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J Med Virol . The challenge of avidity determination in SARS-CoV-2 serology

tetano

Editor, Senior Moderator
J Med Virol


. 2021 Feb 10.
doi: 10.1002/jmv.26863. Online ahead of print.
The challenge of avidity determination in SARS-CoV-2 serology


Georg Bauer[SUP] 1 2 [/SUP], Friedhelm Struck[SUP] 3 [/SUP], Patrick Schreiner[SUP] 3 [/SUP], Eva Staschik[SUP] 3 [/SUP], Erwin Soutschek[SUP] 3 [/SUP], Manfred Motz[SUP] 3 [/SUP]



Affiliations

Abstract

The serological responses towards SARS-CoV-2 nucleoprotein (NP), receptor-binding domain (RBD) and spike protein S1 are characterized by immature avidity maturation. Analysis with varying concentrations of urea allows to determine distinct differences in avidity maturation, though the total process remains at an unusually low level. Despite incomplete avidity maturation, this approach allows to define early and late stages of infection. It therefore can compensate for the recently described irregular kinetic patterns of IgM and IgG directed towards SARS-CoV-2 antigens. The serological responses towards seasonal coronaviruses neither have a negative nor positive impact on SARS-CoV-2 serology in general. Avidity determination in combination with measurement of antibody titers and complexity of the immune response allows to clearly differentiate between IgG responses towards seasonal coronaviruses and SARS-CoV-2. Cross-reactions seem to occur with very low probability. They can be recognized by their pattern of response and through differential treatment with urea. As high avidity has been shown to be essential in several virus systems for the protective effect of neutralizing antibodies, it should be clarified whether high avidity of IgG directed towards RBD indicates protective immunity. If this is the case, monitoring of avidity should be part of the optimization of vaccination programs. This article is protected by copyright. All rights reserved.

Keywords: SARS-CoV-2; avidity; nucleoprotein; protective immunity; receptor-binding domain; seasonal coronavirus.
 
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