A recent analysis of the human sperm N-glycome confirmed the expression of biantennary bisecting type N-glycans and terminal Lewis(x)/Lewis(y) sequences previously implicated in the suppression of the innate and adaptive immune responses, respectively. In this study, glycomic analysis of seminal plasma glycoproteins derived from four fertile men was carried out to determine if the same sequences were expressed on the N- and O-glycome of human seminal plasma glycoproteins. Three major families of N-glycans were detected: (i) high mannose glycans (Man(5-7)GlcNAc(2)); (ii) bi-, tri-, and tetraantennary core-fucosylated complex type N-glycans with antennae terminated with Lewis(x) and/or Lewis(y) sequences; and (iii) bi-, tri-, and tetraantennary core-fucosylated complex type N-glycans with antennae capped with sialic acid. Analysis of the O-glycans revealed Core 1 and Core 2 type structures that are also fucosylated or sialylated or a combination of both. The same high mannose and polyfucosylated N-glycans associated with sperm are also present in seminal plasma. Bisecting type N-glycan expression is greatly decreased compared to sperm, while sialylated glycans are abundant in some individuals and minor in others. In summary, the glycosylation profile of seminal plasma glycoproteins is consistent with the modulation of the adaptive but not the innate arm of the human immune response.