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Aromatic interactions define the binding of the alphavirus spike to its nucleocapsid

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Author

Summary, in English

Background: Most enveloped viruses bud from infected cells by a process in which viral intracellular core components interact with cytoplasmic domains of transmembrane spike glycoproteins. We have demonstrated previously that a tyrosine motif in the cytoplasmic domain of the Semliki Forest virus (SFV) spike glycoprotein E2 is absolutely essential for budding, In contrast, hardly anything is known regarding which region of the capsid protein is involved in spike binding, Therefore, the mechanism by which spikes are selectively sorted into the viral bud or by which energy is provided for envelopment, remains unclear, Results: Molecular models of the SFV capsid protein (SFCP) and the cytoplasmic domain of the spike protein were fitted as a basis for a reverse genetics approach to characterizing the interaction between these two proteins: Biochemical analysis of mutants defined a hydrophobic pocket of the capsid protein that is involved both in spike binding and nucleocapsid assembly, Conclusions: We suggest that aromatic residues in the capsid protein serve to bind the side chain of the essential E2 tyrosine providing both specificity for spike incorporation and energy for budding. The same hydrophobic pocket also appears to play a role in capsid assembly. Furthermore, the results suggest that budding may occur in the absence of preformed nucleocapsids. This is the first demonstration of the molecular mechanisms of spike-nucleocapsid interactions during virus budding.

Publishing year

1996

Language

English

Pages

519-529

Publication/Series

Structure

Volume

4

Issue

5

Document type

Journal article

Publisher

Cell Press

Topic

  • Medical Genetics

Keywords

  • alphavirus
  • Semliki Forest virus
  • tyrosine signal
  • virus assembly
  • virus
  • budding

Status

Published

ISBN/ISSN/Other

  • ISSN: 0969-2126