ABSTRACT
The interaction of "core" 2'-5'-oligoadenylates (2-5A) and their analogues with proteins albumin, interferon and immunoglobulin G was studied by fluorescence spectroscopy methods. Strong quenching of protein fluorescence (up to 67%) was observed upon interaction of oligoadenylates in concentration of 5 x 10(-5) M with albumin. Investigated compounds quenched the emission of interferon to a lesser extent, whereas no significant fluorescence changes occurred upon interaction with immunoglobulin under the same conditions. The level of quenching depended on the structure of 2-5A compounds and decreased with the decrease of their concentration. These data suggest that 2-5A actively bind to albumin and less efficiently to interferon, and practically do not interact with immunoglobulin. Taking into consideration different efficiency of quenching of the fluorescence excited at 280 and 296 nm, the assumption has been made about a possible role of tyrosine and tryptophan in the binding of a given compound to proteins. Possible mechanisms of interaction of oligoadenylates with proteins are discussed.
Subject(s)
Adenine Nucleotides/chemistry , Immunoglobulin G/chemistry , Interferon-alpha/chemistry , Oligoribonucleotides/chemistry , Serum Albumin/chemistry , Dose-Response Relationship, Drug , Humans , Oligopeptides , Protein Binding , Spectrometry, FluorescenceABSTRACT
The antiviral effect of 2',5'-trioligoadenylate (2',5'-A3) and some of its analogues was studied using several model cell culture systems and viruses: mice L929 fibroblast cells inoculated with vaccine virus, testicular piglet cells inoculated with Aueszki disease virus (strain BUK-628), and the same culture inoculated with a reference strain of transmissible gastroenteritis virus, strain Purdue-115. Our results suggest that both 2',5'-trioligoadenylate and its analogues are promising antiviral substances against DNA- and RNA-containing viruses.
Subject(s)
Adenine Nucleotides/pharmacology , Antiviral Agents/pharmacology , Herpesvirus 1, Suid/drug effects , Oligoribonucleotides/pharmacology , Transmissible gastroenteritis virus/drug effects , Vaccinia virus/drug effects , Animals , Cells, Cultured/virology , Fibroblasts/virology , Mice , Microbial Sensitivity Tests , Swine/virologyABSTRACT
The effect of trimeric 2',5'-oligoadenylic acid (2',5' A3) and its epoxy-derivative (2',5'-A2 (RAA) on human immunodeficiency virus (HIV-1) reproduction was studied. An HIV-1 infectivity titer decrease was shown on the model of limphoblastoid cells when the substances under study were used. The interferonogenic effect of both substances was discovered. 2',5'-A2 (RAA) inhibited the activity of retrovirus reverse transcriptase (a C-type).
Subject(s)
Adenine Nucleotides/pharmacology , Antiviral Agents/pharmacology , HIV-1/drug effects , Oligoribonucleotides/pharmacology , RNA-Directed DNA Polymerase/drug effects , Enzyme Repression , HIV-1/enzymology , HIV-1/physiology , Humans , Tumor Cells, Cultured , Virus Replication/drug effectsSubject(s)
Adenine Nucleotides/isolation & purification , DNA/isolation & purification , Deoxyribonucleases/isolation & purification , Oligoribonucleotides/isolation & purification , Salmon/metabolism , Semen/enzymology , Spermatozoa/enzymology , Adenine Nucleotides/analysis , Animals , Cattle , DNA/analysis , Deoxyribonucleases/analysis , Hydrogen-Ion Concentration , Male , Oligoribonucleotides/analysis , Protein Binding , Thymus Gland/enzymologySubject(s)
Bacteriophage lambda/analysis , DNA, Viral/analysis , Alkylation , Bacteriophage lambda/classification , Bacteriophage lambda/drug effects , DNA, Viral/classification , DNA, Viral/drug effects , Electrophoresis, Agar Gel , Hydrolysis , Molecular Weight , Restriction Mapping , Thiotepa/pharmacologyABSTRACT
The ability for nitrification was studied among mesophilic and thermophilic cultures of obligate methylotrophs Methylobacter ucrainicus, Methylomonas methanica, and Methylococcus thermophilus. The strains were almost incapable of nitrification under autotrophic conditions. In the presence of methane, however, they oxidized NH+4 TO NO-2: over 150 mg/litre NO-2 nitrogen was found in the cultural broth. Therefore, obligate methylotrophs are capable of heterotrophic nitrification. The level of nitrification suggests that it is not a side reaction but a necessary stage of the metabolism of obligate methylotrophs. The phenotype relation between obligate methylotrophs and nitrifying organisms is discussed.
