Bacteriophage φ6 envelope elucidated by chemical cross-linking, immunodetection, and cryoelectron microscopy

John M. Kenney, Jarkko Hantula, Stephen D. Fuller, Leonard Mindich, Päivi M. Ojala, Dennis H. Bamford

Research output: Contribution to journalArticlepeer-review

38 Scopus citations

Abstract

Bacteriophage φ6 is an enveloped dsRNA virus which infects the plant pathogenic Pseudomonas syringae bacterium. Using low dose cryoelectron microscopy we show that the nucleocapsid, spikeless virion, and intact virion have radii of 29, 35, and 43 nm, respectively. Thus, the membrane is 6 nm thick and the surface spikes of the receptor binding protein P3 extend 8 nm from the membrane surface. Cross-linking, immunological, and complementation evidence suggest that the spikes are formed of multimeric P3 molecules and that P3 is associated with membrane-bound protein P6. We observe that the envelope can accommodate up to 400 molecules of P3 but that the average virion contains less than one-fourth of this amount. Assembly of a very small number of P3 or truncated P3 molecules onto inactive virions restores infectivity, showing that only a few spikes are necessary for receptor binding and membrane fusion.

Original languageEnglish (US)
Pages (from-to)635-644
Number of pages10
JournalVirology
Volume190
Issue number2
DOIs
StatePublished - Oct 1992

All Science Journal Classification (ASJC) codes

  • Virology

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