TY - JOUR
T1 - Recombinant β-defensin 126 promotes bull sperm binding to bovine oviductal epithelia
AU - Lyons, A.
AU - Narciandi, F.
AU - Donnellan, E.
AU - Romero-Aguirregomezcorta, J.
AU - Farrelly, C. O.
AU - Lonergan, P.
AU - Meade, K. G.
AU - Fair, S.
N1 - Publisher Copyright:
© CSIRO 2018.
PY - 2018
Y1 - 2018
N2 - Primate β-defensin 126 regulates the ability of spermatozoa to bind to oviductal epithelial cells in vitro. Bovine β-defensin 126 (BBD126) exhibits preferential expression in the cauda epididymis of the bull, but there have been few studies on its functional role in cattle. The aim of the present study was to examine the role of BBD126 in bull sperm binding to bovine oviductal epithelial cell (BOEC) explants. BBD126 has been shown to be highly resistant to the standard methods of dissociation used in other species and, as a result, corpus epididymal spermatozoa, which have not been exposed to the protein, were used to study the functional role of BBD126. Corpus epididymal spermatozoa were incubated with recombinant (r) BBD126 in the absence or presence of anti-BBD126 antibody. Addition of rBBD126 significantly enhanced the ability of epididymal spermatozoa to bind to BOEC explants (P < 0.05). Anti-BBD126 antibody blocked the BBD126-mediated increase in sperm binding capacity. Ejaculated spermatozoa, which are coated with native BBD126 protein but also a large number of seminal plasma proteins in vivo, were incubated with rBBD126 in the absence or presence of the anti-BBD126 antibody. Addition of rBBD126 significantly enhanced the ability of ejaculated spermatozoa to bind to BOEC explants (P < 0.05), whereas rBBD126 also reduced corpus sperm agglutination (P < 0.05). These results suggest that, similar to the role of its analogue in the macaque, spermatozoa with more BBD126 in their acrosome may represent spermatozoa with more oviduct binding capacity.
AB - Primate β-defensin 126 regulates the ability of spermatozoa to bind to oviductal epithelial cells in vitro. Bovine β-defensin 126 (BBD126) exhibits preferential expression in the cauda epididymis of the bull, but there have been few studies on its functional role in cattle. The aim of the present study was to examine the role of BBD126 in bull sperm binding to bovine oviductal epithelial cell (BOEC) explants. BBD126 has been shown to be highly resistant to the standard methods of dissociation used in other species and, as a result, corpus epididymal spermatozoa, which have not been exposed to the protein, were used to study the functional role of BBD126. Corpus epididymal spermatozoa were incubated with recombinant (r) BBD126 in the absence or presence of anti-BBD126 antibody. Addition of rBBD126 significantly enhanced the ability of epididymal spermatozoa to bind to BOEC explants (P < 0.05). Anti-BBD126 antibody blocked the BBD126-mediated increase in sperm binding capacity. Ejaculated spermatozoa, which are coated with native BBD126 protein but also a large number of seminal plasma proteins in vivo, were incubated with rBBD126 in the absence or presence of the anti-BBD126 antibody. Addition of rBBD126 significantly enhanced the ability of ejaculated spermatozoa to bind to BOEC explants (P < 0.05), whereas rBBD126 also reduced corpus sperm agglutination (P < 0.05). These results suggest that, similar to the role of its analogue in the macaque, spermatozoa with more BBD126 in their acrosome may represent spermatozoa with more oviduct binding capacity.
KW - oviduct
UR - http://www.scopus.com/inward/record.url?scp=85048265661&partnerID=8YFLogxK
U2 - 10.1071/RD17415
DO - 10.1071/RD17415
M3 - Article
C2 - 29773109
AN - SCOPUS:85048265661
SN - 1031-3613
VL - 30
SP - 1472
EP - 1481
JO - Reproduction, Fertility and Development
JF - Reproduction, Fertility and Development
IS - 11
ER -