ArticleAnalytical and bioanalytical chemistry2025
Development of a novel method for generating Q-bodies using tyrosinase-mediated HA-tag labeling.
Article in Analytical and bioanalytical chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Quenchbodies (Q-bodies) are fluorescent antibodies that respond to antigen binding via a fluorescence quenching and de-quenching mechanism. To enhance the versatility of the generation method and expand the color range, we developed a novel Q-body generation approach using tyrosinase-mediated site-specific conjugation to a tyrosine-rich hemagglutinin (HA)-tag. A single-chain variable fragment (scFv) against programmed cell death-ligand 1 (PDL1) was engineered with an N-terminal HA-tag and expressed in Escherichia coli with high yield and purity. Site-specific conjugation of four hydrazide-functionalized dyes with different emission wavelengths was achieved using recombinant tyrosinase. The resulting Q-bodies were evaluated via fluorescence-linked immunosorbent assay, all of which demonstrated antigen concentration-dependent fluorescence enhancement. Notably, the tetramethylrhodamine (TAMRA)-labeled Q-body showed the highest signal-to-background ratio, limit of detection of 0.51 ± 0.01 μg/mL. This HA-tag-mediated Q-body generation strategy offers a robust and versatile tool for the production of Q-bodies with broad dye compatibility, enabling sensitive and multiplexed fluorescent immunoassays.
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