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1.
Vopr Virusol ; 32(4): 403-9, 1987.
Artigo em Russo | MEDLINE | ID: mdl-3686980

RESUMO

The antigenic structure of hemagglutinin of influenza A virus (H3N2) strains isolated in 1985 was studied using a series of monoclonal antibody to A/Dunedin/4/73/A (H3N2) and A/Bangkok/1/79/A (H3N2), and biological and physico-chemical properties of these strains were compared with those of influenza A (H3N2) virus of 1983 and reference A (H3N2) of 1979-1984 (the rate of adsorption on chick erythrocytes and eluting activity, thermostability of hemagglutinin and neuraminidase, sensitivity to nonionic detergents, sensitivity to remantadine, analysis of virion polypeptide composition). A high degree of heterogeneity of the 1985 strain population of influenza A (H3N2) virus was revealed both in the antigenic structure of hemagglutinin and in all the biological and physico-chemical parameters tested. It was suggested that the A/Caen/1/84 strain originated not from A/Philippines/2/82 but directly from A/Texas/1/77.


Assuntos
Antígenos Virais/análise , Vírus da Influenza A/imunologia , Adsorção , Anticorpos Monoclonais/análise , Fenômenos Químicos , Físico-Química , Eletroforese em Gel de Poliacrilamida , Testes de Inibição da Hemaglutinação , Hemaglutininas Virais/análise , Humanos , Vírus da Influenza A/análise , Vírus da Influenza A/efeitos dos fármacos , Vírus da Influenza A/isolamento & purificação , Rimantadina/farmacologia , Proteínas Virais/análise
2.
Vopr Virusol ; 32(3): 283-5, 1987.
Artigo em Russo | MEDLINE | ID: mdl-2445104

RESUMO

The antigenic properties of neuraminidase of the epidemic strains of 1983-1985 were studied by means of lectin test and thiobarbituric method using polyclonal sera and monoclonal antibody. Populations of the viruses with respect to antigenic relationships of neuraminidase were shown to be heterogeneous. A considerable portion of the strains occurring in 1985 underwent antigenic drift from the reference A/Philippines/2/82 strain. The epidemic novelty of some strains was due to changes in only one supercapsid protein-neuraminidase.


Assuntos
Antígenos Virais/análise , Epitopos/análise , Vírus da Influenza A Subtipo H3N2 , Vírus da Influenza A/imunologia , Neuraminidase/imunologia , Anticorpos Monoclonais/análise , Variação Antigênica , Surtos de Doenças , Humanos , Técnicas Imunológicas , Vírus da Influenza A/enzimologia , Vírus da Influenza A/isolamento & purificação , Influenza Humana/microbiologia , U.R.S.S.
3.
Vopr Virusol ; 32(3): 285-9, 1987.
Artigo em Russo | MEDLINE | ID: mdl-2445105

RESUMO

The antigenic structure of neuraminidases of influenza B viruses isolated in 1940-1984 was studied. Lectin test has first been employed for analysis of influenza B virus neuraminidase. The antigenic composition of neuraminidases of these viruses was shown to be different. The strains isolated in the epidemic of 1983-1984 underwent further drift of the neuraminidase component and represent a heterogeneous group in this respect. The use of monospecific antiserum to purified neuraminidase helped specify antigenic relationships of this protein.


Assuntos
Antígenos Virais/análise , Epitopos/análise , Vírus da Influenza B/imunologia , Neuraminidase/imunologia , Surtos de Doenças , Humanos , Técnicas Imunológicas , Vírus da Influenza B/enzimologia , Vírus da Influenza B/isolamento & purificação , Influenza Humana/microbiologia , U.R.S.S.
4.
Vopr Virusol ; 32(1): 39-44, 1987.
Artigo em Russo | MEDLINE | ID: mdl-3554755

