作者: R Adams , M D Davison , C A MacLean , A J Davison , C Cunningham
DOI: 10.1099/0022-1317-79-4-813
关键词: Gene 、 Biology 、 N-terminus 、 Vesicle-associated membrane protein 8 、 Virology 、 HSPA2 、 Mutant 、 Biochemistry 、 Herpes simplex virus 、 Viral tegument 、 Signal peptide
摘要: Herpes simplex virus type 1 (HSV-1) gene UL49A potentially encodes a primary translation product of 91 residues with signal sequence at the N terminus and membrane anchor domain near C terminus. Mutants were generated in this utilized to characterize encoded protein on SDS-PAGE as 6.7 kDa species which fractionated infected cell membranes, was relatively abundant virion component, not detectably O-glycosylated. The identified by microsequencing 68 residue polypeptide formed removal 23 from product. Cleavage also demonstrated vitro transcription presence microsomal membranes. efficiently solubilized along envelope proteins treatment virions non-ionic detergent but only reducing agent, suggesting that it may be an is disulphide-linked tegument. It apparent mutational analysis 10 amino acid are essential for synthesis protein, cleavage, targeting membranes virions, linkage tegument growth culture.