Virion swelling is not required for cotranslational disassembly of cowpea chlorotic mottle virus in vitro.

F G Albert, J M Fox, M J Young
Author Information
  1. F G Albert: Department of Plant Pathology, Montana State University, Bozeman 59717, USA.

Abstract

The mechanism by which virions of cowpea chlorotic mottle virus (CCMV) disassemble and allow for translation of the virion RNA is not well understood. Previous models have suggested that virion swelling is required to expose the virion RNA for translation in a process referred to as cotranslational disassembly (M. Brisco, R. Hull, and T. M. A. Wilson, Virology 148:210-217, 1986; J. W. Roenhorst, J. W. M. van Lent, and B. J. M. Verduin, Virology 164:91-98, 1988; J. W. Roenhorst, J. M. Verduin, and R. W. Goldbach, Virology 168:138-146, 1989). Previous work in our laboratory has identified point mutations in the CCMV coat protein which result in virions with altered swelling characteristics (J. Fox, F. G. Albert, J. Speir, and M. J. Young, Virology 227:229-233, 1997; J. M. Fox, X. Zhao, J. A. Speir, and M. J. Young, Virology 222:115-122, 1996). The wild-type and mutant CCMV virions were used to correlate virion swelling with the ability of virion RNA to be translated in a cell-free wheat germ extract. Mutant virions unable to swell (cpK42R) are as infectious as wild-type virions in vivo, and the levels of translated encapsidated virion RNA are similar to those of wild-type virions in vitro. Mutant virions capable of swelling but not of disassembling in vitro (cpR26C) are noninfectious and have severely reduced levels of translation of the encapsidated virion RNA in vitro. These studies suggest that virion swelling is not required for the cotranslational disassembly of CCMV. Additionally, the results indicate that there is a pH-dependent structural transition in the virion, other than swelling, that results in the RNA's being exposed for translation in vitro. An alternative model suggesting that cotranslational disassembly of CCMV involves presentation of the virion RNA through the virion fivefold axis is proposed.

References

  1. Virology. 1989 Jan;168(1):138-46 [PMID: 2909987]
  2. J Virol. 1990 May;64(5):1934-45 [PMID: 2157861]
  3. Curr Opin Genet Dev. 1992 Feb;2(1):71-6 [PMID: 1378769]
  4. Structure. 1994 Apr 15;2(4):271-82 [PMID: 8087554]
  5. Virology. 1995 Mar 10;207(2):486-94 [PMID: 7886952]
  6. Virology. 1988 May;164(1):91-8 [PMID: 3363871]
  7. J Mol Biol. 1996 Aug 9;261(1):1-10 [PMID: 8760498]
  8. Virology. 1996 Aug 1;222(1):115-22 [PMID: 8806492]
  9. Virology. 1997 Jan 6;227(1):229-33 [PMID: 9007078]
  10. Virology. 1969 Jun;38(2):324-35 [PMID: 5784855]
  11. Virology. 1971 Sep;45(3):707-15 [PMID: 5166482]
  12. Structure. 1995 Jan 15;3(1):63-78 [PMID: 7743132]

MeSH Term

Cell-Free System
Gene Expression Regulation, Viral
Macromolecular Substances
Plant Viruses
Protein Biosynthesis
RNA, Viral
Virion

Chemicals

Macromolecular Substances
RNA, Viral

Word Cloud

Created with Highcharts 10.0.0virionJMvirionsswellingRNACCMVVirologyvitrotranslationcotranslationaldisassemblyWrequiredwild-typecowpeachloroticmottlevirusPreviousRRoenhorstVerduinFoxSpeirYoungtranslatedMutantlevelsencapsidatedresultsmechanismdisassembleallowwellunderstoodmodelssuggestedexposeprocessreferredBriscoHullTWilson148:210-2171986vanLentB164:91-981988Goldbach168:138-1461989worklaboratoryidentifiedpointmutationscoatproteinresultalteredcharacteristicsFGAlbert227:229-2331997XZhao222:115-1221996mutantusedcorrelateabilitycell-freewheatgermextractunableswellcpK42RinfectiousvivosimilarcapabledisassemblingcpR26CnoninfectiousseverelyreducedstudiessuggestAdditionallyindicatepH-dependentstructuraltransitionRNA'sexposedalternativemodelsuggestinginvolvespresentationfivefoldaxisproposedVirion

Similar Articles

Cited By