RESUMO

IgG to internal (NP, M) and external (HA, NA) proteins of influenza virus were isolated from immune rabbit sera using caprylic acid. The IgG retained their specificity and activity, worked in HI, lectin test, and enzyme-immunoassay. IgG migrated towards cathode in electrophoresis on acetate cellulose. Electrophoresis in polyacrylamide gel revealed a heavy chain (55,000) and a light chain (25,000) in IgG molecule. Different methods revealed changes in IgG structure after lyophilization. The possibility of recovering IgG from rat sera using caprylic acid was demonstrated. A comparative analysis of IgG recovered by means of caprylic acid as well as by polyethylene glycol or ammonium sulphate showed the IgG recovered with caprylic acid to contain less admixtures and to be suitable for use in immunological tests without additional purification.


Assuntos
Soros Imunes/análise , Imunoglobulina G/isolamento & purificação , Vírus da Influenza A/imunologia , Vírus da Influenza B/imunologia , Proteínas Virais/imunologia , Animais , Anticorpos Antivirais/análise , Caprilatos , Imunização , Imunoglobulina G/análise , Técnicas Imunológicas , Coelhos , Ratos
5.
Vopr Virusol ; 31(6): 666-74, 1986.
Artigo em Russo | MEDLINE | ID: mdl-3825089

RESUMO

Consequences of chemical breakage of native disulphide bonds in influenza virus neuraminidase and hemagglutinin glycoproteins induced by mercaptoethanol treatment were studied. Under conditions of blocked reoxidation of thiol groups, this treatment led to significant inhibition of hemagglutinating activity and infectivity of virus particles, and to a lesser inhibition of neuraminidase activity, as well as to promotion of endogenous proteolytic activity. Analysis of virus particles proteins by polyacrylamide gel electrophoresis indicated association of these biological effects with breakage of disulphide bridges, mainly in hemagglutinin glycoproteins. Under certain conditions, the proteins were capable of reformation of disulphide bridges as manifested in restoration of virion biological activity and electrophoretic characteristics of proteins.


Assuntos
Dissulfetos/metabolismo , Vírus da Influenza A/metabolismo , Proteínas Virais/metabolismo , Sítios de Ligação/efeitos dos fármacos , Dissulfetos/análise , Eletroforese em Gel de Poliacrilamida , Glicoproteínas/análise , Glicoproteínas/metabolismo , Hemaglutininas Virais/análise , Vírus da Influenza A/análise , Vírus da Influenza A/efeitos dos fármacos , Mercaptoetanol/farmacologia , Neuraminidase/análise , Neuraminidase/metabolismo , Relação Estrutura-Atividade , Proteínas Virais/análise
6.
Artigo em Russo | MEDLINE | ID: mdl-3538729

RESUMO

Comparative study of the sensitivities of immunofluorescent microscopy (IFM), enzyme immunoassay, (EIA), and lectin test (LT) in the detection of influenza virus antigen in nasopharyngeal washings from patients with influenza, acute respiratory diseases, pneumonia, and laryngitis has been carried out. EIA modification (used in this study) based on the detection of a complex of viral core proteins (M + RNP) has been shown to be no less sensitive than IFM and suitable for use in the rapid diagnosis of influenza. It can be used in combination with other methods. The optimum time for collecting the washings off is day 2 from the disease onset for analysis by EIA technique and day 4 for LT.


Assuntos
Imunofluorescência , Técnicas Imunoenzimáticas , Influenza Humana/diagnóstico , Lectinas , Adolescente , Animais , Antígenos Virais/análise , Criança , Diagnóstico Diferencial , Eritrócitos/imunologia , Estudos de Avaliação como Assunto , Cobaias , Humanos , Vírus da Influenza A/imunologia , Vírus da Influenza B/imunologia
8.
Vopr Virusol ; 30(6): 668-71, 1985.
Artigo em Russo | MEDLINE | ID: mdl-4095974

RESUMO

Four strains of influenza C virus were studied by cellulose acetate electrophoresis. All of them were found to contain super-capsid proteins destroyed by electrophoresis apparently due to contact with sodium dodecylsulphate. According to Laver's classification, influenza C viruses may be placed with Group 3 viruses. Among major virion proteins of influenza C viruses matrix protein was found to be the most stable forming a separate protein band on cellulose acetate, and it may be readily identified and eluted from paper in preparative amounts.


