Serological relationships between the cylindrical inclusion proteins of potyviruses

Antisera to the cytoplasmic inclusion proteins (CIPs) of bean yellow mosaic (BYMV), clover yellow vein (ClYVV), turnip mosaic (TuMV), sweet potato feathery mottle (SPFMV), and maize dwarf mosaic (MDMV) potyviruses were used to examine the relationships between the CIPs of 18 potyviruses. The antisera to CIPs of BYMV, ClYVV, TuMV, and SPFMV cross-reacted to most or all of the purified CIPs tested in western blot assays. The MDMV CIP antiserum reacted significantly only to the MDMV and sorghum mosaic virus CIPs. Reactivity of antisera to CIPs of dicot-infecting viruses was generally higher with CIPs of other dicot-infecting than with monocot-infecting potyvirus CIPs. Analysis of amino acid sequences of the CI genes of 11 well-characterized potyviruses suggested that epitopes specific for individual potyviruses are primarily in the C-terminal domains of the CIP, whereas epitopes shared among different viruses are clustered in the N-terminal domains. The most highly conserved predicted epitope overlaps the nucleotide binding motif of the N-terminal helicase domain of the CIP. Antibodies to this domain will probably be present in antisera to any potyvirus CIP and contribute to the cross-reactivity observed. Differences in the C-terminal domains may correlate with interactions between the CIP and coat protein necessary for replication and movement.