scholarly journals Characterization of the Polymerase and RNase H Activities of Human Foamy Virus Reverse Transcriptase

2004 ◽  
Vol 78 (12) ◽  
pp. 6112-6121 ◽  
Author(s):  
Paul L. Boyer ◽  
Carolyn R. Stenbak ◽  
Patrick K. Clark ◽  
Maxine L. Linial ◽  
Stephen H. Hughes

ABSTRACT Foamy virus (FV) replication, while related to that of orthoretroviruses, differs at a number of steps. Several of these differences involve the reverse transcriptase (RT). There appear to be fewer RTs present in FV than in orthoretroviruses; we previously proposed that the polymerase of FV RT was more active than orthoretroviral RTs to compensate for the numerical difference. Here we present further characterization of the RT of FV. The polymerase activity of FV RT was greater than that of human immunodeficiency virus type 1 RT in a variety of assays. We also examined the RNase H activity of FV RT, and we propose that FV RT has a basic loop in the RNase H domain. Although the sequence of the basic loop of FV RT is different from the basic loop of either Moloney leukemia virus RNase H or Escherichia coli RNase H, the FV RT basic loop appears to have a similar function.

1983 ◽  
Vol 47 (1) ◽  
pp. 249-252 ◽  
Author(s):  
A B Benzair ◽  
A Rhodes-Feuillette ◽  
R Emanoil-Ravicovitch ◽  
J Peries

1996 ◽  
Vol 7 (1) ◽  
pp. 37-45 ◽  
Author(s):  
S. J. W. Allen ◽  
S. H. Krawczyk ◽  
L. R. McGee ◽  
N. Bischofberger ◽  
A. S. Mulato ◽  
...  

Nucleotide dimers and monomers were shown to inhibit human immunodeficiency virus type 1 (HIV) RNase H activity. Several effective inhibitors were identified and placed into three general groups based on biochemical characterization of their inhibition, The first group (group A) inhibited HIV RNase H and the closely related feline immunodeficiency virus (FIV) RNase H, but did not inhibit less related retroviral or cellular RNases H or HIV reverse transcriptase (RT). The second group (group B) inhibited the RNase H activity of several retroviruses as well as the reverse transcriptase function of HIV RT. The third group (group C) inhibited RNases H from retroviral and cellular sources but did not inhibit HIV RT. Kinetic analyses of HIV RNase H inhibition were conducted and all three types of inhibitors exhibited a competitive mode of inhibition with regard to substrate. The small nucleotides described here represent the most potent (Ki values from 0.57 to 16 μM) and selective inhibitors of HIV RNase H reported to date. Further structure - function analyses of these molecules may lead to the discovery of unique, potent antiretroviral therapeutics.


2015 ◽  
Vol 113 ◽  
pp. 44-50 ◽  
Author(s):  
Kosaku Nishimura ◽  
Kanta Yokokawa ◽  
Tetsuro Hisayoshi ◽  
Kosuke Fukatsu ◽  
Ikumi Kuze ◽  
...  

2004 ◽  
Vol 48 (8) ◽  
pp. 3122-3126 ◽  
Author(s):  
Soo-Yon Rhee ◽  
Tommy Liu ◽  
Jaideep Ravela ◽  
Matthew J. Gonzales ◽  
Robert W. Shafer

ABSTRACT In a sample of 6,156 sequences from 4,183 persons, the top 30 patterns of protease inhibitor, nucleoside reverse transcriptase (RT) inhibitor, and nonnucleoside RT inhibitor mutations accounted for 55, 46, and 66%, respectively, of sequences with drug resistance mutations. Characterization of the phenotypic and clinical significance of these common patterns may lead to improved treatment recommendations for a large proportion of patients for whom antiretroviral therapy is failing.


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