Evolution and function of mammalian binder of sperm proteins

Plante, Gérard E.; Prud’homme, Bruno; Fan, Jinjiang; Lafleur, Michel; Manjunath, Puttaswamy

doi:10.1007/s00441-015-2289-2

Cited by 70 publications

(72 citation statements)

References 182 publications

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“…Gelatin has been characterized as a ligand for proteins present in the seminal fluids of many mammals, which are called GBPs [5]. Although, no known biological function of gelatin and GBPs interactions has been reported so far, gelatin has been used to purify GBPs from different sources such as seminal plasma, seminal vesicles and sperm in different mammals [5].…”

Section: Gelatinmentioning

confidence: 99%

“…Although, no known biological function of gelatin and GBPs interactions has been reported so far, gelatin has been used to purify GBPs from different sources such as seminal plasma, seminal vesicles and sperm in different mammals [5]. In best of my knowledge, it is also not clear that whether gelatin is naturally present in seminal plasma or is liberated from collagen.…”

Section: Gelatinmentioning

confidence: 99%

“…Various studies have revealed that BSP proteins can be purified and characterized using gelatin agarose column chromatography from a number of sources such as seminal plasma and seminal vesicles in different mammals including the bull, stallion, goat, buffalo, boar, ram and bison [5,7]. BSP homologue genes (BSPH4, BSPH5 and BSPH6) have been recognized in the bovine model [7].…”

Section: Gelatin Binding Proteins (Gbps) Bsp Proteins and Their Homologsmentioning

confidence: 99%

“…Some of BSP proteins (especially epididymal in origin) contain also small variable carboxyl terminal end. Typically, in BSP proteins each fn2 domain contains eight cysteine residues, which make four disulphide bonds, two in each domain [5,7,11,28] (Fig. 2a).…”

Section: Gelatin Binding Domainmentioning

confidence: 99%

“…Amongst the proteins found in seminal plasma, gelatin binding proteins (GBPs) are a highly conserved group and have been thoroughly explored in various mammal species over the past few decades [5]. In the present review we detail the current available literatures on GBPs in relation to their biological functions, particularly with respect to reproductive physiology.…”

Section: Introductionmentioning

confidence: 99%

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Gelatin Binding Proteins in Reproductive Physiology

Kumar¹,

Tinson²,

Mulligan³

et al. 2016

Indian J Microbiol

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In order to advance the assisted reproductive technologies used in animals and human beings, it is important to accumulate basic informations about underlying molecular mechanisms that shape the biological processes of reproduction. From within seminal plasma, proteins perform a wide variety of distinct functions that regulate major reproductive events such as fertilization. The ability of such proteins to bind and interact with different antagonistic ions and biomolecules such as polysaccharides, lipids, and other proteins present in the male and female reproductive tract define these capabilities. Over the last two decades, extensive work has been undertaken in an attempt to define the role of seminal plasma proteins, of which, Gelatin binding proteins (GBPs) represent a large family. GBPs comprise of known group of Bovine seminal plasma (BSP) protein family, matrix metallo proteinases (MMP 2 and MMP 9) and fibronectin, which have been widely studied. The presence of a type II repeat is a characteristic feature of GBPs, which is similar in structure to the fibronectin type II domain (fn2), which has ability to bind multiple ligands including gelatin, glycosaminoglycans, choline phospholipids, and lipoproteins. Two fn2 domains are present within the BSP protein family, while, three fn2 domains are found in gelatinases (MMP-2 and MMP9), and ELSPBP1 (Epididymosomes Transfer Epididymal Sperm Binding Protein 1) contains four long fn2 domains. For the most part BSP proteins are exclusively expressed in seminal vesicles although mBSPH1, mBSPH2 and hBSPH1 are all expressed in the epididymis. The expression of gelatinases has been demonstrated in several organs and tissues such as the prostate, testis, epididymis, ovary, human placenta, cervix and endometrial wall. This review intends to bring current updates on the role of GBPs in reproductive physiology to light, which may act as basis for future studies on GBPs.

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Section: Gelatinmentioning

confidence: 99%

Section: Gelatinmentioning

confidence: 99%

Section: Gelatin Binding Proteins (Gbps) Bsp Proteins and Their Homologsmentioning

confidence: 99%

Section: Gelatin Binding Domainmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Gelatin Binding Proteins in Reproductive Physiology

Kumar¹,

Tinson²,

Mulligan³

et al. 2016

Indian J Microbiol

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Novel affinity chromatography method for the efficient purification of recombinant Binder of SPerm homolog proteins

Zarafshan

Manjunath

2020

J of Separation Science

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In mammalian species, a family of proteins named the Binder of SPerm proteins, which are expressed in the male reproductive tract, have been shown to play a role in epididymal sperm maturation and sperm capacitation. Recently, one homolog from human and two homologs from mouse were characterized. In order to further investigate the biochemical activity of these proteins, efficient purification procedures are required to isolate the proteins. Since these proteins are produced in very minute quantities, we exploited the high capacity of Escherichia coli to produce larger quantities of recombinant proteins that were subsequently purified using affinity chromatography on a diethylaminoethyl‐Sephadex A‐25 column. Binder of SPerm proteins have been shown to interact with pseudo‐choline groups such as diethylaminoethyl through affinity rather than ionic interactions. The aim of the current study was to develop a novel method for purifying these recombinant proteins, produced in Escherichia coli cells. Diethylaminoethyl is positively charged and is a weak anion exchanger, but binder of sperm proteins interacts with affinity to this resin. This study presents a new, rapid, and cost‐effective purification method that provides with an exceptional purity level, which can be used to study their roles in mammalian fertilization.

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CRISPR–Cas9‐mediated mutation revealed BSPH2 protein is dispensable for male fertility

Eskandari-Shahraki

Prud’homme

Manjunath

2018

Molecular Reproduction Devel

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Members of the Binder of SPerm (BSP) superfamily have been identified in both human and mouse epididymis. These proteins are known to bind sperm membrane and promote sperm capacitation. Studies suggest that BSPH2 might play a different role in sperm functions from its counterparts; however, the role of BSPH2 remains mainly unexplored. To investigate whether the absence of one member of the BSP family could affect fertility, mice lacking Bsph2 expression were generated using clustered regularly interspaced short palindromic repeats (CRISPR) associated 9 (Cas9) technology. Knockout (KO) male mice were mated with wild-type (WT) females, and the number and weight of the pups were determined. Sperm motility in WT and KO was assessed using sperm class analyzer (SCA). Liquid chromatography tandem mass spectrometry (LC-MS/MS) was used for protein identification. Fertility analysis of null Bsph2 mice did not reveal any phenotype. No differences were noticed on average litter size or average pup weight. Normal testis weight and morphology were observed in Bsph2 and Bsph2 compared to the WT. Quantitative polymerase chain reaction analyses revealed that Bsph1 messenger RNA expression was increased in mutant mice, whereas LC-MS/MS analysis displayed no increase in protein expression level. Taken together, we show the existence of redundant function for murine BSPH2 and the lack of BSPH2 itself does not lead to sterility.

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Evolution and function of mammalian binder of sperm proteins

Cited by 70 publications

References 182 publications

Gelatin Binding Proteins in Reproductive Physiology

Gelatin Binding Proteins in Reproductive Physiology

Novel affinity chromatography method for the efficient purification of recombinant Binder of SPerm homolog proteins

CRISPR–Cas9‐mediated mutation revealed BSPH2 protein is dispensable for male fertility

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