Mammalian fertilization: the strange case of sperm protein 56

BioEssays ◽  
2009 ◽  
Vol 31 (2) ◽  
pp. 153-158 ◽  
Author(s):  
Paul M. Wassarman
Keyword(s):  
Sperm Protein ◽  
Mammalian Fertilization

scholarly journals The sperm protein SPACA4 is required for efficient fertilization in mice

2021 ◽  
Author(s):  
Sarah Herberg ◽  
Yoshitaka Fujihara ◽  
Andreas Blaha ◽  
Karin Panser ◽  
Kiyonari Kobayashi ◽  
...  
Keyword(s):  
Zona Pellucida ◽  
Knockout Mice ◽  
Mammalian Species ◽  
Wild Type ◽  
Sperm Protein ◽  
Mammalian Sperm ◽  
Fundamental Process ◽  
Mammalian Fertilization

Fertilization is the fundamental process that initiates the development of a new individual in all sexually reproducing species. Despite its importance, our understanding of the molecular players that govern mammalian sperm-egg interaction is incomplete, partly because many of the essential factors found in non-mammalian species do not have obvious mammalian homologs. We have recently identified the Ly6/uPAR protein Bouncer as a new, essential fertilization factor in zebrafish (Herberg et al., 2018). Here, we show that Bouncer's homolog in mammals, SPACA4, is also required for efficient fertilization in mice. In contrast to fish, where Bouncer is expressed specifically in the egg, SPACA4 is expressed exclusively in the testis. Male knockout mice are severely sub-fertile, and sperm lacking SPACA4 fail to fertilize wild-type eggs in vitro. Interestingly, removal of the zona pellucida rescues the fertilization defect of Spaca4-deficient sperm in vitro, indicating that SPACA4 is not required for the interaction of sperm and the oolemma but rather of sperm and zona pellucida. Our work identifies SPACA4 as an important sperm protein necessary for zona pellucida penetration during mammalian fertilization.

scholarly journals TMEM95 is a sperm membrane protein essential for mammalian fertilization

eLife ◽  
2020 ◽  
Vol 9 ◽  
Author(s):  
Ismael Lamas-Toranzo ◽  
Julieta G Hamze ◽  
Enrica Bianchi ◽  
Beatriz Fernández-Fuertes ◽  
Serafín Pérez-Cerezales ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Membrane Fusion ◽  
Zona Pellucida ◽  
Sperm Protein ◽  
Egg Protein ◽  
Egg Membrane ◽  
Sperm Membrane ◽  
Mammalian Fertilization ◽  
Male Specific ◽  
Mechanical Injection

The fusion of gamete membranes during fertilization is an essential process for sexual reproduction. Despite its importance, only three proteins are known to be indispensable for sperm-egg membrane fusion: the sperm proteins IZUMO1 and SPACA6, and the egg protein JUNO. Here we demonstrate that another sperm protein, TMEM95, is necessary for sperm-egg interaction. TMEM95 ablation in mice caused complete male-specific infertility. Sperm lacking this protein were morphologically normal exhibited normal motility, and could penetrate the zona pellucida and bind to the oolemma. However, once bound to the oolemma, TMEM95-deficient sperm were unable to fuse with the egg membrane or penetrate into the ooplasm, and fertilization could only be achieved by mechanical injection of one sperm into the ooplasm, thereby bypassing membrane fusion. These data demonstrate that TMEM95 is essential for mammalian fertilization.

Purification of P26h: a hamster sperm protein

1996 ◽  
Vol 74 (2) ◽  
pp. 227-231 ◽  
Author(s):  
Louise Coutu ◽  
Pascal Des Rosiers ◽  
Robert Sullivan
Keyword(s):  
Aqueous Phase ◽  
Exchange Chromatography ◽  
Dead Volume ◽  
Total Protein Content ◽  
Two Dimensional Gel Electrophoresis ◽  
Sperm Protein ◽  
Step Procedure ◽  
The Matrix ◽  
Mammalian Fertilization ◽  
Triton X

