ArticleAnalytical chemistry2025
Development of a Liposome-Based Serological Assay for SARS-CoV-2 Variants with Special Emphasis on Coupling Chemistries Required to Maintain Protein Antigenicity.
Article in Analytical chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
4 citing papers in PubMed.
- His-Tag-Aptamer-Liposome-Conjugates as a Multipurpose Tool for Recombinant Protein Screening and Protein-Based Bioassays.Analytical chemistry · 2026Article
- Engineering Liposomes and Polymer Conjugates: A Platform for Mechanistic Complement Activation Studies and Controlled Release Applications.ACS applied materials & interfaces · 2026Article
- From Population Averaging to Single Event Resolution: Evolution of Sensing Platforms for Membrane Fusion.Sensors (Basel, Switzerland) · 2026Review
- Development of a Novel Homogeneous Liposome-Based One-Step Assay for SARS-CoV-2 Antibody Detection in Human Serum Based on Fluorescent Liposomes and Complement Activity.Analytical chemistry · 2025Article
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The conjugation of proteins to the outer membranes of liposomes is a standard procedure used in bioanalytical and drug delivery approaches. Herein, we describe the development of a liposome-based surrogate assay for the quantification of SARS-CoV-2 neutralizing antibodies. Taking into consideration differences in amino acid sequences within the receptor-binding domain (RBD) of SARS-CoV-2 Spike proteins derived from five selected variants of concern (VoC), we studied the impact of coupling chemistries on physicochemical properties and antigenicity. Naturally occurring lysine residues were used for standard EDC/NHS chemistry, while an N-terminal Cys-tag and a C-terminal Avi-tag were genetically added to the proteins for site-directed immobilization. Despite only minor differences regarding the number, positioning, and sequence context of lysine residues within the different RBD variants, those differences led to a dramatic change in their functionality after EDC/NHS coupling. In contrast, site-specific biotinylation of the proteins alongside targeted immobilization on streptavidin- or neutravidin-modified liposomes resulted in restored functionality and enhanced storage stability across all variants. The developed adaptable liposome-based test showed excellent correlation with an established pseudovirus neutralization test and could identify variations in neutralization patterns of Alpha/Delta and Omicron variants in patient sera. The study highlights the benefits of using neutravidin-liposomes for site-directed protein immobilization with independence from the proteins' amino acid sequences, enhanced storage stability, and applicability to various biotinylation strategies, serving as a versatile platform technology that can also be applied to the coupling of other proteins or peptides used for diagnostic purposes.
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Registered trials
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