Boar Seminal Plasma Proteins and Their Binding Properties. A Review

Binding properties of a group of proteins isolated from boar seminal plasma and their role in the fertilization process are discussed. Boar seminal plasma contains different types of proteins: spermadhesins of AQN and AWN family, DQH and PSP proteins belong to the most abundant. Some of these proteins are bound to the sperm surface during ejaculation and thus protein-coating layers are formed. Sperms coated with proteins participate in different types of interactions in the following steps of the fertilization process: formation of oviductal sperm reservoir, sperm capacitation, oocyte recognition and sperm binding. Saccharide-based interactions of boar seminal plasma proteins play role in the binding of sperm to oviductal epithelium, in sperm capacitation and primary binding of sperm to zona pellucida. An interaction with phospholipid components is responsible for the protein adsorption to sperm membrane. Interactions between proteins participate in the arrangement and remodelling of sperm-coating layers. Study of boar seminal plasma proteins, their characterization and elucidation of their interactions will contribute to understanding the fertilization process. A review with 82 references.

Download Full-text

The Ubiquitin-Proteasome System Does Not Regulate the Degradation of Porcine β-Microseminoprotein during Sperm Capacitation

International Journal of Molecular Sciences ◽

10.3390/ijms21114151 ◽

2020 ◽

Vol 21 (11) ◽

pp. 4151

Author(s):

Lucie Tumova ◽

Michal Zigo ◽

Peter Sutovsky ◽

Marketa Sedmikova ◽

Pavla Postlerova

Keyword(s):

Seminal Plasma ◽

Plasma Proteins ◽

Protein Composition ◽

Surface Protein ◽

Ubiquitin Proteasome System ◽

Sperm Capacitation ◽

Sperm Surface ◽

Ubiquitin Proteasome ◽

Seminal Plasma Proteins

Sperm capacitation, one of the key events during successful fertilization, is associated with extensive structural and functional sperm remodeling, beginning with the modification of protein composition within the sperm plasma membrane. The ubiquitin-proteasome system (UPS), a multiprotein complex responsible for protein degradation and turnover, participates in capacitation events. Previous studies showed that capacitation-induced shedding of the seminal plasma proteins such as SPINK2, AQN1, and DQH from the sperm surface is regulated by UPS. Alterations in the sperm surface protein composition also relate to the porcine β-microseminoprotein (MSMB/PSP94), seminal plasma protein known as immunoglobulin-binding factor, and motility inhibitor. MSMB was detected in the acrosomal region as well as the flagellum of ejaculated boar spermatozoa, while the signal disappeared from the acrosomal region after in vitro capacitation (IVC). The involvement of UPS in the MSMB degradation during sperm IVC was studied using proteasomal interference and ubiquitin-activating enzyme (E1) inhibiting conditions by image-based flow cytometry and Western blot detection. Our results showed no accumulation of porcine MSMB either under proteasomal inhibition or under E1 inhibiting conditions. In addition, the immunoprecipitation study did not detect any ubiquitination of sperm MSMB nor was MSMB detected in the affinity-purified fraction containing ubiquitinated sperm proteins. Based on our results, we conclude that UPS does not appear to be the regulatory mechanism in the case of MSMB and opening new questions for further studies. Thus, the capacitation-induced processing of seminal plasma proteins on the sperm surface may be more complex than previously thought, employing multiple proteolytic systems in a non-redundant manner.

Download Full-text

Proteomic analysis of spermatozoa reveals caseins play a pivotal role in preventing short-term periods of subfertility in stallions

Biology of Reproduction ◽

10.1093/biolre/ioab225 ◽

2022 ◽

Author(s):

Róisín Ann Griffin ◽

Aleona Swegen ◽

Mark A Baker ◽

Rachel Ann Ogle ◽

Nathan Smith ◽

...

Keyword(s):

Seminal Plasma ◽

Plasma Proteins ◽

Low Fertility ◽

High Fertility ◽

Short Term ◽

Sperm Binding ◽

Merocyanine 540 ◽

Seminal Plasma Proteins ◽

Assessment Strategies

Abstract Stallions experience transient fluctuations in fertility throughout the breeding season. Considering pregnancy diagnoses cannot be ascertained until ~14 days post-breeding, the timely detection of decreases in stallion fertility would enhance industry economic and welfare outcomes. Therefore, this study aimed to identify the proteomic signatures reflective of short-term fertility fluctuations, and to determine the biological mechanisms governing such differences. Using LC–MS/MS, we compared the proteomic profile of semen samples collected from commercially “fertile” stallions, during high- and low-fertility periods. A total of 1702 proteins were identified, of which, 38 showed a significant change in abundance (p ≤ 0.05). Assessment of intra- and inter-stallion variability revealed that caseins (namely κ-, α-S1-, and α-S2-casein), were significantly more abundant during “high-fertility” periods, while several epididymal, and seminal plasma proteins (chiefly, epididymal sperm binding protein 1 [ELSPbP1], horse seminal plasma protein 1 [HSP-1] and clusterin), were significantly more abundant during “low-fertility” periods. We hypothesised that an increased abundance of caseins offers greater protection from potentially harmful seminal plasma proteins, thereby preserving cell functionality and fertility. In vitro exposure of spermatozoa to casein resulted in decreased levels of lipid scrambling (Merocyanine 540), higher abundance of sperm-bound caseins (α-S1-, α-S2-, and κ-casein), and lower abundance of sperm-bound HSP-1 (p ≤ 0.05). This study demonstrates key pathways governing short-term fertility fluctuations in the stallion, thereby providing a platform to develop robust, fertility assessment strategies into the future.

Download Full-text

Seminal plasma proteins inhibit in vitro- and cooling-induced capacitation in boar spermatozoa

Reproduction Fertility and Development ◽

10.1071/rd09274 ◽

2010 ◽

Vol 22 (6) ◽

pp. 893 ◽

Cited By ~ 27

Author(s):

Melissa L. Vadnais ◽

Kenneth P. Roberts

Keyword(s):

Mass Spectrometry ◽

Seminal Plasma ◽

Plasma Proteins ◽

Acrosome Reaction ◽

Heparin Binding ◽

Total Proteins ◽

Binding Properties ◽

Seminal Plasma Proteins ◽

Boar Spermatozoa

Dilute boar seminal plasma (SP) has been shown to inhibit in vitro capacitation and cooling-induced capacitation-like changes in boar spermatozoa, as assessed by the ability of the spermatozoa to undergo an ionophore-induced acrosome reaction. We hypothesised that the protein component of SP is responsible for this effect. To test this hypothesis, varying concentrations of total SP protein or SP proteins fractionated by heparin binding were assayed for their ability to inhibit in vitro capacitation, as well as cooling- and cryopreservation-induced capacitation-like changes. In vitro capacitation and cooling-induced capacitation-like changes were prevented by 10% whole SP, as well as by total proteins extracted from SP at concentrations greater than 500 μg mL−1. No amount of SP protein was able to prevent cryopreservation-induced capacitation-like changes. Total SP proteins were fractionated based on their heparin-binding properties and the heparin-binding fraction was shown to possess capacitation inhibitory activity at concentrations as low as 250 µg mL−1. The proteins in the heparin-binding fraction were subjected to mass spectrometry and identified. The predominant proteins were three members of the spermadhesin families, namely AQN-3, AQN-1 and AWN, and SP protein pB1. We conclude that one or more of these heparin-binding SP proteins is able to inhibit in vitro capacitation and cooling-induced capacitation-like changes, but not cryopreservation-induced capacitation-like changes, in boar spermatozoa.

Download Full-text