Reports

Unusual Aggregation of a Nonfunctional Tobacco Mosaic Virus Protein

Science  27 Mar 1964:
Vol. 143, Issue 3613, pp. 1451-1452
DOI: 10.1126/science.143.3613.1451

Abstract

The nonfunctional virus protein isolated from plants infected with the PM2 strain of tobacco mosaic virus aggregates to form elongated, two-stranded, open helical structures, in marked contrast with functional tobacco mosaic virus protein which aggregates into rods. This unique type of aggregation may explain why the PM2 protein is unable to combine with viral nucleic acid to form stable infectious virus particles.

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