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Multiple receptors for sulfated Lewis X trisaccharide and sialylated N ‐acetyllactosamine are present on the boar sperm plasma membrane contributing to oviduct reservoir formation
Author(s) -
Silva Elena,
Miller David,
Bovin Nicolai
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.828.2
Subject(s) - sperm , receptor , oviduct , chemistry , glycan , medicine , endocrinology , biology , glycoprotein , biochemistry , genetics
After insemination, a sperm reservoir is established in the oviduct by sperm binding to oviductal glycans containing sulfated Lewis X (sLe X ) and biantennary sialylated N ‐acetyllactosamine (SiLN) motifs. Based on a binding assay to fluoresceinated sLe X , SiLN or N ‐acetyllactosamine (LN) glycans, we localized glycan receptors on the sperm plasma membrane. Fluorescent staining revealed two binding regions: the anterior head region (AR) or both the anterior and posterior region (APR). sLe X bound preferentially to the AR (71.0% of sperm) and LN to the APR (98.9% of sperm) whereas SiLN bound to both regions, suggesting the involvement of two distinct receptors. Sperm preferentially bound to sLe X and SiLN compared to LN (61.5, 61.7 and 25.2% of sperm bound respectively, P=0.001), indicating the necessity of sialic acid and multivalency for optimal glycan recognition. Glycan blot analysis identified several proteins that bind specifically to sLe X with apparent molecular weights of 250, 130, 80, 55 and 47 kD. Bands of 70 and 37 kD recognized sLe X and SiLN, whereas a 15kD band recognized all three motifs. Based on these results, we determined that sperm recognition of the sLe X motif is mediated by multiple receptors that may also recognize the SiLN motif. We propose a binding model in which Lewis X and SiLN receptors are components of sperm adhesion to the oviduct. Supported by USDA Grant no. 2011–67015‐20099.