TAILIEUCHUNG - Báo cáo khoa học: The binding of foot-and-mouth disease virus leader proteinase to eIF4GI involves conserved ionic interactions

The leader proteinase (L pro ) of foot-and-mouth disease virus (FMDV) ini-tially cleaves itself from the polyprotein. Subsequently, L pro cleaves the host proteins eukaryotic initiation factor (eIF) 4GI and 4GII. This prevents protein synthesis from capped cellular mRNAs; the viral RNA is still trans-lated, initiating from an internal ribosome entry site. L pro cleaves eIF4GI between residues G674 and R675. We showed previously, however, that L pro binds to residues 640–669 of eIF4GI. Binding was substantially improved when the eIF4GI fragment contained the eIF4E binding site and eIF4E was present in the binding assay | iFEBS Journal The binding of foot-and-mouth disease virus leader proteinase to eIF4GI involves conserved ionic interactions Nicole Foeger Elisabeth Kuehnelt Regina Cencic and Tim Skern Max F. Perutz Laboratories University Departments at the Vienna Biocenter Department of MedicalBiochemistry MedicalUniversity of Vienna Austria Keywords Foot-and-mouth disease virus papain-like proteinase self-processing exosite protein synthesis inhibition Correspondence T. Skern Max F. Perutz Laboratories University Departments at the Vienna Biocenter Department of Medical Biochemistry MedicalUniversity of Vienna Dr Bohr-Gasse 9 3 A-1030 Vienna Austria Fax 43 14277 9616 Tel 43 14277 61620 E-mail Website http medbch Present addresses Division of Cell Biology and tDivision of Tumour Genetics German Cancer Research Center Im Neuheimer Feld 280 D-69120 Heidelberg Germany Received 22 February 2005 revised 20 March 2005 accepted 24 March 2005 doi The leader proteinase Lpro of foot-and-mouth disease virus FMDV initially cleaves itself from the polyprotein. Subsequently Lpro cleaves the host proteins eukaryotic initiation factor elF 4GI and 4GII. This prevents protein synthesis from capped cellular mRNAs the viral RNA is still translated initiating from an internal ribosome entry site. Lpro cleaves eIF4GI between residues G674 and R675. We showed previously however that Lpro binds to residues 640-669 of eIF4GI. Binding was substantially improved when the eIF4GI fragment contained the eIF4E binding site and eIF4E was present in the binding assay. Lpro interacts with eIF4GI via residue C133 and residues 183-195 of the C-terminal extension. This binding domain lies about 25 A from the active site. Here we examined the binding of Lpro to eIF4GI fragments generated by in vitro translation to narrow the binding site down to residues 645-657 of human eIF4GI. Comparison of these amino acids with those in human .

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