The N-terminal region of the luteovirus readthrough domain determines virus binding to Buchnera GroEL and is essential for virus persistence in the aphid.
Luteoviruses and the luteovirus-like pea enation mosaic virus (PEMV; genus Enamovirus) are transmitted by aphids in a circulative, nonreplicative manner. Acquired virus particles persist for several weeks in the aphid hemolymph, in which a GroEL homolog, produced by the primary endosymbiont of the aphid, is abundantly present. Six subgroup II luteoviruses and PEMV displayed a specific but differential affinity for Escherichia coli GroEL and GroEL homologs isolated from the endosymbiotic bacteria of both vector and nonvector aphid species. These observations suggest that the basic virus-binding capacity resides in a conserved region of the GroEL molecule, although other GroEL domains may influence the efficiency of binding. Purified luteovirus and enamovirus particles contain a major 22-kDa coat protein (CP) and lesser amounts of an approximately 54-kDa readthrough protein, expressed by translational readthrough of the CP into the adjacent open reading frame. Beet western yellows luteovirus (BWYV) mutants devoid of the readthrough domain (RTD) did not bind to Buchnera GroEL, demonstrating that the RTD (and not the highly conserved CP) contains the determinants for GroEL binding. In vivo studies showed that virions of these BWYV mutants were significantly less persistent in the aphid hemolymph than were virions containing the readthrough protein. These data suggest that the Buchnera GroEL-RTD interaction protects the virus from rapid degradation in the aphid. Sequence comparison analysis of the RTDs of different luteoviruses and PEMV identified conserved residues potentially important in the interaction with Buchnera GroEL.
van den Heuvel
J F
JF
Department of Virology, DLO Research Institute for Plant Protection (IPO-DLO), Wageningen, The Netherlands. J.F.J.M.vandenHeuvel@IPO.DLO.NL
Bruyère
A
A
Hogenhout
S A
SA
Ziegler-Graff
V
V
Brault
V
V
Verbeek
M
M
van der Wilk
F
F
Richards
K
K
D000595:Amino Acid Sequence; D000818:Animals; D001042:Aphids / Q000382:microbiology / Q000821:virology*; D001419:Bacteria / Q000821:virology; D018407:Bacterial Physiological Phenomena; D001937:Brassica; D002213:Capsid / Q000737:chemistry / Q000502:physiology*; D018834:Chaperonin 60 / Q000302:isolation & purification / Q000378:metabolism* / Q000648:ultrastructure; D017124:Conserved Sequence; D004926:Escherichia coli / Q000378:metabolism; D006458:Hemolymph / Q000821:virology; D017793:Luteovirus / Q000235:genetics / Q000502:physiology*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D018532:Pisum sativum / Q000821:virology; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity; D013559:Symbiosis
D018834:Chaperonin 60