Relationship between poliovirus neutralization and aggregation

Thomas, Adrianus; Vrijsen, Raphael; Boeyé, Albert

doi:10.1128/jvi.59.2.479-485.1986

Cited by 45 publications

(25 citation statements)

References 21 publications

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“…With the exception of antibody NImII-35, the nonaggregated virions displayed neutral pl values and restored infectivity ( Table 2). These data are similar to data obtained in earlier studies performed on poliovirus (13,16,28). Virions characterized after neutralization with NImII-35 and subsequent papain treatment differed significantly from virions neutralized with the other antibodies tested.…”

Section: Discussionsupporting

confidence: 89%

“…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: 79%

“…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).…”

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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: Discussionsupporting

confidence: 89%

Section: Discussionmentioning

confidence: 79%

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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“…Neutralization is an important function of antibodies that recognize respiratory viruses, and the development of a neutralizing antibody response is the primary goal of most vaccines [316,317]. Antibody-mediated neutralization can occur by steric hindrance or by directly binding to viral spike proteins and blocking virus binding or fusion to the host cell [315,318,319]. Neutralizing antibodies are an important component of immunity against influenza [320], RSV [321,322], coronavirus [323], rhinovirus [324], and Sendai virus [325] infection.…”

Section: Adaptive Immunity-b Cells and Antibodiesmentioning

confidence: 99%

Pulmonary immunity to viruses

Allie

Randall

2017

Clinical Science

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Mucosal surfaces, such as the respiratory epithelium, are directly exposed to the external environment and therefore, are highly susceptible to viral infection. As a result, the respiratory tract has evolved a variety of innate and adaptive immune defenses in order to prevent viral infection or promote the rapid destruction of infected cells and facilitate the clearance of the infecting virus. Successful adaptive immune responses often lead to a functional state of immune memory, in which memory lymphocytes and circulating antibodies entirely prevent or lessen the severity of subsequent infections with the same virus. This is also the goal of vaccination, although it is difficult to vaccinate in a way that mimics respiratory infection. Consequently, some vaccines lead to robust systemic immune responses, but relatively poor mucosal immune responses that protect the respiratory tract. In addition, adaptive immunity is not without its drawbacks, as overly robust inflammatory responses may lead to lung damage and impair gas exchange or exacerbate other conditions, such as asthma or chronic obstructive pulmonary disease (COPD). Thus, immune responses to respiratory viral infections must be strong enough to eliminate infection, but also have mechanisms to limit damage and promote tissue repair in order to maintain pulmonary homeostasis. Here, we will discuss the components of the adaptive immune system that defend the host against respiratory viral infections.

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“…Currently available techniques for direct determination of the number of antibodies bound to virus particles include assays with radiolabeled antibodies,13–18 sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS‐PAGE),19 capillary electrophoresis (CE),20 and enzyme‐linked immunosorbent assays (ELISA) 21. These techniques typically require: 1) a minimum concentration of 3×10 9 particles mL −1 (ELISA and CE typically use >3×10 11 particles mL −1 ), 2) labeled antibodies, 3) reaction volumes ranging from 10 μL (CE) to ≥100 μL, and 4) in most cases, fairly bulky and sophisticated laboratory equipment with high power requirements (such as a CE apparatus, plate readers, etc).…”

mentioning

confidence: 99%

Submicrometer Pore‐Based Characterization and Quantification of Antibody–Virus Interactions

Uram

Hunt

et al. 2006

Small

120

113

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A resistive‐pulse sensor (see scheme) employs a submicrometer pore for the detection, characterization, and quantification of the binding of polyclonal antibodies to intact Paramecium bursaria chlorella virus (PBCV‐1) particles. The assay is rapid, label‐free, requires no immobilization or modification of the antibody or virus, detects the formation of viral aggregates, and can be performed using antibodies in complex media such as serum. The maximum number of antibodies able to bind to the virus was estimated to be 4200±450.

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Relationship between poliovirus neutralization and aggregation

Cited by 45 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

Pulmonary immunity to viruses

Submicrometer Pore‐Based Characterization and Quantification of Antibody–Virus Interactions

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