The Immunological Reactions of the Filterable Viruses

Burnet, F. M.; Keogh, E. V.; Lush, Dora

doi:10.1038/icb.1937.23

Cited by 111 publications

(70 citation statements)

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“…The literature contains many references suggesting that polysaccharides, or materials containing polysaccharides, produced by individual bacterial species specifically interfere with the activity of bacteriophages that attack those species (Levine & Frisch, 1933; Burnet, 1934; Gough & Burnet, 1934; White, 1936; Miller & Goebel, 1949). Some authors have also related polysaccharides capable of interfering specifically with bacteriophages to those that confer serological specificity to their host bacteria (see Burnet, Keogh & Lush, 1937). On the other hand, Ashenburg, Sandholzer, Scherp & Berry (1940) found no evidence for specific inhibition of activity of bacteriophage by a polysaccharide produced by its host bacteria, for polysaccharides of widely different origins inhibited similarly.…”

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confidence: 99%

Effect of Specific Polysaccharides from the Host Bacteria and of Ribonuclease on the Multiplication of Rhizobium Phages

Kleczkowski

1952

Journal of General Microbiology

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SUMMARY : Two serologically unrelated strains of nodule bacteria produced two different polysaccharides, only one of which precipitated with antiserum to its parent bacterium. Both polysaccharides interfered with the multiplication of two bacteriophages in liquid cultures of the two bacterial strains, each of which was susceptible to only one of the two bacteriophages. One polysaccharide was slightly more effective than the other in interfering with multiplication of both bacteriophages; one phage was much more susceptible than the other to the interfering action of both polysaccharides. Crystallized pancreatic ribonuclease interfered with multiplication of bacteriophages much more strongly than did the polysaccharides. Xeither the polysaccharides nor ribonuclease destroyed the phage particles.

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confidence: 99%

Effect of Specific Polysaccharides from the Host Bacteria and of Ribonuclease on the Multiplication of Rhizobium Phages

Kleczkowski

1952

Journal of General Microbiology

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“…Also, the above-cited lag in neutralization reaction observed at a low temperature (10) may mean that one of the multi-step changes caused by N antibody is temperaturedependent. The similar lag found with low concentrations of antibody (2,9) or with IgM antibody (16) cannot be explained at this moment. In our experience, we have never been encountered by such a lag with whatever low dilutions of antibody nor with IgM antibody.…”

Section: Discussionmentioning

confidence: 75%

“…This concept was obviously derived from the observation that the neutralization of a T bacteriophage was effectuated through blocking of its tail tip by antibody (11). This explanation is, however, contradictory in case the virus has multiple critical sites per virion, since the above-stated neutralization kinetic curve experiments all testified the one-hit nature of the reaction, although some investigators observed a lag in the neutralization curve when the reaction proceeded at a low temperature (10), with a low concentration of antibody (2,9) or with IgM antibody (16).…”

Section: Discussionmentioning

confidence: 94%

Studies on the Neutralization of Herpes Simplex Virus

Yoshino

Hashimoto

Shinkai

1977

Microbiology and Immunology

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Early and late IgG of rabbits immunized with herpes virus showed, respectively, 8-fold and 2-fold enhancement of neutralization endpoint in the presence of complement (C). Kinetic curve experiments employing an appropriate amount of virus revealed that both neutralization and sensitization followed firstorder reaction, and each IgG possessed a certain range of concentration where neutralization was negligible while sensitization was marked. Dose responses of neutralization and sensitization velocities demonstrated that the C enhancement of late IgG was about 7-fold and that of early IgG more than 20-fold. These facts suggested that the IgGs contained two different entities of complement-requiring (CRN) and non-requiring neutralizing (N) antibodies at different proportions, only the former being responsible for sensitization. The different CRN: N ratios obtained by the endpoint and kinetic methods may mean either that the two antibodies differ in avidity for the virus or that the number of critical sites per virion for CRN antibody is greater than that for N antibody. In this interpretation, sensitization by CRN antibody as well as neutralization by N antibody is thought to result from attachment of a single antibody molecule to the viral critical site. Alternative explanations, ascribing the mechanism of neutralization to steric hindrance of critical sites or to multiple hit of those sites by antibody, were denied by analyses of the present data.Enhancement of viral neutralization by complement (C) has attracted interest of many investigators, but the mechanism of viral sensitization by antibody for subsequent inactivation by C still remains in the realm of speculation. Explanations ascribing the C action to coverage of a wide area of viral surface (5,12, 17), to aggregation of virus-antibody complexes (23) or to virolysis (1, 17, 24) cannot account for the reason why the C enhancement differs between early and late antibodies of rabbits immunized with herpes simplex virus (HSV) (26). One could presume that IgM antibody might represent complement-requiring neutralizing (CRN) antibody.

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“…This law, however, has to be qualified: the concentration of antibody has to be in considerable excess compared with the concentration of virus. In addition, this law is actually the expected effect of the excess of antibody compared with antigen, which makes the fraction of the complexed antibody negligible (43). Using poliovirus as an example, Brioen and Boxyé (44) studied the validity range of the percentage law and found that it is valid when the virus concentration is approximately Ͻ1 ϫ 10 8 PFU/ml.…”

Section: Discussionmentioning

confidence: 99%

Development of an Enzyme-Linked Immunosorbent Spot Assay To Measure Serum-Neutralizing Antibodies against Coxsackievirus B3

Yang

Tang

et al. 2014

Clin. Vaccine Immunol.

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Coxsackievirus B3 (CVB3) is the most common pathogen that induces acute and chronic viral myocarditis in children. The cytopathic effect (CPE)-based neutralization test (Nt-CPE) and the plaque reduction neutralization test (PRNT) are the most common methods for measuring neutralizing antibody titers against CVB3 in blood serum samples. However, these two methods are inefficient for CVB3 vaccine clinical trials, which require the testing of a large number of serum specimens. In this study, we developed an efficient neutralization test based on the enzyme-linked immunospot (Nt-ELISPOT) assay for measuring CVB3-neutralizing antibodies. This modified ELISPOT assay was based on the use of a monoclonal antibody against the viral capsid protein VP1 to detect the cells that are infected with CVB3, which, after immunoperoxidase staining, are counted as spots using an automated ELISPOT analyzer. Using the modified ELISPOT assay, we characterized the infection kinetics of CVB3 and divided the infection process of CVB3 on a cluster of cells into four phases. The stability of the Nt-ELISPOT was then evaluated. We found that over a wide range of infectious doses (10 2 to 10 6.5 ؋ 50% tissue culture infectious dose [TCID 50 ] per well), the neutralizing titers of the sera were steady as long as they were tested during the log phase or the first half of the stationary phase of growth of the spots. We successfully shortened the testing period from 7 days to approximately 20 h. We also found that there was a good correlation (R 2 ‫؍‬ 0.9462) between the Nt-ELISPOT and the Nt-CPE assays. Overall, the Nt-ELISPOT assay is a reliable and efficient method for measuring neutralizing antibodies in serum.

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The Immunological Reactions of the Filterable Viruses

Cited by 111 publications

References 0 publications

Effect of Specific Polysaccharides from the Host Bacteria and of Ribonuclease on the Multiplication of Rhizobium Phages

Effect of Specific Polysaccharides from the Host Bacteria and of Ribonuclease on the Multiplication of Rhizobium Phages

Studies on the Neutralization of Herpes Simplex Virus

Development of an Enzyme-Linked Immunosorbent Spot Assay To Measure Serum-Neutralizing Antibodies against Coxsackievirus B3

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