[The infecting role of viral nucleic acids].
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DNA, Viral↗
Biomedical subjects
I Samuel
Publications and source records attributed to I Samuel.
[Action of formaldehyde on the infectious character of MM virus and on its ribonucleic acid].
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Encephalomyocarditis virus↗
Myocardial infarction and pulmonary embolism.
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Adult↗
Neutralizing influenza antibodies, IgA and total protein in the nasopharyngeal secretions of subjects vaccinated by nasal route with the inactivated influenza vaccine prepared in the "Stefan S. Nicolau" Institute of Virology.
Intranasal administration of two doses of the inactivated influenza vaccine prepared in the "Stefan S. Nicolau" Institute of Virology was followed by rises in the level of neutralizing secretory influenza antibodies in 82% of the cases. The concomitant study of secretory antibody, IgA and total protein levels, as well as of the serum HAI influenza antibodies demonstrated that their evolution was parallel only in 23% of the vaccinees. The percentage of secretory antibody conversion was similar to the rate of protection conferred by the vaccine.
Administration, Intranasal↗
Interaction between ceruloplasmin and Sendai virus envelope components. Note i. Gel-filtration of Tween 20-solubilized envelope components.
Sindai virus was disrupted by treatment with different concentrations of Tween 20 in an alkaline medium and the variations in infectivity, turbidity, hemagglutinin, neuraminidase and hemolytic activities were followed up. Gel-filtration of virus envelope fragments obtained by disruption with 1% Tween 20 demonstrated their heterogeneity as regards shape, size and biological activity. The elution type, the ratio between hemagglutinin and neuraminidase activities and the affinity for red blood cells of the envelope fragments depend on the detergent concentration used for virus disruption and on the presence or absence of detergent in the eluent.
Adsorption↗
Interaction between ceruloplasmin and Sendai virus envelope components. Note ii. Some characteristics of Tween 20-solubilized envelope components isolated by gel-filtration.
Biological activities of Tween 20-solubilized Sendai virus envelope differ according to the structure of the components obtained, which depends on: conditions of virus disruption, presence or absence of detergent during gel-filtration, duration of maintenance, type of fragments contained in the samples, and can be correlated neither with the size of fragments, nor with protein concentration.
Adsorption↗
Interaction between ceruloplasmin and Sendai virus envelope components. Note III. Separation of Sendai virus envelope components by affinity chromatography.
Sendai virus envelopes solubilized by Triton X-100 at an alkaline pH were submitted to affinity chromatography on fetuin-Sepharose 4B. In the absence of Triton three groups of envelope fragments were eluted, while in the presence of detergent only two groups were separated. In both cases, envelope fragment populations eluted at low temperature contained hemagglutinin (HA), neuraminidase (N-ase) and HI-antibody blocking (HIb) activity. The populations eluted at 37 degrees C contained N-ase and HIb activity, but no HA. The populations isolated show various ratios of HA, N-ase and HIb, and have different affinities for the coupled fetuin and formolated RBC. Our data strongly suggest that binding to coupled fetuin takes place via enzymatic centres, while binding to RBC occurs via hemagglutinating centres.
Ceruloplasmin↗
Immunoelectrophoretic characterization of Sendai virus antigens.
Antigens extracted from Sendai virus by solubilization with Triton X-100 (Tx). Tween-20 (Tw) or Triton X-100 and SDS (Tx-SDS) were analysed by rocket, crossed and tandem immunoelectrophoresis. The migration of these antigens through 1% agarose supplemented with guinea pig anti-viral envelope protein anti-serum shows that Tx and Tw antigens consist of three fractions differing in their quantitative ratios, while Tx-SDS exhibits five different fractions. The method proved to be useful for the identification of anti-host antibodies in immune antisera by means of an antigen extracted from the chorio-allantoic membrane of embryonated hen eggs.
Antigens, Viral↗
Immunoelectrophoretic investigations on Sendai virus envelope antigens in relation to host antigens.
The different antigenic fractions characteristic of egg-cultivated Sendai virus envelopes were studied by immunoelectrophoresis. Virus-specific and host-specific fractions were identified. It was proved that incorporation of the host membrane fragments into the viral envelopes is not a passive phenomenon. During the last stages of its assembly and release, the virus incorporates into the envelopes some host glycoproteins, after an active biochemical processing resulting in a considerable reduction of their molecular weight, while the host antigenic determinants remain almost unaltered.
Animals↗
Interaction between ceruloplasmin and Sendai virus envolpe components. Note IV. Effect of ceruloplasmin on the hemagglutinin and neuraminidase activities of Tween 20-solubilized envelope components separated by adsorption--elution on RBC.
