Neutralization of poliovirus by a monoclonal antibody: Kinetics and stoichiometry

Icenogle, Joseph P.; Hong, Saw-See; Duke, Gregory; Gilbert, Scott A.; Rueckert, Roland R.; Anderegg, J. W.

doi:10.1016/0042-6822(83)90154-x

Cited by 119 publications

(121 citation statements)

References 31 publications

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“…single hit kinetics) but on average 70 IgG molecules have to bind before a relevant spike is hit. Interestingly a very similar mechanism of neutralization has been proposed for poliovirus where again the kinetics and stoichiometric data appear at odds [17]. There are four IgG molecules bound per poliovirus particle at 63% neutralization.…”

Section: Kinetic Analysissupporting

confidence: 53%

“…Secondly viruses have many attachment sites for cells (3000 in influenza virus, 60 in poliovirus) and since the majority of infectivity is neutralized when there are 70 (influenza virus; [8]) or 4 (poliovirus; [17]) molecules of IgG per particle, it seems unlikely that binding of low amounts of antibody would affect attachment.…”

Section: Discussionmentioning

confidence: 99%

“…There are four IgG molecules bound per poliovirus particle at 63% neutralization. An alternative stepwise model of neutralization was also suggested [17], where the binding of each IgG reduced the infectivity of each individual poliovirus particle by a factor of 3/4. Unfortunately the data were not sufficiently precise to distinguish between this and the critical site model.…”

Section: Kinetic Analysismentioning

confidence: 99%

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Insights into neutralization of animal viruses gained from study of influenza virus

Outlaw

Dimmock

1991

Epidemiol. Infect.

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SUMMARYIt has long been known that the binding of antibodies to viruses can result in a loss of infectivity, or neutralization, but little is understood of the mechanism or mechanisms of this process. This is probably because neutralization is a multifactorial phenomenon depending upon the nature of the virus itself, the particular antigenic site involved, the isotype of immunoglobulin and the ratio of virus to immunoglobulin (see below). Thus not only is it likely that neutralization of one virus will differ from another but that changing the circumstances of neutralization can change the mechanism itself. To give coherence to the topic we are concentrating this review on one virus, influenza type A which is itself well studied and reasonably well understood [1–3]. Reviews of the older literature can be found in references 4 to 7.

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Section: Kinetic Analysissupporting

confidence: 53%

Section: Discussionmentioning

confidence: 99%

Section: Kinetic Analysismentioning

confidence: 99%

See 1 more Smart Citation

Insights into neutralization of animal viruses gained from study of influenza virus

Outlaw

Dimmock

1991

Epidemiol. Infect.

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“…In this case, there would be no need for saturating the virus with Fab or Mab to cause neutralization. That may be the case in poliovirus where only a few Mabs of a certain type are needed for neutralization [27].…”

Section: Mechanisms Of Neutralizationmentioning

confidence: 99%

The structure of a neutralized virus: canine parvovirus complexed with neutralizing antibody fragment

et al. 1994

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Background-Members of the Parvovirus genus cause a variety of diseases in mammals, including humans. One of the major defences against viral infection is the presence of neutralizing antibodies that prevent virus particles from infecting target cells. The mechanism of neutralization is not well understood. We therefore studied the structure of canine parvovirus (CPV) complexed with the Fab fragment of a neutralizing antibody, A3B10, using image reconstruction of electron micrographs of vitrified samples, together with the already known structure of CPV from X-ray crystallographic data.

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“…But for some antibodies, bivalent binding of the IgG was determined to be important to its ability to neutralize the virion 11 . The centres of pairs of 5B2 Fab fragments, related by an adjacent icosahedral 2-fold symmetry axis, are 60 Å apart.…”

mentioning

confidence: 99%

Identification of a Fab interaction footprint site on an icosahedral virus by cryoelectron microscopy and X-ray crystallography

Wang

Porta

Chen

et al. 1992

Nature

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Biological processes frequently require the formation of multi-protein or nucleoprotein complexes. Some of these complexes have been produced in homogeneous form, crystallized, and analysed at high resolution by X-ray crystallography (for example, see refs 1-3). Most, however, are too large or too unstable to crystallize. Individual components of such complexes can often be purified and analysed by crystallography. Here we report how the coordinated application of cryoelectron microscopy, three-dimensional image reconstruction, and X-ray crystallography provides a powerful approach to study large, unstable macromolecular complexes. Three-dimensional reconstructions of native cowpea mosaic virus (CMPV) and a complex of CPMV saturated with a Fab fragment of a monoclonal antibody against the virus have been determined at 23 Å resolution from low-irradiation images of unstained, frozen-hydrated samples. Despite the nominal resolution of the complex, the physical footprint of the Fab on the capsid surface and the orientation and position of the Fab have been determined to within a few angstroms by fitting atomic models of CPMV 4 and Fab (Kol) 5 to reconstructed density maps.Comoviruses are plant viruses whose structural and biological properties are strikingly similar to the animal picornaviruses 6,7 . For example, the protein capsids of CPMV, the type member of the comovirus group, and poliovirus, the most extensively studied picornavirus, are comparable (Fig. 1a). The CPMV coat contains 60 copies each of large (relative molecular mass 42,000 (M r 42K) and small (24K) protein subunits arranged with icosahedral symmetry. Each large subunit (L) is composed of two antiparallel β-barrel domains which are positioned close to the icosahedral 3-fold axes. The β-barrel domain at the amino-terminal end of L corresponds to the VP2 subunit in poliovirus and the β-barrel at the carboxy-terminal end of L corresponds to VP3 in poliovirus. The small subunits (S), packed near the icosahedral 5-fold axes, correspond to VP1 in poliovirus.CPMV is strongly immunogenic when injected into rabbits or mice. We prepared nine monoclonal antibodies against CPMV using standard methods 8 . The binding properties of these antibodies were analysed by enzyme-linked immunosorbent assay (ELISA) and all nine would only bind to virus particles presented in a double antibody sandwich-type ELISA © 1992 Nature Publishing Group Correspondence to: John E. Johnson. G.W. and C.P. are joint first authors. in which the virus is bound to a polyclonal antibody attached to the plastic plate. Denaturation of the virus by its direct adsorption onto a plastic surface destroys the antigenic sites for all nine monoclonal antibodies. Only monoclonal antibodies 5B2 and 10B7 reacted strongly with CPMV that was free in solution (antibody binding was assayed by electron microscopy analysis of negatively stained complexes marked with gold-labelled anti-mouse immunoglobulin). Fab fragments from monoclonal antibody 5B2 were prepared by digestion of IgGs with insoluble...

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Neutralization of poliovirus by a monoclonal antibody: Kinetics and stoichiometry

Cited by 119 publications

References 31 publications

Insights into neutralization of animal viruses gained from study of influenza virus

Insights into neutralization of animal viruses gained from study of influenza virus

The structure of a neutralized virus: canine parvovirus complexed with neutralizing antibody fragment

Identification of a Fab interaction footprint site on an icosahedral virus by cryoelectron microscopy and X-ray crystallography

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