Imperial College London
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ProfessorGrahamCooke

Faculty of Medicine, Department of Infectious Disease

Vice Dean (Research); Professor of Infectious Diseases
 
 
 
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Contact

 

g.cooke

 
 
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Location

 

Infectious Diseases SectionMedical SchoolSt Mary's Campus

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Summary

 

Publications

Citation

BibTex format

@article{Rosadas:2022:10.1016/j.jviromet.2022.114475,
author = {Rosadas, C and Khan, M and Parker, E and Marchesin, F and Katsanovskaja, K and Sureda-Vives, M and Fernandez, N and Randell, P and Harvey, R and Lilley, A and Harris, BH and Zuhair, M and Fertleman, M and Ijaz, S and Dicks, S and Short, C-E and Quinlan, R and Taylor, GP and Hu, K and McKay, P and Rosa, A and Roustan, C and Zuckerman, M and El, Bouzidi K and Cooke, G and Flower, B and Moshe, M and Elliott, P and Spencer, AJ and Lambe, T and Gilbert, SC and Kingston, H and Baillie, JK and Openshaw, PJ and G, Semple M and ISARIC4C, Investigators and Cherepanov, P and O, McClure M and S, Tedder R},
doi = {10.1016/j.jviromet.2022.114475},
journal = {Journal of Virological Methods},
title = {Detection and quantification of antibody to SARS CoV 2 receptor binding domain provides enhanced sensitivity, specificity and utility},
url = {http://dx.doi.org/10.1016/j.jviromet.2022.114475},
volume = {302},
year = {2022}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Accurate and sensitive detection of antibody to SARS-CoV-2 remains an essential component of the pandemic response. Measuring antibody that predicts neutralising activity and the vaccine response is an absolute requirement for laboratory-based confirmatory and reference activity. The viral receptor binding domain (RBD) constitutes the prime target antigen for neutralising antibody. A double antigen binding assay (DABA), providing the most sensitive format has been exploited in a novel hybrid manner employing a solid-phase S1 preferentially presenting RBD, coupled with a labelled RBD conjugate, used in a two-step sequential assay for detection and measurement of antibody to RBD (anti-RBD). This class and species neutral assay showed a specificity of 100% on 825 pre COVID-19 samples and a potential sensitivity of 99.6% on 276 recovery samples, predicting quantitatively the presence of neutralising antibody determined by pseudo-type neutralisation and by plaque reduction. Anti-RBD is also measurable in ferrets immunised with ChadOx1 nCoV-19 vaccine and in humans immunised with both AstraZeneca and Pfizer vaccines. This assay detects anti-RBD at presentation with illness, demonstrates its elevation with disease severity, its sequel to asymptomatic infection and its persistence after the loss of antibody to the nucleoprotein (anti-NP). It also provides serological confirmation of prior infection and offers a secure measure for seroprevalence and studies of vaccine immunisation in human and animal populations. The hybrid DABA also displays the attributes necessary for the detection and quantification of anti-RBD to be used in clinical practice. An absence of detectable anti-RBD by this assay predicates the need for passive immune prophylaxis in at-risk patients.
AU  - Rosadas,C
AU  - Khan,M
AU  - Parker,E
AU  - Marchesin,F
AU  - Katsanovskaja,K
AU  - Sureda-Vives,M
AU  - Fernandez,N
AU  - Randell,P
AU  - Harvey,R
AU  - Lilley,A
AU  - Harris,BH
AU  - Zuhair,M
AU  - Fertleman,M
AU  - Ijaz,S
AU  - Dicks,S
AU  - Short,C-E
AU  - Quinlan,R
AU  - Taylor,GP
AU  - Hu,K
AU  - McKay,P
AU  - Rosa,A
AU  - Roustan,C
AU  - Zuckerman,M
AU  - El,Bouzidi K
AU  - Cooke,G
AU  - Flower,B
AU  - Moshe,M
AU  - Elliott,P
AU  - Spencer,AJ
AU  - Lambe,T
AU  - Gilbert,SC
AU  - Kingston,H
AU  - Baillie,JK
AU  - Openshaw,PJ
AU  - G,Semple M
AU  - ISARIC4C,Investigators
AU  - Cherepanov,P
AU  - O,McClure M
AU  - S,Tedder R
DO  - 10.1016/j.jviromet.2022.114475
PY  - 2022///
SN  - 0166-0934
TI  - Detection and quantification of antibody to SARS CoV 2 receptor binding domain provides enhanced sensitivity, specificity and utility
T2  - Journal of Virological Methods
UR  - http://dx.doi.org/10.1016/j.jviromet.2022.114475
UR  - https://www.ncbi.nlm.nih.gov/pubmed/35077719
UR  - http://hdl.handle.net/10044/1/95238
VL  - 302
ER  -
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