Nectarine reactivity targets protein families common to stone fruits (Prunus species), including PR-10 homologs, profilins, and lipid transfer proteins (LTPs). These proteins are plant-derived allergens or antigenic components that can trigger antibody binding in sensitized individuals. Taxonomically, nectarines are closely related to peaches and share many conserved proteins that can cross-react immunologically. Historically, links between pollen and fruit proteins (pollen–food cross-reactivity) highlighted PR-10 and profilin families as causes of cross-sensitization; LTPs were later recognized for their stability across digestion and processing. Biologically, the proteins measured are involved in plant defense and structure, but in human testing they serve as targets for IgA and IgG antibody assays to map immune recognition patterns to this specific food source.

Elevated antibody signals to nectarine proteins may indicate prior immune exposure or sensitization to nectarines or closely related stone fruits; higher IgA could reflect mucosal/gut-associated responses while higher IgG may reflect systemic immune recognition. Low or absent signals generally indicate little to no detectable antibody response to nectarine proteins at the time of sampling, which can occur with limited exposure or immune tolerance. All results should be interpreted alongside the full Food Zoomer panel and clinical history. Cross-reactivity with other Rosaceae fruits or pollen can influence patterns, so isolated nectarine reactivity is best understood in the context of related fruit and environmental markers on the report.

Nectarine is included to detect antibody reactivity to a common stone fruit and its specific protein families. At the peptide and isotype level, the marker helps distinguish mucosal versus systemic patterns and clarifies cross-reactivity with related fruits, supporting targeted dietary planning and personalized interpretation within the Food Zoomer profile.