Ceruloplasmin inhibits the hemagglutinin (HA) and neuraminidase (N-ase) activities of envelope fragment populations isolated from Sendai virus disrupted by alkali--Tween 20 treatment. The inhibition induced differs according to adsorption--elution characteristics, value and ratio of HA and N-ase activities and sterical configuration of the envelope fragments.
Ceruloplasmin↗
Interaction between cerulopasmin and Sendai virus envelope components. Note V. Serological response in the rabbit to Sendal virus and subviral fractions.
Immunization of rabbits with Sendai virus and subviral fractions induced the appearance in the serum of both hemagglutinin- and neuraminidase-inhibiting antibodies. The study of the correlation between antigen characteristics and the level and kinetics of the antibodies suggests that a single antigenic glycoprotein carries both hemagglutinin and neuraminidase activities. The level of serum antibodies depends both on the size and structure of the antigens and on their organization, and reflects the role of the protein and carbohydrate moieties of the different antigen preparations used.
Animals↗
Infectivity of Sendal virus and of its RNA for Nicotiana tabacum leaves.
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In Vitro Techniques↗
Immunoelectrophoretic study of Sendae virus envelope antigens with hyperimmune sera prepared in different laboratory animals.
At similar HAI titers rabbit sera reveal a larger number of fractions (ten) in immunoelectrophoretic analysis of Sendai virus envelopes than do guinea pig sera, which only yield three distinct fractions. These differences are observed in both rocket and crossed immunoelectrophoresis, and are more marked in the latter. The number of fractions revealed does not differ in relation to the antigen used for hyperimmunization (intact Sendai virus, Triton-disrupted virus or envelope fractions extracted by Triton or Tween-ether). Solubilized Sendai virus envelopes obtained by Tween-ether or Triton treatment contain host antigens in their structure, the same as intact virus.
Animals↗
Immunoelectrophoretic study of the host antigens of Sendai virus cultivated in different substrates (embryonated hen eggs and KB cells). Note I. Analysis of chorioallantoic membrane host antigens.
The immunoelectrophhoretic analysis of two preparations of the same virus cultivated in different substrates (Sendai/egg and Sendai/KB) demonstrate that virus envelopes contain: a) identical virus-specific antigens (but also some virus antigens with only partial immunochemical identity, or even non-identity); b) antigens incorporated by the virus from the host cell, during assembly and release. The latter differ according to the host, and some of them are only partially identical with the corresponding antigens of the host cell, which suggests that host cell glycoproteins are incorporated into the virus envelope after certain virus-induced modifications.
Animals↗
Effects and mechanism of the interaction between ceruloplasmin and some viruses or subviral components.
The results of investigations concerning the interaction between ceruloplasmin (a serum nonspecific inhibitor) and some myxo- and paramyxoviruses, as well as certain viruses with oncogenic potential (herpes virus, SV--40) are reviewed. The data presented point out the inhibiting action of ceruloplasmin on virus multiplication and the ceruloplasmin-induced modification in the antigenicity of Sendai virus and subviral fractions. The stages and mechanisms of ceruloplasmin action are discussed.
Animals↗
Immunoelectrophoretic study on the host antigens of Sendai virus cultivated in different substrates (embryonated hen eggs and KB cells). Note II. Analysis of KB cell host antigens.
It could be demonstrated by immunoelectrophoretic analysis that the host antigen incorporated in the envelopes of Sendai virus cultivated in KB cells (Sendai/KB) is characteristic of these cells and does not occur in the envelopes of the same virus grown in the embryonated hen egg (Sendai/egg). This host antigen appears from the first passage in KB cells and is constantly maintained over subsequent passages. The glycoproteins released by Triton X-100 disruption from Sendai/KB envelopes have a concomitant antigenic specificity for both virus and host. In the case of Sendai/egg virus, exclusively virus-specific macromolecules are also released.
Antigens↗
Investigations on the interaction between several fluorescent naphthalic acid derivatives and Sendai virus.
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Dicarboxylic Acids↗
Study of host antigens in the envelopes of different myxo- and paramyxoviruses cultivated in the embryonated hen egg.
By immunoelectrophoretic analysis it was shown that different viruses--such as myxo- (influenza A0PR8) and paramyxoviruses (Sendai, SV5, NDV, mumps)--cultivated in the same host cells (chorioallantoic membranes) incorporate similar host antigens into their envelopes. The amount of host cell antigens incorporated into the virus envelopes differs from one virus to another. The fact that incorporation of host cell antigens occurs only after a virus-induced modification seems to be a general characteristic of enveloped viruses such as myxo- and paramyxoviruses.
Animals↗