P26h is a 26 kDa glycoprotein, located on the acrosome cap of hamster spermatozoa, involved in the species specificity of gamete interaction. We have purified this protein from hamster spermatozoa collected from the distal cauda region of the epididymis. Its purification was realized following a three-step procedure: detergent extraction, ion-exchange chromatography, and chromatofocusing. Protein partitioning using Triton X-114 (the first step) showed a ratio of 5:1 between the resulting aqueous and detergent phase. P26h was found almost exclusively in the aqueous phase where it represented about 10–12% of the total protein content. When the desalted aqueous phase was loaded on a carboxymethyl column for cation-exchange chromatography, about 80% of the proteins did not bind to the matrix and were eliminated. P26h was eluted from the column with a linear gradient of salt. At this point, P26h had a rate of purification estimated at 45–55%; three other major proteins of <21, 45, and 63 kDa remained in the sample. These undesired proteins were eliminated by submitting these samples to chromatofocusing using a PBE 94 polybuffer exchanger column. Indeed, P26h was collected almost in the dead volume of the column while the other proteins were eluted much later. Two-dimensional gel electrophoresis and Western blotting were performed to determine the purity of P26h. Only one major spot was detected, confirming the purity of P26h. Usefulness of this purified sperm antigen in the understanding of the physiology of mammalian fertilization is discussed.Key words: sperm protein, epididymis, purification.

scholarly journals The conserved fertility factor SPACA4/Bouncer has divergent modes of action in vertebrate fertilization

2021 ◽  
Vol 118 (39) ◽  
pp. e2108777118
Author(s):  
Yoshitaka Fujihara ◽  
Sarah Herberg ◽  
Andreas Blaha ◽  
Karin Panser ◽  
Kiyonori Kobayashi ◽  
...  
Keyword(s):  
Zona Pellucida ◽  
Wild Type ◽  
Sperm Protein ◽  
Mammalian Sperm ◽  
Type Plasminogen Activator ◽  
Urokinase Type Plasminogen Activator ◽  
Fundamental Process ◽  
Mammalian Fertilization ◽  
Plasminogen Activator Receptor

Fertilization is the fundamental process that initiates the development of a new individual in all sexually reproducing species. Despite its importance, our understanding of the molecular players that govern mammalian sperm–egg interaction is incomplete, partly because many of the essential factors found in nonmammalian species do not have obvious mammalian homologs. We have recently identified the lymphocyte antigen-6 (Ly6)/urokinase-type plasminogen activator receptor (uPAR) protein Bouncer as an essential fertilization factor in zebrafish [S. Herberg, K. R. Gert, A. Schleiffer, A. Pauli, Science 361, 1029–1033 (2018)]. Here, we show that Bouncer’s homolog in mammals, Sperm Acrosome Associated 4 (SPACA4), is also required for efficient fertilization in mice. In contrast to fish, in which Bouncer is expressed specifically in the egg, SPACA4 is expressed exclusively in the sperm. Male knockout mice are severely subfertile, and sperm lacking SPACA4 fail to fertilize wild-type eggs in vitro. Interestingly, removal of the zona pellucida rescues the fertilization defect of Spaca4-deficient sperm in vitro, indicating that SPACA4 is not required for the interaction of sperm and the oolemma but rather of sperm and the zona pellucida. Our work identifies SPACA4 as an important sperm protein necessary for zona pellucida penetration during mammalian fertilization.

scholarly journals Binding of sperm protein Izumo1 and its egg receptor Juno drives Cd9 accumulation in the intercellular contact area prior to fusion during mammalian fertilization

Development ◽  
2014 ◽  
Vol 141 (19) ◽  
pp. 3732-3739 ◽  
Author(s):  
M. Chalbi ◽  
V. Barraud-Lange ◽  
B. Ravaux ◽  
K. Howan ◽  
N. Rodriguez ◽  
...  
Keyword(s):  
Contact Area ◽  
Intercellular Contact ◽  
Sperm Protein ◽  
Mammalian Fertilization

