Cross-functional analysis of the Microviridae internal scaffolding protein

April D. Burch, Josephine Ta, Bentley A. Fane

Research output: Contribution to journalArticlepeer-review

37 Scopus citations


The assembly of the viral structural proteins into infectious virions is often mediated by scaffolding proteins. These proteins are transiently associated with morphogenetic intermediates but not found in the mature particle. The genes encoding three Microviridae (∅X174, G4 and α3) internal scaffolding proteins (B proteins) have been cloned, expressed in vivo and assayed for the ability to complement null mutations of different Microviridae species. Despite divergence as great as 70% in amino acid sequence over the aligned length, cross-complementation was observed, indicating that these proteins are capable of directing the assembly of foreign structural proteins into infectious particles. These results suggest that the Microviridae internal scaffolding proteins may be inherently flexible. There was one condition in which a B protein could not cross-function. The ∅X174 B protein cannot productively direct the assembly of the G4 capsid at temperatures above 21°C. Under these conditions, assembly is arrested early in the morphogenetic pathway, before the first B protein mediated reaction. Two G4 mutants, which can productively utilize the ∅X174 B protein at elevated temperatures, were isolated. Both mutations confer amino acid substitutions in the viral coat protein but differ in their relative abilities to utilize the foreign scaffolding protein. The more efficient substitution is located in a region where coat-scaffolding interactions have been observed in the atomic structure and may emphasize the importance of interactions in this region.

Original languageEnglish (US)
Pages (from-to)95-104
Number of pages10
JournalJournal of Molecular Biology
Issue number1
StatePublished - Feb 12 1999


  • Scaffolding proteins
  • Viral assembly
  • ∅X174

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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