Eukaryotic initiation factor 4GI is a poor substrate for HIV-1 proteinase

FEBS Lett. 2002 Oct 9;529(2-3):337-40. doi: 10.1016/s0014-5793(02)03415-4.

Abstract

Eukaryotic initiation factor (eIF) 4GI is efficiently cleaved during picornaviral replication. eIF4GI processing has also recently been observed during HIV-1 replication. We have compared the efficiency of eIF4GI proteolysis in rabbit reticulocyte lysates during translation of mRNAs encoding the foot-and-mouth disease virus leader proteinase (L(pro)) or the HIV-1 proteinase (HIV-1(pro)). L(pro) cleaved 50% eIF4GI within 12 min whereas HIV-1(pro) required 4 h; the concentrations were 2 pg/microl (0.1 nM) for L(pro) and 60 pg/microl (2.66 nM) for HIV-1(pro). HIV-1(pro) processing of eIF4GI is therefore not quantitatively analogous to that of L(pro), suggesting that the primary function of eIF4GI cleavage in HIV-1 replication may not be protein synthesis inhibition.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Electrophoresis, Polyacrylamide Gel
  • Eukaryotic Initiation Factor-4G
  • HIV Protease / metabolism*
  • HIV-1 / physiology
  • Hydrolysis
  • Peptide Fragments / genetics
  • Peptide Fragments / metabolism*
  • Peptide Initiation Factors / genetics
  • Peptide Initiation Factors / metabolism*
  • RNA, Messenger / genetics
  • Substrate Specificity
  • Virus Replication

Substances

  • EIF4G1 protein, human
  • Eukaryotic Initiation Factor-4G
  • Peptide Fragments
  • Peptide Initiation Factors
  • RNA, Messenger
  • HIV Protease