Mutational analysis of the capsid protein of Leishmania RNA virus LRV1-4.
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.
Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts.
T L
TL
Cadd
K
K
MacBeth
D
D
Furlong
J L
JL
Patterson
D000818:Animals; D001483:Base Sequence; D002213:Capsid / Q000096:biosynthesis* / Q000302:isolation & purification; D003001:Cloning, Molecular; D017931:DNA Primers; D004587:Electrophoresis, Agar Gel; D007891:Leishmania / Q000821:virology*; D008969:Molecular Sequence Data; D016296:Mutagenesis; D016366:Open Reading Frames; D016133:Polymerase Chain Reaction; D012328:RNA Viruses / Q000378:metabolism* / Q000648:ultrastructure; D015183:Restriction Mapping; D017384:Sequence Deletion; D014771:Virion / Q000378:metabolism / Q000648:ultrastructure
D017931:DNA Primers