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. 1994 Dec;68(12):7738–7745. doi: 10.1128/jvi.68.12.7738-7745.1994

Mutational analysis of the capsid protein of Leishmania RNA virus LRV1-4.

T L Cadd 1, K MacBeth 1, D Furlong 1, J L Patterson 1
PMCID: PMC237235  PMID: 7966563

Abstract

The virion of Leishmania RNA virus is predicted to be composed of a 742-amino-acid major capsid protein and a small percentage of capsid-polymerase fusion molecules. Recently, the capsid protein alone was expressed and shown to spontaneously assemble into viruslike particles. Since the major structural protein of the virion shell self-assembles into viruslike particles when expressed in the baculovirus expression system, assembly of the virion can be studied by mutational analysis and expression of a single open reading frame. In this study, several deletions and one addition of the capsid protein of Leishmania RNA virus LRV1-4 were generated. These mutants show different degrees of assembly. Assembly domains are being identified such that the capsid protein may be used as a macromolecular packaging and delivery system for Leishmania species.

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Selected References

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