The catalytic properties of the reverse transcriptase of the lentivirus equine infectious anemia virus

Tami RUBINEK, Shoshana LOYA, Miriam SHAHARABANY, Stephen H. HUGHES, Patrick K. CLARK, Amnon HIZI

Research output: Contribution to journalArticlepeer-review

Abstract

The reverse transcriptase (RT) of equine infectious anemia virus (EIAV) shares sequence similarity with the RTs of other lentiviruses, particularly with the RTs of human immunodeficiency viruses types 1 and 2 (HIV‐1 and HIV‐2, respectively), the causative agents of acquired immunodeficiency syndrome (AIDS). There is a 41–42% sequence identity between EIAV RT and both HIV RTs (which have 61% sequence identity to each other). We have compared the enzymic properties of EIAV RT with those of HIV‐1 RT. Several aspects of the activities of EIAV RT differ from the corresponding activities of HIV‐1 RT. There are significant differences in the inhibition of the DNA polymerase activities by the deoxynucleoside triphosphate analogs, 3′‐azido‐2,3′‐dideoxythymidine triphosphate, dideoxyTTP and dideoxyGTP and by the nonnucleoside inhibitor, tetrahydroimidazo[4,5,1‐jk‐1,4]benzodiazepin‐2‐(1H)‐one and thione; in the dependence of DNA polymerase and RNase H activities on pH; in the inhibition of the DNA polymerase activities by the thiol‐specific reagent N‐ethylmaleimide; in the specific DNA polymerase activity; in the inhibition of the ribonuclease H activity by the zinc chelator orthophenanthroline. However, there are several cases in which EIAV RT and HIV‐1 RT are more similar than was previously found for HIV‐1 RT and HIV‐2 RT. These include the Km values for the DNA polymerase activities, the heat stability of the DNA polymerase functions and the specific activity of the RNase H function.

Original languageEnglish
Pages (from-to)977-983
Number of pages7
JournalEuropean Journal of Biochemistry
Volume219
Issue number3
DOIs
StatePublished - Feb 1994

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