Leporipoxvirus Cu-Zn superoxide dismutase homologs inhibit cellular superoxide dismutase, but are not essential for virus replication or virulence

Jing Xin Cao, Melissa LT Teoh-Fitzgerald, Mijin Moon, Grant McFadden, David H. Evans

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

Vertebrate poxviruses encode homologs of cellular cupro-zinc superoxide dismutases (Cu-Zn SOD). In this study we have examined the molecular genetic properties of two Cu-Zn SOD homologs encoded by the Shope fibroma virus (SFV) and myxoma virus. These Leporipoxvirus proteins should be catalytically inactive as judged by the point mutations which alter a key catalytic arginine and restructure the predicted Cu-binding domain. This prediction was confirmed using in situ gel assays and recombinant proteins produced both in bacteria and in mammalian cells. Western blot analysis showed that these proteins are produced in abundance late in infection and can, upon exposure to oxidizing conditions, form disulfide cross-linked dimers. They are also virion components and not essential for growth in culture or virulence. Leporipoxvirus Cu-Zn SOD homologs affected two phenotypes. First, deletion of the myxoma M131R gene caused the mutant virus to grow better (∼10-fold) in culture than does the wild-type parent. Second, expression of either native or recombinant Leporipoxvirus proteins is accompanied by a decline in cellular Cu-Zn SOD activity. We concluded that these gene products can somehow modulate the activity of host Cu-Zn SODs, but what advantage is thus gained by the virus remains to be established.

Original languageEnglish (US)
Pages (from-to)125-135
Number of pages11
JournalVirology
Volume296
Issue number1
DOIs
StatePublished - Jan 1 2002

Fingerprint

Leporipoxvirus
Virus Replication
Superoxide Dismutase
Virulence
Zinc
Recombinant Proteins
Rabbit Fibroma Virus
Myxoma virus
Viruses
Poxviridae
Myxoma
Point Mutation
Disulfides
Virion
Genes
Arginine
Vertebrates
Molecular Biology
Proteins
Western Blotting

Keywords

  • A45R
  • Cu-Zn SOD
  • M131R
  • Myxoma virus
  • S131R
  • Shope fibroma virus
  • Vaccinia virus

ASJC Scopus subject areas

  • Virology

Cite this

Leporipoxvirus Cu-Zn superoxide dismutase homologs inhibit cellular superoxide dismutase, but are not essential for virus replication or virulence. / Cao, Jing Xin; Teoh-Fitzgerald, Melissa LT; Moon, Mijin; McFadden, Grant; Evans, David H.

In: Virology, Vol. 296, No. 1, 01.01.2002, p. 125-135.

Research output: Contribution to journalArticle

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