208 Sperm Retention, Storage and Release from the Oviduct: A Story of Sugars, Steroids, and Channels

2021 ◽  
Vol 99 (Supplement_1) ◽  
pp. 113-114
Author(s):  
David J Miller
Keyword(s):  
Reproductive Tract ◽  
Female Reproductive Tract ◽  
Sperm Protein ◽  
Cumulus Oocyte Complex ◽  
Sperm Release ◽  
Normal Increase ◽  
Complex Origin

Abstract Because mating is not always synchronized with ovulation, females from many species store sperm in the female reproductive tract until ovulation and fertilization. This may be done for short periods, a day or two for swine and cattle, or longer periods. Other mammals, such as some species of bats, store sperm for several months. Chickens and turkeys store sperm for 2–4 weeks and queens of some species of insects store sperm for over a decade in specialized structures. How sperm are retained, kept fertile for varying times and released is unclear. We have identified two specific carbohydrate motifs that are abundant in the porcine oviduct that bind and retain sperm in the isthmus. When immobilized, these two glycans lengthen sperm lifespan and suppress the normal increase in intracellular Ca2+ that normally accompanies capacitation. Porcine sperm can be released from oviduct cells and immobilized glycans by progesterone, perhaps of ovarian or cumulus-oocyte complex origin, which activates CatSper, a sperm-specific Ca2+ channel. Progesterone, as well as other compounds that stimulate hyperactivated motility, trigger sperm release, suggesting that hyperactivated motility is sufficient to release porcine sperm from oviduct glycans. We also have found that blocking proteasome-induced sperm protein lysis diminishes the number of sperm released from oviduct glycans. Finally, a transcriptomic approach has identified several groups of genes that are differentially regulated in both bovine and porcine oviducts from estrus animals that are storing sperm compared to oviducts from diestrus animals. This provides clues about how sperm lifespan is extended during storage.

scholarly journals A specific flagellum beating mode for inducing fusion in mammalian fertilization and kinetics of sperm internalization

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Benjamin Ravaux ◽  
Nabil Garroum ◽  
Eric Perez ◽  
Hervé Willaime ◽  
Christine Gourier
Keyword(s):  
Mammalian Fertilization ◽  
Kinetics Of

scholarly journals Localized Depolymerization of the Major Sperm Protein Cytoskeleton Correlates with the Forward Movement of the Cell Body in the Amoeboid Movement of Nematode Sperm

1999 ◽  
Vol 146 (5) ◽  
pp. 1087-1096 ◽  
Author(s):  
Joseph E. Italiano ◽  
Murray Stewart ◽  
Thomas M. Roberts
Keyword(s):  
Cell Body ◽  
Body Movement ◽  
Leading Edge ◽  
Amoeboid Movement ◽  
Major Sperm Protein ◽  
Membrane Protrusion ◽  
Forward Movement ◽  
Sperm Protein ◽  
Amoeboid Motility ◽  
Tightly Coupled

The major sperm protein (MSP)-based amoeboid motility of Ascaris suum sperm requires coordinated lamellipodial protrusion and cell body retraction. In these cells, protrusion and retraction are tightly coupled to the assembly and disassembly of the cytoskeleton at opposite ends of the lamellipodium. Although polymerization along the leading edge appears to drive protrusion, the behavior of sperm tethered to the substrate showed that an additional force is required to pull the cell body forward. To examine the mechanism of cell body movement, we used pH to uncouple cytoskeletal polymerization and depolymerization. In sperm treated with pH 6.75 buffer, protrusion of the leading edge slowed dramatically while both cytoskeletal disassembly at the base of the lamellipodium and cell body retraction continued. At pH 6.35, the cytoskeleton pulled away from the leading edge and receded through the lamellipodium as its disassembly at the cell body continued. The cytoskeleton disassembled rapidly and completely in cells treated at pH 5.5, but reformed when the cells were washed with physiological buffer. Cytoskeletal reassembly occurred at the lamellipodial margin and caused membrane protrusion, but the cell body did not move until the cytoskeleton was rebuilt and depolymerization resumed. These results indicate that cell body retraction is mediated by tension in the cytoskeleton, correlated with MSP depolymerization at the base of the lamellipodium.

Sign in / Sign up

Export Citation Format

Share Document