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Phosphatidylserine on viable sperm and phagocytic machinery in oocytes regulate mammalian fertilization

Fertilization is essential for species survival. Although Izumo1 and Juno are critical for initial interaction between gametes, additional molecules necessary for sperm:egg fusion on both the sperm and the oocyte remain to be defined. Here, we show that phosphatidylserine (PtdSer) is exposed on the...

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Autores principales: Rival, Claudia M., Xu, Wenhao, Shankman, Laura S., Morioka, Sho, Arandjelovic, Sanja, Lee, Chang Sup, Wheeler, Karen M., Smith, Ryan P., Haney, Lisa B., Isakson, Brant E., Purcell, Scott, Lysiak, Jeffrey J., Ravichandran, Kodi S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6773685/
https://www.ncbi.nlm.nih.gov/pubmed/31575859
http://dx.doi.org/10.1038/s41467-019-12406-z
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author Rival, Claudia M.
Xu, Wenhao
Shankman, Laura S.
Morioka, Sho
Arandjelovic, Sanja
Lee, Chang Sup
Wheeler, Karen M.
Smith, Ryan P.
Haney, Lisa B.
Isakson, Brant E.
Purcell, Scott
Lysiak, Jeffrey J.
Ravichandran, Kodi S.
author_facet Rival, Claudia M.
Xu, Wenhao
Shankman, Laura S.
Morioka, Sho
Arandjelovic, Sanja
Lee, Chang Sup
Wheeler, Karen M.
Smith, Ryan P.
Haney, Lisa B.
Isakson, Brant E.
Purcell, Scott
Lysiak, Jeffrey J.
Ravichandran, Kodi S.
author_sort Rival, Claudia M.
collection PubMed
description Fertilization is essential for species survival. Although Izumo1 and Juno are critical for initial interaction between gametes, additional molecules necessary for sperm:egg fusion on both the sperm and the oocyte remain to be defined. Here, we show that phosphatidylserine (PtdSer) is exposed on the head region of viable and motile sperm, with PtdSer exposure progressively increasing during sperm transit through the epididymis. Functionally, masking phosphatidylserine on sperm via three different approaches inhibits fertilization. On the oocyte, phosphatidylserine recognition receptors BAI1, CD36, Tim-4, and Mer-TK contribute to fertilization. Further, oocytes lacking the cytoplasmic ELMO1, or functional disruption of RAC1 (both of which signal downstream of BAI1/BAI3), also affect sperm entry into oocytes. Intriguingly, mammalian sperm could fuse with skeletal myoblasts, requiring PtdSer on sperm and BAI1/3, ELMO2, RAC1 in myoblasts. Collectively, these data identify phosphatidylserine on viable sperm and PtdSer recognition receptors on oocytes as key players in sperm:egg fusion.
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spelling pubmed-67736852019-10-03 Phosphatidylserine on viable sperm and phagocytic machinery in oocytes regulate mammalian fertilization Rival, Claudia M. Xu, Wenhao Shankman, Laura S. Morioka, Sho Arandjelovic, Sanja Lee, Chang Sup Wheeler, Karen M. Smith, Ryan P. Haney, Lisa B. Isakson, Brant E. Purcell, Scott Lysiak, Jeffrey J. Ravichandran, Kodi S. Nat Commun Article Fertilization is essential for species survival. Although Izumo1 and Juno are critical for initial interaction between gametes, additional molecules necessary for sperm:egg fusion on both the sperm and the oocyte remain to be defined. Here, we show that phosphatidylserine (PtdSer) is exposed on the head region of viable and motile sperm, with PtdSer exposure progressively increasing during sperm transit through the epididymis. Functionally, masking phosphatidylserine on sperm via three different approaches inhibits fertilization. On the oocyte, phosphatidylserine recognition receptors BAI1, CD36, Tim-4, and Mer-TK contribute to fertilization. Further, oocytes lacking the cytoplasmic ELMO1, or functional disruption of RAC1 (both of which signal downstream of BAI1/BAI3), also affect sperm entry into oocytes. Intriguingly, mammalian sperm could fuse with skeletal myoblasts, requiring PtdSer on sperm and BAI1/3, ELMO2, RAC1 in myoblasts. Collectively, these data identify phosphatidylserine on viable sperm and PtdSer recognition receptors on oocytes as key players in sperm:egg fusion. Nature Publishing Group UK 2019-10-01 /pmc/articles/PMC6773685/ /pubmed/31575859 http://dx.doi.org/10.1038/s41467-019-12406-z Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Rival, Claudia M.
Xu, Wenhao
Shankman, Laura S.
Morioka, Sho
Arandjelovic, Sanja
Lee, Chang Sup
Wheeler, Karen M.
Smith, Ryan P.
Haney, Lisa B.
Isakson, Brant E.
Purcell, Scott
Lysiak, Jeffrey J.
Ravichandran, Kodi S.
Phosphatidylserine on viable sperm and phagocytic machinery in oocytes regulate mammalian fertilization
title Phosphatidylserine on viable sperm and phagocytic machinery in oocytes regulate mammalian fertilization
title_full Phosphatidylserine on viable sperm and phagocytic machinery in oocytes regulate mammalian fertilization
title_fullStr Phosphatidylserine on viable sperm and phagocytic machinery in oocytes regulate mammalian fertilization
title_full_unstemmed Phosphatidylserine on viable sperm and phagocytic machinery in oocytes regulate mammalian fertilization
title_short Phosphatidylserine on viable sperm and phagocytic machinery in oocytes regulate mammalian fertilization
title_sort phosphatidylserine on viable sperm and phagocytic machinery in oocytes regulate mammalian fertilization
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6773685/
https://www.ncbi.nlm.nih.gov/pubmed/31575859
http://dx.doi.org/10.1038/s41467-019-12406-z
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