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1.
Zh Mikrobiol Epidemiol Immunobiol ; (8): 112-5, 1988 Aug.
Article in Russian | MEDLINE | ID: mdl-3143203

ABSTRACT

In this work new data are presented on the comparative quantitative amino acid analysis of allergens, isolated and purified from different bacteria. On the basis of a high content of basic amino acids, such as lysine, arginine and histidine, in Mycobacterium, Brucella and Francisella tularensis allergens, a suggestion is made to classify bacterial allergens with histone-like proteins.


Subject(s)
Allergens/analysis , Bacterial Proteins/analysis , Histones/analysis , Hypersensitivity, Delayed/diagnosis , Allergens/isolation & purification , Amino Acids/analysis , Bacterial Proteins/isolation & purification , Brucella abortus/immunology , Francisella tularensis/immunology , Histones/isolation & purification , Humans , Hypersensitivity, Delayed/immunology , Mycobacterium bovis/immunology , Skin Tests
4.
Ukr Biokhim Zh (1978) ; 50(6): 688-90, 1978.
Article in Russian | MEDLINE | ID: mdl-749293

ABSTRACT

The possibility of the proteolotic enzymes incorporation into the viral particle and the changes in proteolysis during interaction of the purified influenza virus (A2 Hong-Kong (1)68) with isolated plasmatic membranes of the mice lungs were studied. The presence of trypsin-like protease in the purified influenza virion was found. It is established that proteolysis intensifies during a short-term interaction of the isolated plasmatic membranes with the influenza virus.


Subject(s)
Cell Membrane/metabolism , Influenza A virus/metabolism , Peptide Hydrolases/metabolism , Animals , Cells, Cultured , Mice , Virion/enzymology
5.
Mol Biol (Mosk) ; 11(3): 516-20, 1977.
Article in Russian | MEDLINE | ID: mdl-752790

ABSTRACT

A mechanism responsible for proteolytic deproteinization of influenza virus A2 Hong-Kong (I)68 by plasmatic membranes of sensitive cells was studied. Presence of trypsinlike protease in plasmatic membranes of white mice lungs was demonstrated. A considerable inhibition of the membrane proteolitic activity was obtained in the presence of epsilon-aminocaproic acid. Disintegration of the virus labeled by [3H]uridine by plasmatic membranes was investigated and it was found that this process required ATP. Inhibition of the protease activity by epsilon-aminocaproic acid led to the suppression of deproteinization of influenza virus. The experimental data obtained indicate that the proteolytic enzymes of plasmatic membranes participate in the complex process of virus "uncoating".


Subject(s)
Cell Membrane/enzymology , Endopeptidases/metabolism , Lung/enzymology , Orthomyxoviridae Infections , Trypsin , Aminocaproic Acid/pharmacology , Animals , Cell Membrane/drug effects , Mice
6.
Vopr Virusol ; (1): 36-40, 1977.
Article in Russian | MEDLINE | ID: mdl-910440

ABSTRACT

The evidence has been obtained indicating an increase in proteolysis in the lungs of mice within 1 1/2 - 2 1/2 hours and on the 2nd day after inoculation of the animals with 1X10(5)-1X10(6) LD50 of influenza AO/32 virus, whereas on the 5th day in the affected organ proteolysis was significantly reduced as compared to the controls. No significant differences in the levels of cateptic activity at pH 5.0 in the lungs of infected and noninfected animals were found at any intervals of the study. At 1 1/2--2 1/2 hours and 5 days postinfection the antitryptic activity of the serum was found to be increased. The increased proteolysis early in infection is considered to be a virus-induced process, while its decline on the 5th day postinfection may be of protective nature. The participation of the system of proteases and their inhibitors in influenza virus--sensitive cells interaction as well as in the pathogenesis of influenza pneumonia is suggested.


Subject(s)
Orthomyxoviridae Infections/enzymology , Peptide Hydrolases/metabolism , Protease Inhibitors , Animals , Caseins/metabolism , Cathepsins/metabolism , Enzyme Activation , Influenza A virus , Lung/enzymology , Mice , Time Factors , Trypsin Inhibitors/metabolism
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