Assuntos
Gammainfluenzavirus/análise , Orthomyxoviridae/análise , Proteínas Virais/análise , Eletroforese em Acetato de Celulose/métodos , Eletroforese em Gel de Poliacrilamida , Vírus da Influenza A/análise , Vírus da Influenza A/efeitos dos fármacos , Vírus da Influenza A/isolamento & purificação , Vírus da Influenza B/análise , Vírus da Influenza B/efeitos dos fármacos , Vírus da Influenza B/isolamento & purificação , Gammainfluenzavirus/efeitos dos fármacos , Gammainfluenzavirus/isolamento & purificação , Peptídeos/análise , Peptídeos/isolamento & purificação , Dodecilsulfato de Sódio/farmacologia , Proteínas Virais/isolamento & purificação
9.
Vopr Virusol ; 30(4): 394-7, 1985.
Artigo em Russo | MEDLINE | ID: mdl-4060697

RESUMO

Internal proteins of influenza B/USSR/14/80 virus retaining their antigenic and immunogenic activities were obtained by electrophoresis in 1% agarose. Antisera to eluted NP and M polypeptides were prepared. Study of influenza B viruses isolated in 1940-1984, performed by solid-phase radioimmunoassay, revealed no differences in the antigenic properties of nucleoprotein and matrix protein, except in the B/Yamagata/73 virus.


Assuntos
Vírus da Influenza B/análise , Nucleoproteínas/análise , Proteínas Virais/análise , Eletroforese em Gel de Ágar , Vírus da Influenza A/análise , Nucleoproteínas/isolamento & purificação , Radioimunoensaio/métodos , Proteínas da Matriz Viral , Proteínas Virais/isolamento & purificação , Vírion/análise
10.
Zh Mikrobiol Epidemiol Immunobiol ; (1): 85-90, 1985 Jan.
Artigo em Russo | MEDLINE | ID: mdl-3920848

RESUMO

Test systems for ELISA, containing antibodies to internal or supercapsid proteins and intended for the detection and differentiation of influenza A, B and C viruses in small amounts, have been developed. The possibility of using these systems for the determination of viruses both in material obtained directly from humans and in chick embryo isolates has been demonstrated.


Assuntos
Vírus da Influenza A/isolamento & purificação , Vírus da Influenza B/isolamento & purificação , Animais , Anticorpos Antivirais/análise , Especificidade de Anticorpos , Antígenos Virais/análise , Capsídeo/imunologia , Capsídeo/isolamento & purificação , Embrião de Galinha , Criança , Ensaio de Imunoadsorção Enzimática , Humanos , Imunização/métodos , Imunodifusão , Vírus da Influenza A/imunologia , Vírus da Influenza B/imunologia , Vacinas contra Influenza/imunologia , Camundongos
12.
Vopr Virusol ; 28(6): 663-8, 1983.
Artigo em Russo | MEDLINE | ID: mdl-6199899

RESUMO

A highly purified lectin was obtained from peanuts. The lectin test was modified for determination of the neuraminidase activity of influenza viruses. The test was found to be useful for the determination of the antigenic specificity of neuraminidase. It was found to be 10-50 times as sensitive as the Aminoff test and more economic. The potentials of lectin test are discussed.


Assuntos
Vírus da Influenza A/enzimologia , Lectinas/análise , Neuraminidase/análise , Animais , Anticorpos Antivirais/análise , Antígenos Virais/análise , Epitopos/análise , Eritrócitos/imunologia , Cobaias , Imunização , Técnicas Imunológicas , Vírus da Influenza A/imunologia , Neuraminidase/imunologia , Coelhos , Ratos , Especificidade da Espécie
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