merge, forming a hemifusion state. Finally, a stable entry pore is formed through which the viral envelope contents are introduced to the host cell.
A mosaic protein or peptide is an artificial recombinant protein designed from a set of reference protein sequences so that every constituent peptide (k-mer) is found some place in the set of input proteins. (For common usage, k-mer lengths correspond to T-cell epitope lengths.) Mosaics differ from other artificial recombinants, such as "peptide beads-on-a-string" or consensus sequences, because for the chosen value of k amino acids, there are no non-natural k-mers. Values of k between 9 and 12 are typically chosen because that is the size of epitopes recognized by cytotoxic T-cells.