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J Gen Virol 38 (1978), 505-518; DOI 10.1099/0022-1317-38-3-505
© 1978 Society for General Microbiology
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An Infective Pyridoxyl-derivative of Potato Virus X: PVX-PLP

W. S. Pierpoint and J. M. Carpenter

Departments of Biochemistry and Plant Pathology, Rothamsted Experimental Station, Harpenden, Herts. AL5 2JQ, U.K.

The reduced initial product (PVX-PLP) of the reaction of pyridoxyl 5'-phosphate (PLP) and particles of potato virus X (PVX) contains about 1 (0.6 to 1.2) molecules of PLP per protein subunit and is infective. Hydrolysates of the protein contain N-{varepsilon}-pyridoxyl-lysine. PVX-PLP reacts with chlorogenoquinone to 1/4 of the extent of PVX; similarly, PVX which has reacted with chlorogenoquinone (PVX-Q1) binds only 1/3 to 1/5 as much PLP as does PVX. PVX-PLP contains two types of fluorescent subunit which can be separated by electrophoresis in SDS-acrylamide gels: one of these is fluorescent and is not degraded by brief exposure to trypsin, whereas the other is degraded to a smaller form which is also fluorescent. Tryptic digests of the protein from PVX-PLP contain at least two fluorescent peptides. It is argued that PLP reacts with two lysine {varepsilon}-amino groups of PVX, one of which also reacts with chlorogenoquinone, and the other of which is recognized by trypsin.

Protein isolated from PVX reacts with up to 6 molecules of PLP. The conformation of the subunits in the intact virus apparently makes many {varepsilon}-amino groups inaccessible to PLP.

Received 1 July 1977; accepted 30 September 1977.




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Copyright © 1978 by the Society for General Microbiology.