2A Proteinases of Coxsackie- and Rhinovirus Cleave Peptides Derived from eIF-4γ via a Common Recognition Motif

• Published in: Virology (New York, N.Y.) Vol. 198; no. 2; pp. 741 - 745
• Main Authors: Sommergruber, W., Ahorn, H., Klump, H., Seipelt, J., Zoephel, A., Fessl, F., Krystek, E., Blaas, D., Kuechler, E., Liebig, H.D., Skern, T.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.02.1994
• Subjects: Amino Acid Sequence; Cysteine Endopeptidases - metabolism; Enterovirus B, Human - enzymology; Molecular Sequence Data; Peptide Fragments - metabolism; Peptide Initiation Factors - metabolism; Rhinovirus - enzymology; Species Specificity; Substrate Specificity; Viral Proteins
• ISSN: 0042-6822; 1096-0341
• DOI: 10.1006/viro.1994.1089

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 clearable peptides to be designed using the common motif Ile/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-4γ; 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-4γ [B. J. Lamphear et al. (1993) J. Biol. Chem. 268, 19200-19203]. This supports the hypothesis that cleavage of eIF-4γ by picornaviral 2A proteinases occurs directly.