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Monitoring SARS-CoV-2 IgA, IgM and IgG antibodies in dried blood and saliva samples using antibody proximity extension assays (AbPEA)
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Immunology, Genetics and Pathology, Molecular Tools and Functional Genomics. Uppsala University, Science for Life Laboratory, SciLifeLab.
Uppsala University, Science for Life Laboratory, SciLifeLab. Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Immunology, Genetics and Pathology, Molecular Tools and Functional Genomics.ORCID iD: 0000-0002-1303-2218
Uppsala University, Science for Life Laboratory, SciLifeLab. Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Immunology, Genetics and Pathology, Molecular Tools and Functional Genomics.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Immunology, Genetics and Pathology. Uppsala University, Science for Life Laboratory, SciLifeLab.
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2024 (English)In: Scientific Reports, E-ISSN 2045-2322, Vol. 14, no 1, article id 21655Article in journal (Refereed) Published
Abstract [en]

Using a modified proximity extension assay, total and immunoglobulin (Ig) class-specific anti-SARS-CoV-2 antibodies were sensitively and conveniently detected directly from & oslash;1.2 mm discs cut from dried blood and saliva spots (DBS and DSS) without the need for elution. For total Ig detection, antigen probes were prepared by conjugating recombinant spike protein subunit 1 (S1-RBD) to a pair of oligonucleotides. To detect isotype-specific antibody reactivity, one antigen probe was replaced with oligonucleotide-conjugated antibodies specific for antibody isotypes. Binding of pairs of oligonucleotide-conjugated probes to antibodies in patient samples brings oligonucleotides in proximity. An added DNA polymerase uses a transient hybridization between the oligonucleotides to prime synthesis of a DNA strand, which serves as a DNA amplicon that is quantified by real-time PCR. The S1-RBD-specific IgG, IgM, and IgA antibodies in DBS samples collected over the course of a first and second vaccination exhibited kinetics consistent with previous reports. Both DBS and DSS collected from 42 individuals in the autumn of 2023 showed significant level of total S1-RBD antibodies with a correlation of R = 0.70. However, levels in DSS were generally 10 to 100-fold lower than in DBS. Anti-S1-RBD IgG and IgA in DSS demonstrated a correlation of R = 0.6.

Place, publisher, year, edition, pages
Springer Nature, 2024. Vol. 14, no 1, article id 21655
Keywords [en]
Immunoassays, Antibody proximity extension assay, Antibody isotypes, IgG, IgM, IgA, SARS-CoV-2 antibody, Vaccination, Dried blood spot (DBS), Dried saliva spot (DSS), Real-time PCR
National Category
Immunology in the medical area Infectious Medicine Clinical Laboratory Medicine
Identifiers
URN: urn:nbn:se:uu:diva-540655DOI: 10.1038/s41598-024-72453-5ISI: 001317187900044PubMedID: 39289450OAI: oai:DiVA.org:uu-540655DiVA, id: diva2:1907410
Funder
Knut and Alice Wallenberg Foundation, 2020.0182Knut and Alice Wallenberg Foundation, SB16-0046Swedish Foundation for Strategic Research, SB16-0046Swedish Research Council, 2020-02258Science for Life Laboratory, SciLifeLabAvailable from: 2024-10-22 Created: 2024-10-22 Last updated: 2024-10-22Bibliographically approved

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Wang, MengqiKamali-Moghaddam, MasoodLöf, LizaÅberg, MikaelLandegren, UlfZhao, Hongxing

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Wang, MengqiKamali-Moghaddam, MasoodLöf, LizaÅberg, MikaelLandegren, UlfZhao, Hongxing
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Molecular Tools and Functional GenomicsScience for Life Laboratory, SciLifeLabDepartment of Immunology, Genetics and PathologyDepartment of Medical Sciences
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