Identification of potyviral amorphous inclusion protein as a nonstructural, virus-specific protein related to helper component

Abstract

Antisera to amorphous inclusion (AI) proteins associated with infections by pepper mottle virus (PeMV) and the watermelon mosaic virus-1 strain of papaya ringspot virus (PRSV-W) were used to probe in vitro translation products of the viral RNAs. The major translation product of PeMV RNA in the rabbit reticulocyte lysate (RRL) system was a previously reported polypeptide of apparent molecular weight 78,000 ( M r 78K). It reacted with anti-AI serum, whereas the major translation product in the wheat germ (WG) system was a 30K polypeptide that did not react with the antiserum. These results, the M r values, and analyses of peptides generated by partial digestion with proteinase indicate that the amino acid sequences of the 30K polypeptide and the Mr 51K AI protein are distinct subsets of the 78K polypeptide amino acid sequence. Similar results were obtained with PRSV-W except that the M r values of the corresponding translation products are 110K (RRL) and 60K (WG). Thus the 5′-most region of the PeMV and PRSV-W RNAs (corresponding to 78K and 110K, respectively) appears to encode two proteins rather than one as previously supposed on the basis of RRL translation products. Reciprocal serological tests revealed that the tobacco vein mottling virus aphid transmission helper component protein was related to AI protein. There is direct evidence that the AI represent another potyviral-coded nonstructural protein and the first evidence that a biologically functional protein is related to a component of a potyviral inclusion.