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. 1996 Jun;70(6):4045–4052. doi: 10.1128/jvi.70.6.4045-4052.1996

Chimeric hepatitis B virus core particles as probes for studying peptide-integrin interactions.

M A Chambers 1, G Dougan 1, J Newman 1, F Brown 1, J Crowther 1, A P Mould 1, M J Humphries 1, M J Francis 1, B Clarke 1, A L Brown 1, D Rowlands 1
PMCID: PMC190284  PMID: 8648742

Abstract

An RGD-containing epitope from the foot-and-mouth disease virus (FMDV) VP1 protein was inserted into the e1 loop of the hepatitis B virus core (HBc) protein. This chimeric protein was expressed at high levels in Escherichia coli and spontaneously assembled into virus-like particles which could be readily purified. These fusion particles elicited high levels of both enzyme-linked immunosorbent assay- and FMDV-neutralizing antibodies in guinea pigs. The chimeric particles bound specifically to cultured eukaryotic cells. Mutant particles carrying the tripeptide sequence RGE in place of RGD and the use of a competitive peptide, GRGDS, confirmed the critical involvement of the RGD sequence in this binding. The chimeric particles also bound to purified integrins, and inhibition by chain-specific anti-integrin monoclonal antibodies implicated alpha 5 beta 1 as a candidate cell receptor for both the chimeric particle and FMDV. Some serotypes of FMDV bound to beta 1 integrins in solid- phase assays, and the chimeric particles competed with FMDV for binding to susceptible eukaryotic cells. Thus, HBc particles may provide a simple, general system for exploring the interactions of specific peptide sequences with cellular receptors.

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Selected References

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