Importance of disulphide bonds for vaccinia virus L1R protein function

<p>Abstract</p> <p>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 is produced. Prev...

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Main Authors: Hruby Dennis E, Byrd Chelsea M, Blouch Robert E
Format: Article
Language:English
Published: BMC 2005-12-01
Series:Virology Journal
Online Access:http://www.virologyj.com/content/2/1/91
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author Hruby Dennis E
Byrd Chelsea M
Blouch Robert E
author_facet Hruby Dennis E
Byrd Chelsea M
Blouch Robert E
author_sort Hruby Dennis E
collection DOAJ
description <p>Abstract</p> <p>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 is produced. Previous studies have shown that the L1R protein is exclusively associated with the IMV membrane and that myristylation is required for correct targeting. 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 have been mutated to serine (either individually or in combination) were tested for their ability to rescue a L1R conditional lethal mutant virus 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 the L1R protein.</p>
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spelling doaj.art-b9ea1058d6604d7993211528cbda1ae72022-12-22T03:17:59ZengBMCVirology Journal1743-422X2005-12-01219110.1186/1743-422X-2-91Importance of disulphide bonds for vaccinia virus L1R protein functionHruby Dennis EByrd Chelsea MBlouch Robert E<p>Abstract</p> <p>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 is produced. Previous studies have shown that the L1R protein is exclusively associated with the IMV membrane and that myristylation is required for correct targeting. 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 have been mutated to serine (either individually or in combination) were tested for their ability to rescue a L1R conditional lethal mutant virus 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 the L1R protein.</p>http://www.virologyj.com/content/2/1/91
spellingShingle Hruby Dennis E
Byrd Chelsea M
Blouch Robert E
Importance of disulphide bonds for vaccinia virus L1R protein function
Virology Journal
title Importance of disulphide bonds for vaccinia virus L1R protein function
title_full Importance of disulphide bonds for vaccinia virus L1R protein function
title_fullStr Importance of disulphide bonds for vaccinia virus L1R protein function
title_full_unstemmed Importance of disulphide bonds for vaccinia virus L1R protein function
title_short Importance of disulphide bonds for vaccinia virus L1R protein function
title_sort importance of disulphide bonds for vaccinia virus l1r protein function
url http://www.virologyj.com/content/2/1/91
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