TY - JOUR
T1 - Semen amyloids participate in spermatozoa selection and clearance
AU - Roan, Nadia R.
AU - Sandi-Monroy, Nathallie
AU - Kohgadai, Nargis
AU - Usmani, Shariq M.
AU - Hamil, Katherine G.
AU - Neidleman, Jason
AU - Montano, Mauricio
AU - Ständker, Ludger
AU - Röcker, Annika
AU - Cavrois, Marielle
AU - Rosen, Jared
AU - Marson, Kara
AU - Smith, James F.
AU - Pilcher, Christopher D.
AU - Gagsteiger, Friedrich
AU - Sakk, Olena
AU - O’Rand, Michael
AU - Lishko, Polina V.
AU - Kirchhoff, Frank
AU - Münch, Jan
AU - Greene, Warner C.
N1 - Publisher Copyright:
© Roan et al.
PY - 2017/6/27
Y1 - 2017/6/27
N2 - Unlike other human biological fluids, semen contains multiple types of amyloid fibrils in the absence of disease. These fibrils enhance HIV infection by promoting viral fusion to cellular targets, but their natural function remained unknown. The similarities shared between HIV fusion to host cell and sperm fusion to oocyte led us to examine whether these fibrils promote fertilization. Surprisingly, the fibrils inhibited fertilization by immobilizing sperm. Interestingly, however, this immobilization facilitated uptake and clearance of sperm by macrophages, which are known to infiltrate the female reproductive tract (FRT) following semen exposure. In the presence of semen fibrils, damaged and apoptotic sperm were more rapidly phagocytosed than healthy ones, suggesting that deposition of semen fibrils in the lower FRT facilitates clearance of poor-quality sperm. Our findings suggest that amyloid fibrils in semen may play a role in reproduction by participating in sperm selection and facilitating the rapid removal of sperm antigens.
AB - Unlike other human biological fluids, semen contains multiple types of amyloid fibrils in the absence of disease. These fibrils enhance HIV infection by promoting viral fusion to cellular targets, but their natural function remained unknown. The similarities shared between HIV fusion to host cell and sperm fusion to oocyte led us to examine whether these fibrils promote fertilization. Surprisingly, the fibrils inhibited fertilization by immobilizing sperm. Interestingly, however, this immobilization facilitated uptake and clearance of sperm by macrophages, which are known to infiltrate the female reproductive tract (FRT) following semen exposure. In the presence of semen fibrils, damaged and apoptotic sperm were more rapidly phagocytosed than healthy ones, suggesting that deposition of semen fibrils in the lower FRT facilitates clearance of poor-quality sperm. Our findings suggest that amyloid fibrils in semen may play a role in reproduction by participating in sperm selection and facilitating the rapid removal of sperm antigens.
UR - http://www.scopus.com/inward/record.url?scp=85022319168&partnerID=8YFLogxK
U2 - 10.7554/eLife.24888
DO - 10.7554/eLife.24888
M3 - Article
C2 - 28653619
AN - SCOPUS:85022319168
SN - 2050-084X
VL - 6
JO - eLife
JF - eLife
M1 - e24888
ER -