Disulphide bond formation is essential for vaccinia virus late protein L1R function and for production of infectious progeny Public Deposited

http://ir.library.oregonstate.edu/concern/graduate_thesis_or_dissertations/1c18dj72m

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  • L1R, a myristylated late gene product of vaccinia virus, is essential for formation of infectious intracellular mature virions (IMV). In its absence, only viral particles arrested at an immature stage are detected and no infectious progeny virus are produced. Previous studies have shown that the L1R protein is exclusively associated with the IMV membrane and that myristylation is required for correct targeting. Furthermore, the L1R protein contains six cysteine amino acid residues that have all been shown to participate in intramolecular disulphide bonds. However, it was not clear what role, if any, the disulfide bonds play in the membrane topology of the L1R protein. To address this question, a comprehensive library of L1R mutants in which the cysteine residues had been mutated to serine (either individually or in combination) were tested for their ability to marker rescue a L1R conditional lethal mutant under non-permissive conditions. Much to our surprise, we determined that C57 was not essential for production of infectious IMV. These results suggest that protein disulphide isomerases may be involved in reorganization of disulfide bonds within L1R.
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