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  • 1
    Electronic Resource
    Electronic Resource
    Inhibition of adenovirus DNA polymerase by modified nucleoside triphosphate analogs correlate with their antiviral effects on cellular level (2000)
    Springer
    Medical microbiology and immunology 189 (2000), S. 91-95 
    Details
    ISSN: 1432-1831
    Keywords: Key words Human adenovirus ; Antiviral activity ; Modified nucleoside analogs ; Polymerase ; L-Enantiomers
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Adenovirus (Ad) infection results in significant morbidity and mortality in both immunocompetent and immunosuppressed hosts. There is currently no licensed chemotherapy effective in dealing with this virus infection. In this study the anti-adenoviral activity of a group of modified nucleoside analogs was investigated. The most efficient 3-fluorosubstituted nucleoside triphosphate inhibitors of Ad DNA polymerase were 3′-fluorothymidine triphosphate (IC50 0.63 μM), 2′,3′-dideoxy-3′-fluoroguanosine triphosphate (IC50 0.71 μM) and 2′,3′-dideoxy-3′-fluorouridine triphosphate (IC50 2.96 μM). The most efficient 2′,3′-dideoxynucleoside triphosphates were 2′,3′-dideoxycytidine triphosphate (ddCTP; IC50 1.0 μM), 2′,3′-dideoxyadenosine triphosphate (IC50 1.6 μM) and 2′,3′-dideoxythymidine triphosphate (IC50 1.82 μM). Kinetic studies indicate competitive inhibition of adenovirus DNA polymerase by ddCTP. These data confirm results previously obtained at the cellular level using a focus reduction assay involving Ad2-infected FL cells. Whereas the D-enantiomers 3′-fluorothymidine and 2′,3′-dideoxycytidine are potent inhibitors of adenoviral replication, the corresponding L-enantiomers exhibited no inhibitory activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004300000046
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  • 2
    Electronic Resource
    Electronic Resource
    Inhibition of Tryptase TL2 from Human T4+ Lymphocytes and Inhibition of HIV-1 Replication in H9 Cells by Recombinant Aprotinin and Bikunin Homologues (1997)
    Springer
    The protein journal 16 (1997), S. 651-660 
    Details
    ISSN: 1573-4943
    Keywords: Kunitz-type inhibitor ; aprotinin ; bikunin ; tryptase TL2 ; HIV infection
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The serine esterase TL2 from human T4+ lymphocytes is a binding component to HIV-1 glycoprotein gp120 and seems to play a role in the HIV-1 infection mechanism. Recombinant variants of the Kunitz-type serine proteinase inhibitor aprotinin were investigated for their ability to inhibit tryptase TL2 and the binding of gp120 to this enzyme. Furthermore, the viral replication of HIV-1 was investigated in H9 cell cultures under the influence of recombinant aprotinin and bikunin variants. In contrast to native aprotinin, the recombinant variant [Arg15, Phe17, Glu52]aprotinin with a reactive-site sequence homologous to the V3 loop of HIV-1 gp120 showed a specific inhibition of tryptase TL2 (〉80%). However, the [Leu15, Phe17, Glu52]aprotinin variant with hydrophobic subsites was the most potent inhibitor of the binding of gp120 to tryptase TL2 (68%). Our results show that the enzyme activity of purified tryptase TL2 is inhibited not only by variants with basic amino acids, but also those with hydrophobic residues in the reactive-site region. Therefore, tryptase TL2 is not a typical trypsin-like or chymotrypsin-like protease. Investigations on inhibition of HIV-1 replication in H9 cell cultures showed that tryptase TL2 is involved in the mechanism of virus internalization into human lymphocytes. The [Leu15, Phe17, Glu52]aprotinin showed a significant retardation of syncytium formation over a period of 5 days in a 1 μM concentration. Similar investigations were performed with recombinant variants of bikunin, the light chain of human inter-α-trypsin inhibitor. Only the single-headed variant [Arg94]82bikunin inhibited slightly the syncytium formation over a period of 2 days in a 2.2 μM concentration. Wild-type bikunin and all full-length variants showed no effect, possibly due to steric hindrance by the second domain of the double-headed inhibitor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1026379109403
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  • 3
    Electronic Resource
    Electronic Resource
    Inter-α-trypsin inhibitor polymorphism in African blacks (1992)
    Weinheim : Wiley-Blackwell
    Electrophoresis 13 (1992), S. 337-338 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The inter-α-trypsin inhibitor (ITI) polymorphism was analyzed in an African Negroid population using polyacrylamide gel isoelectic focusing and subsequent immunoblotting. Gene frequencies of ITI*1, ITI*2, ITI*3 and ITI*4 were calculated to be 0.564, 0.083, 0.337 and 0.004, respectively. One unknown rare allele, ITI*6 determines further phenotypes in combination with the alleles ITI*1 and ITI*3 Gene frequency of ITI*6 was calculated to be 0.012. The common alleles are represented by ITI*1 and ITI*3. The allele distribution is therefore different from European and Asian populations.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150130168
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