Dc. Baulcombe et al., SIGNAL FOR POTYVIRUS-DEPENDENT APHID TRANSMISSION OF POTATO AUCUBA MOSAIC-VIRUS AND THE EFFECT OF ITS TRANSFER TO POTATO VIRUS-X, Journal of General Virology, 74, 1993, pp. 1245-1253
A British isolate of potato aucuba mosaic potexvirus (PAMV) was transm
itted by aphids (Myzus persicae) which had fed previously on a source
of potato Y potyvirus (PVY). Nucleotide sequence analysis of the PAMV
coat protein gene indicated that amino acid residues 14 to 16 from the
N terminus of the coat protein have the sequence DAG, which is also f
ound in the coat proteins of potyviruses and is required for their aph
id transmissibility. A recombinant virus isolate (TXPA7) was produced
in which a segment of the coat protein gene of PAMV encoding the 40 N-
terminal amino acids was inserted in the genome of potato X potexvirus
(PVX) in place of the segment encoding the 28 N-terminal amino acids
of PVX coat protein. This isolate, and a second similar recombinant (T
XPA5) in which the DAG motif was changed to YTS, were mechanically tra
nsmissible to intact plants, in which they caused slightly milder symp
toms than PVX. Particles of TXPA7 reacted in immunosorbent electron mi
croscopy with PVX- and PAMV-specific antibodies and so were antigenica
lly distinguishable from PAMV and PVX particles, which reacted only wi
th their homologous antibody, and from TXPA5 particles, which reacted
only with the PVX antibody. Recombinant TXPA7 was transmitted by aphid
s that had already fed on a source of PVY whereas TXPA5 and PVX were n
ot. TXPA7 was not transmitted by aphids that had not fed on a PVY sour
ce. It is concluded that (i) the potyvirus-dependent aphid transmissib
ility of PAMV results from possession of a domain which includes the D
AG motif and is located near the N terminus of the virus coat protein,
and (ii) potyvirus-dependent aphid transmissibility can be conferred
on PVX, a non-aphid-borne potexvirus, by substituting this domain for
the N-terminal part of its coat protein.