title: Porcine sperm bind to specific 6-sialylated biantennary glycans to form the oviduct reservoir.
abstract: After mating, many female mammals store a subpopulation of sperm in the lower portion of the oviduct, forming a reservoir. The reservoir lengthens sperm lifespan, regulates sperm capacitation, controls polyspermy, and selects normal sperm. It is believed that sperm bind to glycans on the oviduct epithelium to form the reservoir, but the specific adhesion molecules that retain sperm are unclear. Herein, using a glycan array to test 377 glycans for their ability to bind porcine sperm, we found two glycan motifs in common among all glycans with sperm-binding ability: the Lewis X trisaccharide and biantennary structures containing a mannose core with 6-sialylated lactosamine at one or more termini. Binding to both motifs was specific; isomers of each motif did not bind sperm. Further work focused on sialylated lactosamine. Sialylated lactosamine was found abundantly on the apical side of epithelial cells collected from the oviduct isthmus, among N-linked and O-linked glycans. Sialylated lactosamine bound to the head of sperm, the region that interacts with the oviduct epithelium. After capacitation, sperm lost affinity for sialylated lactosamine. Receptor modification may contribute to release from the reservoir so that sperm can move to the site of fertilization. Sialylated lactosamine was required for sperm to bind oviduct cells. Simbucus nigra agglutinin or an antibody specific to sialylated lactosamine with a preference for Neu5Acalpha2-6Gal rather than Neu5Acalpha2-3Gal reduced sperm binding to oviduct isthmic cells, as did occupying putative receptors on sperm with sialylated biantennary glycans. These results demonstrate that sperm binding to oviduct 6-sialylated biantennary glycans is necessary for normal adhesion to the oviduct.
authors.affiliation: Department of Animal Sciences, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.
authors.forename: Govindasamy
authors.initials: G
authors.lastname: Kadirvel
authors.forename: Sergio A
authors.initials: SA
authors.lastname: Machado
authors.forename: Claudia
authors.initials: C
authors.lastname: Korneli
authors.forename: Emily
authors.initials: E
authors.lastname: Collins
authors.forename: Paul
authors.initials: P
authors.lastname: Miller
authors.forename: Kelsey N
authors.initials: KN
authors.lastname: Bess
authors.forename: Kazuhiro
authors.initials: K
authors.lastname: Aoki
authors.forename: Michael
authors.initials: M
authors.lastname: Tiemeyer
authors.forename: Nicolai
authors.initials: N
authors.lastname: Bovin
authors.forename: David J
authors.initials: DJ
authors.lastname: Miller
mesh_terms: D000606:Amino Sugars / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D000911:Antibodies, Monoclonal / Q000378:metabolism; D002448:Cell Adhesion; D016764:Cell Polarity; D004847:Epithelial Cells / Q000166:cytology / Q000378:metabolism*; D005260:Female; D054794:Glycomics / Q000379:methods; D007536:Isomerism; D016256:Lewis X Antigen / Q000031:analogs & derivatives; D008297:Male; D046228:Microarray Analysis; D015394:Molecular Structure; D010057:Oviducts / Q000166:cytology / Q000378:metabolism*; D037121:Plant Lectins / Q000378:metabolism; D011134:Polysaccharides / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D013075:Sperm Capacitation; D013077:Sperm Head / Q000378:metabolism; D013083:Sperm Transport; D013094:Spermatozoa / Q000166:cytology / Q000378:metabolism*; D013499:Surface Properties; D034421:Sus scrofa / Q000502:physiology*; D014312:Trisaccharides / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism
chemical_list: D000606:Amino Sugars; D000911:Antibodies, Monoclonal; D016256:Lewis X Antigen; D037121:Plant Lectins; D011134:Polysaccharides; D014312:Trisaccharides; C110530:galactosyl-(1,4)-fucopyranosyl-(1,3)-N-acetylglucosamine; C032233:lactosamine