| Title | 2A proteinases of coxsackie- and rhinovirus cleave peptides derived from eIF-4 gamma via a common recognition motif. | ||
| Author | Sommergruber, W; Ahorn, H; Klump, H; Seipelt, J; Zoephel, A; Fessl, F; Krystek, E; Blaas, D; Kuechler, E; Liebig, H D | ||
| Journal | Virology | Publication Year/Month | 1994-Feb |
| PMID | 8291255 | PMCID | -N/A- |
| Affiliation | 1.BENDER+CO Ges mbH, Ernst Boehringer Institut fuer Arzneimittelforschung, Vienna, Austria. | ||
The cleavage specificities of the 2A proteinases from coxsackievirus B4 (CVB4) and human rhinovirus 2 (HRV2) on oligopeptide substrates have been determined. Comparison of the specificity of CVB4 2A proteinase with that of HRV2 2A proteinase allowed cleavable peptides to be designed using the common motif IIe/Leu-X-Thr-X*Gly; little resemblance to the viral cleavage site remained. The data also allowed the prediction of three possible cleavage sites for 2A proteinases on eIF-4 gamma; two peptides derived from these sequences were cleaved by both 2A proteinases. One of these peptides corresponds to the cleavage site for 2A proteinases mapped on eIF-4 gamma [B. J. Lamphear et al. (1993) J. Biol. Chem. 268, 19200-19203]. This supports the hypothesis that cleavage of eIF-4 gamma by picornaviral 2A proteinases occurs directly.