We have developed IP for a SARS-CoV-2 corona virus in situ intravital detection (COVISID) assay, which is based on an enzymatic immune- proximity complementation approach that produces a distinct odor and taste as positive readout. SARS-CoV-2-specific antibodies (or derivatives thereof), conjugated to a substrate-converting enzymatic moiety, will be applied as aerosol via a standard, “asthma spray-like” inhaler to the nasopharyngeal mucosa. No washing step is required, since normal breathing for a few minutes will exhale unbound antibody. Consecutively, a second inhalation delivers an aerosol containing the substrate for the enzymatic activity. By this “flavor & fragrance” strategy the SARS-CoV- 2-bound antibody/enzyme conjugate converts an odor- and tasteless substrate into a smell and taste signal, objectively recognizable by both the individual itself and its surroundings. To ensure high specificity we have divided the enzymatic moiety – an esterase activity that cleaves a butyric ester to butyric acid – into two individually inert components that only operate as an enzyme if brought into close proximity in situ by binding to SARS-CoV-2. Split-enzyme-conjugated antibodies might also be administered in one single aerosol formulation together with its substrate due to the lack of activity if not placed in close proximity. This platform technology can rapidly be adapted to detect other respiratory tract infectious agents.