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A GroEL homolog with a molecular mass of 60 kDa, produced by the primary endosymbiotic bacterium (aBuchnera sp.) ofMyzus persicae and released into the hemolymph, has previously been shown to be a key protein in the transmission of potato leafroll virus (PLRV). Like other luteoviruses and pea enation mosaic virus, PLRV readily binds to extracellularBuchnera GroEL, and in vivo interference in this interaction coincides with reduced capsid integrity and loss of infectivity. To gain more knowledge of the nature of the association between PLRV andBuchnera GroEL, thegroE operon of the primary endosymbiont ofM. persicae (MpBgroE ) and its flanking sequences were characterized and the PLRV-binding domain ofBuchnera GroEL was identified by deletion mutant analysis. MpB GroEL has extensive sequence similarity (92%) withEscherichia coli GroEL and other members of the chaperonin-60 family. The genomic organization of theBuchnera groE operon is similar to that of thegroE operon ofE. coli except that a constitutive promoter sequence could not be identified; only the heat shock promoter was present. By a virus overlay assay of protein blots, it was shown that purified PLRV bound as efficiently to recombinant MpB GroEL (expressed inE. coli ) as it did to wild-type MpB GroEL. Mutational analysis of the gene encoding MpB GroEL revealed that the PLRV-binding site was located in the so-called equatorial domain and not in the apical domain which is generally involved in polypeptide binding and folding.Buchnera GroEL mutants lacking the entire equatorial domain or parts of it lost the ability to bind PLRV. The equatorial domain is made up of two regions at the N and C termini that are not contiguous in the amino acid sequence but are in spatial proximity after folding of the GroEL polypeptide. Both the N- and C-terminal regions of the equatorial domain were implicated in virus binding.

Potato Leafroll Virus Binds to the Equatorial Domain of the Aphid Endosymbiotic GroEL Homolog