High and low efficiency neutralization epitopes on the haemagglutinin of type A influenza virus.

Schofield, Darren J.; Stephenson, John; Dimmock, Nigel J.

doi:10.1099/0022-1317-78-10-2441

Cited by 20 publications

(23 citation statements)

References 38 publications

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“…Their ranking order was (HC61, HC2, HC3W) HC58 HC10. Very similar ranking was obtained by kinetic analysis with a flow system, surface plasmon resonance (SPR) and captured whole influenza A virions, except that no data could be obtained for HC58 IgG (Schofield & Dimmock, 1996 ;Schofield et al, 1997). As others have found, affinities (K dissoc. )…”

Section: Discussion Neutralizationsupporting

confidence: 54%

“…Titres ranged nearly 6-fold from 1n2 to 6n8 nM. This contrasts with the rates of neutralization which varied by 40-fold (Schofield & Dimmock, 1997), indicating that rate is a more stringent parameter of antiviral efficacy than specific activity. Conversion to F(abh) # reduced neutralization by a small but reproducible amount (2-to 3-fold : Fig.…”

Section: Resultsmentioning

confidence: 40%

“…l 4n1 to 14 nM), and varied by only 3n4-fold in a system in which virus and IgG were reacted to equilibrium (Schofield et al, 1997). Their ranking order was (HC61, HC2, HC3W) HC58 HC10.…”

Section: Discussion Neutralizationmentioning

confidence: 99%

“…However, over 100-fold more HC58 was required to give the same HI titre as HC61. This was unexpected as HI is generally regarded to occur by simple steric inhibition of the attachment of virus to RBCs by antibody, and HC58 has the second highest functional affinity by an equilibrium method (Schofield & Dimmock, 1997). All IgGs lost 3-to 6-fold HI activity on conversion to F(abh) # fragments (Table 2).…”

Section: Haemagglutination-inhibition By Igg F(abh) 2 Fab and Fabmentioning

confidence: 99%

“…Data are discussed with reference to the three-dimensional structure of the HA (Wiley et al, 1981), functional affinities (Schofield & Dimmock, 1996 ;Schofield et al, 1997), and mechanisms of action .…”

Section: Introductionmentioning

confidence: 99%

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Variations in the neutralizing and haemagglutination-inhibiting activities of five influenza A virus-specific IgGs and their antibody fragments.

Schofield

Stephenson

Dimmock

1997

Journal of General Virology

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Neutralization and haemagglutination-inhibition (HI) of a type A influenza virus by a panel of five monoclonal IgGs, their F(abh) 2 s, Fabs and FabsM anti-mouse Fab were compared. The MAbs were specific for antigenic sites A, B and D of the haemagglutinin. Activities of the IgGs varied by up to 6-fold on a molar basis, apart from the HI activity of HC58 which was 100-fold lower. This was not due to low functional affinity as HC58 had the second highest value (nM) as determined by an equilibrium method with whole virions. Conversion to the F(abh) 2 reduced neutralization and HI by only 2-to 6-fold, indicating that the Fc region had little involvement in these processes. However, all Fabs had low neutralization and HI activity compared with their IgGs, neutralization being reduced by 86

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Section: Discussion Neutralizationsupporting

confidence: 54%

Section: Resultsmentioning

confidence: 40%

“…l 4n1 to 14 nM), and varied by only 3n4-fold in a system in which virus and IgG were reacted to equilibrium (Schofield et al, 1997). Their ranking order was (HC61, HC2, HC3W) HC58 HC10.…”

Section: Discussion Neutralizationmentioning

confidence: 99%

Section: Haemagglutination-inhibition By Igg F(abh) 2 Fab and Fabmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Variations in the neutralizing and haemagglutination-inhibiting activities of five influenza A virus-specific IgGs and their antibody fragments.

Schofield

Stephenson

Dimmock

1997

Journal of General Virology

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Analysis of the relationship between immunogenicity and immunity for viral subunit vaccines

Wilson¹,

Nokes²,

Dimmock³

2001

Journal of Medical Virology

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The prevention of viral infection by vaccination relies on stimulating an appropriate immune response in order to reduce the probability with which a virus can establish an infection. Post-vaccination antibody responses have therefore been associated with reducing the probability with which an individual can be infected (i.e., the vaccine's "impact"). Quantifying this relationship is essential in evaluating new vaccines, especially since comparisons between vaccines, and vaccine licensure, may be dependent on antibody responses alone. In this paper two principal questions are identified which need to be addressed in the evaluation of subunit vaccines: i) how do specific antibody levels relate to complete protection from infection or disease and ii) how do antigenic subunits interact in developing protection when combined together in a single vaccine. The aim is to identify explicitly certain assumptions that are frequently made implicitly in the discussion of vaccine action. First, antibody levels are related to levels of protection through a novel statistical analysis of incidence data from a published hepatitis B vaccine trial. The antibody response observed after influenza A virus infection is discussed in relation to the selection of neutralisation escape variants. Finally, by way of example, a theoretical situation is examined and three simple models of subunit vaccine action are constructed in order to describe how antibody levels may be related to population level phenomena such as the elimination of an infection by mass vaccination.

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Valency of antibody binding to virions and its determination by surface plasmon resonance

Dimmock

Hardy

2004

Reviews in Medical Virology

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All IgGs are homobivalent, but their ability to bind bivalently to the surface of a virus particle depends mainly on a favourable spacing of cognate epitopes and the angle that the FAb arm makes with the virus surface. If the angle of binding forces the second FAb arm to point into solution, monovalent binding is inevitable. This IgG will have the same affinity as its FAb, will be less stably bound than if it were bound bivalently, cannot cross-link epitopes on the surface of a virion, and cannot neutralise by cross-linking surface proteins. However, at moderate IgG concentrations, monovalently bound IgG can reduce infectivity by aggregating virions, a phenomenon that cannot occur with IgG bound bivalently. This review describes how surface plasmon resonance can be used to determine the valency of IgG binding to enveloped and non-enveloped virus particles, and discusses the implications of this new methodology.

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High and low efficiency neutralization epitopes on the haemagglutinin of type A influenza virus.

Cited by 20 publications

References 38 publications

Variations in the neutralizing and haemagglutination-inhibiting activities of five influenza A virus-specific IgGs and their antibody fragments.

Variations in the neutralizing and haemagglutination-inhibiting activities of five influenza A virus-specific IgGs and their antibody fragments.

Analysis of the relationship between immunogenicity and immunity for viral subunit vaccines

Valency of antibody binding to virions and its determination by surface plasmon resonance

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