A monoclonal antibody that neutralizes poliovirus by cross-linking virions

Thomas, Adrianus; Brioen, Paul; Boeyé, Albert

doi:10.1128/jvi.54.1.7-13.1985

Cited by 42 publications

(28 citation statements)

References 21 publications

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“…The two major consequences of neutralization which have been reported for other picornaviruses include an acidic shift in the pl of virions and the formation of viral aggregates (3,12,16,20,27,28). Analysis of neutralized HRV-14 particles also demonstrated the involvement of these effects in the neutralization of rhinoviruses.…”

Section: Discussionmentioning

confidence: 80%

“…Keller (17,18) also reported that monovalent Fab fragments obtained by papain digestion were effective in neutralizing poliovirus to a lesser extent than intact, bivalent antibodies, while Mandel (20) reported complete neutralization with Fab fragments obtained from polyclonal antiserum. In contrast, Thomas et al (27) could not prepare Fab fragments that were capable of binding to poliovirus.…”

Section: Discussionmentioning

confidence: 96%

“…A major difficulty with a number of the early studies has been the use of hyperimmune antiserum that contains a mixture of antibodies, not all of which neutralize, and which are directed against different epitopes on intact virions. More recently, aggregation or polymerization of virions has been proposed (3,27,28) as the major mechanism of neutralization. Supportive of this mechanism is the finding that papain treatment of poliovirus-antibody complexes disrupts the aggregates and restores virus infectivity (13,16,28).…”

mentioning

confidence: 99%

“…The observed pl shift was not merely due to the presence of the IgG antibody, since radiolabeled NImII-35 antibody chromatographed in the absence of virus focused with a pI of 6.6 (data not shown).Aggregation of virus particles. Previous neutralization studies(3,16,26,27) on poliovirus have demonstrated that virions aggregate as a result of antibody neutralization. To determine whether any of the HRV-14 neutralizing antibodies caused a similar aggregation of HRV virions under ND95 J. VIROL.…”

mentioning

confidence: 99%

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Inhibition of rhinovirus attachment by neutralizing monoclonal antibodies and their Fab fragments

Colonno

Callahan

Leippe

et al. 1989

J Virol

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Previous molecular and immunological studies have mapped four neutralization sites on human rhinovirus type 14 (B. Sherry, A. G. Mosser, R. J. Colonno, and R. R. Rueckert, J. Virol. 57:246-257, 1986). Eight monoclonal antibodies, one pair for each of the four target sites and all belonging to a single isotype, immunoglobulin G2a, were studied under conditions which resulted in 95% neutralization of infectious viral particles. All eight antibodies shifted the isoelectric point of virions from 6.7 to much more acidic forms, ranging from pl 1.8 to 3.2. In addition, antibodies targeted against three of the four neutralization sites caused significant aggregation of virions under the neutralization conditions employed. Aggregation could be reversed by digesting virus-antibody complexes with papain. Following papain digestion, the acidic pls of three of the neutralized virus preparations returned to neutral and infectivity was restored. Membrane-binding assays with virus neutralized with a nonaggregating antibody showed a dose-related inhibition of virus attachment to cellular receptors. Purified Fab fragments at a 13to 61-fold-higher concentration than intact antibodies caused a comparable isoelectric shift, neutralized virions in the absence of aggregation, and interfered with attachment of virions to host cell receptors in a membrane-binding assay. These findings suggest that neutralizing antibodies interfere with the attachment of rhinoviruses to cellular receptors and that bivalent attachment of antibody is not a prerequisite for neutralization.on July 6, 2020 by guest

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Section: Discussionmentioning

confidence: 80%

Section: Discussionmentioning

confidence: 96%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Inhibition of rhinovirus attachment by neutralizing monoclonal antibodies and their Fab fragments

Colonno

Callahan

Leippe

et al. 1989

J Virol

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“…Several mechanisms of antibody-mediated neutralization have been proposed. Perhaps the simplest is based on aggregation of virions (5,53,54), which generally occurs over a narrow range of antibody/virus ratios. This limited range has raised questions about the role of aggregation in vivo.…”

mentioning

confidence: 99%

Antibody-Mediated Neutralization of Human Rhinovirus 14 Explored by Means of Cryoelectron Microscopy and X-Ray Crystallography of Virus-Fab Complexes

Che

Olson

Leippe

et al. 1998

J Virol

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The structures of three different human rhinovirus 14 (HRV14)-Fab complexes have been explored with X-ray crystallography and cryoelectron microscopy procedures. All three antibodies bind to the NIm-IA site of HRV14, which is the β-B–β-C loop of the viral capsid protein VP1. Two antibodies, Fab17-IA (Fab17) and Fab12-IA (Fab12), bind bivalently to the virion surface and strongly neutralize viral infectivity whereas Fab1-IA (Fab1) strongly aggregates and weakly neutralizes virions. The structures of the two classes of virion-Fab complexes clearly differ and correlate with observed binding neutralization differences. Fab17 and Fab12 bind in essentially identical, tangential orientations to the viral surface, which favors bidentate binding over icosahedral twofold axes. Fab1 binds in a more radial orientation that makes bidentate binding unlikely. Although the binding orientations of these two antibody groups differ, nearly identical charge interactions occur at all paratope-epitope interfaces. Nucleotide sequence comparisons suggest that Fab17 and Fab12 are from the same progenitor cell and that some of the differing residues contact the south wall of the receptor binding canyon that encircles each of the icosahedral fivefold vertices. All of the antibodies contact a significant proportion of the canyon region and directly overlap much of the receptor (intercellular adhesion molecule 1 [ICAM-1]) binding site. Fab1, however, does not contact the same residues on the upper south wall (the side facing away from fivefold axes) at the receptor binding region as do Fab12 and Fab17. All three antibodies cause some stabilization of HRV14 against pH-induced inactivation; thus, stabilization may be mediated by invariant contacts with the canyon.

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Identification of poliovirions and subviral particles by capillary electrophoresis

et al. 2010

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Poliovirions, purified from infected cell extracts with anion-exchange chromatography, can be analyzed and identified by CE in untreated fused silica capillaries using UV detection. Other subviral particles can be eluted as well from the same infected cell extract using a higher salt concentration buffer on the ion-exchange chromatography. Virions can be identified because of their conversion into empty capsids upon heating at 561C. As a result of heating, the viral genome is released from the capsid. Here, we show that during this incubation some intermediate particles were found. The latter were identified by enzymatic peak shift analysis. The high salt concentration eluate subviral particles were analyzed with preincubation affinity CE together with their sensitivity for RNase and proteinase K treatment. Electropherograms of the higher salt concentration eluate display a mixture of at least four different subviral particles. One particle proved to have an [N1, H] antigenicity and was resistant to RNase and proteinase K digestion. The remaining particles were all sensitive to proteinase K treatment. This CE method proved to be valuable in the detection, identification and analysis of poliovirions and poliovirus particles offering an alternative powerful, cheap, fast and easy analysis method.

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A monoclonal antibody that neutralizes poliovirus by cross-linking virions

Cited by 42 publications

References 21 publications

Inhibition of rhinovirus attachment by neutralizing monoclonal antibodies and their Fab fragments

Inhibition of rhinovirus attachment by neutralizing monoclonal antibodies and their Fab fragments

Antibody-Mediated Neutralization of Human Rhinovirus 14 Explored by Means of Cryoelectron Microscopy and X-Ray Crystallography of Virus-Fab Complexes

Identification of poliovirions and subviral particles by capillary electrophoresis

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