Several plant lectins were used to characterize the cell-surface carbohydrates expressed on sensory ganglion cells and their central terminals in the spinal cord dorsal horn. In the rat, galactose-terminal glycoconjugates on a large subpopulation of small neurons whose central axons project to the substantia gelatinosa were demonstrated with the alpha-D-galactose-specific Griffonia Simplicifolia I-B4 (GSA) lectin. This neuron subset was labelled by alternative D-galactose-, N-Acetylgalactosamine-, and beta Gal(1,3)NAcGal-binding lectins. Similar GSA lectin reactivity was also illustrated in selected peripheral autonomic, gustatory and visceral sensory and enteric neurons, and the accessory olfactory bulb. The sensory neuron-specific isoenzyme, fluoride-resistant acid phosphatase (FRAP) co-localized with the GSA lectin, as did the monoclonal antibody (MAb) 2C5, which is directed against a lactoseries carbohydrate constituting a backbone structure of ABH human blood group antigens. In contrast, calcitonin gene-related peptide-immunoreactivity (CGRP-IR), used as a representative marker of peptidergic neurons, exhibited limited co-localization with GSA. A polyclonal anti-rat red blood cell (RBC) antibody co-localized with GSA, suggesting that lectin-reactive carbohydrates on rat sensory neurons are related to rat RBC antigens. In the human spinal cord, the L-fucose-binding Ulex europaeus-I (UEA) lectin also labelled the substantia gelatinosa; in rabbit, a small sensory ganglion cell subset and the spinal cord substantial gelatinosa was co-labelled by both the GSA and UEA lectins. These studies illustrate significant lectin-reactive cell surface carbohydrate expression by non-peptidergic, FRAP(+) sensory ganglion cells in the rat, and provide a means for visualizing the extensive, non-peptidergic, small sensory ganglion cell subpopulations, probably including a substantial proportion of nociceptive and unmyelinated peripheral axons.