Disulphide bond reduction and S-carboxamidomethylation of PSP94 affects its conformation but not the ability to bind immunoglobulin

Jagtap, Dhanashree D.; Akkaladevi, Narahari; Swamy, Musti J.; Mahale, Smita D.

doi:10.1016/j.bbapap.2007.03.017

Cited by 12 publications

(20 citation statements)

References 26 publications

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“…The protocol followed was as described earlier ( Jagtap et al 2007). Briefly, peptides of the individual proteins with concentration 2 mg each were adsorbed overnight at 4 8C in carbonate buffer (pH 9.0).…”

Section: Peptide Elisamentioning

confidence: 99%

Identification of novel immunodominant epididymal sperm proteins using combinatorial approach

Khan

Suryawanshi²,

Ranpura³

et al. 2009

Reproduction

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Functionally immature spermatozoa leave the testis mature during epididymal transit. This process of maturation involves either addition of new proteins or modification of existing proteins onto the sperm domains that are responsible for domain-specific functions. Epididymal proteins are preferred targets for immunocontraception. In an attempt to identify epididymis-specific sperm proteins, we used a novel combinatorial approach comprising subtractive immunization (SI) followed by proteomics. Following SI, sera of mice were used for immunoproteomics, which led to the identification of 30 proteins, of which four proteins namely sperm head protein 1, sperm flagella protein 2 (SFP2), SFP3, and SFP4 are being reported for the first time on sperm. Another group of four proteins namely collagen a-2 (I) chain precursor, homeodomain-interacting protein kinase 1, GTP-binding protein Rab1, and ubiquinol cytochrome c reductase core protein II although reported earlier in testis are being reported for the first time in epididymal sperm. Furthermore, seven out of these eight novel proteins could be validated using peptide ELISA. These data are a useful repository, which could be exploited to develop targets for post-testicular immunocontraception or biomarkers for infertility diagnosis and management.

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Section: Peptide Elisamentioning

confidence: 99%

Identification of novel immunodominant epididymal sperm proteins using combinatorial approach

Khan

Suryawanshi²,

Ranpura³

et al. 2009

Reproduction

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“…Previous studies by our group and others have shown that PSP94 has the ability to bind to human immunoglobulin [19], [20]. It has been hypothesized that high amounts of PSP94 present in the seminal plasma would bind to immunoglobulin and prevent an immune response to spermatozoa in the female reproductive tract [21].…”

Section: Introductionmentioning

confidence: 97%

Prostate Secretory Protein of 94 Amino Acids (PSP94) Binds to Prostatic Acid Phosphatase (PAP) in Human Seminal Plasma

et al. 2013

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Prostate Secretory Protein of 94 amino acids (PSP94) is one of the major proteins present in the human seminal plasma. Though several functions have been predicted for this protein, its exact role either in sperm function or in prostate pathophysiology has not been clearly defined. Attempts to understand the mechanism of action of PSP94 has led to the search for its probable binding partners. This has resulted in the identification of PSP94 binding proteins in plasma and seminal plasma from human. During the chromatographic separation step of proteins from human seminal plasma by reversed phase HPLC, we had observed that in addition to the main fraction of PSP94, other fractions containing higher molecular weight proteins also showed the presence of detectable amounts of PSP94. This prompted us to hypothesize that PSP94 could be present in the seminal plasma complexed with other protein/s of higher molecular weight. One such fraction containing a major protein of ∼47 kDa, on characterization by mass spectrometric analysis, was identified to be Prostatic Acid Phosphatase (PAP). The ability of PAP present in this fraction to bind to PSP94 was demonstrated by affinity chromatography. Co-immunoprecipitation experiments confirmed the presence of PSP94-PAP complex both in the fraction studied and in the fresh seminal plasma. In silico molecular modeling of the PSP94-PAP complex suggests that β-strands 1 and 6 of PSP94 appear to interact with domain 2 of PAP, while β-strands 7 and 10 with domain 1 of PAP. This is the first report which suggests that PSP94 can bind to PAP and the PAP-bound PSP94 is present in human seminal plasma.

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“…8 The binding of PSP94 to human IgG remains unaffected even when all the five disulfides in PSP94 are reduced, suggesting the involvement of sequential epitopes of PSP94 in IgG binding. 9 Further, our recent results suggest that PSP94 binds to Fab as well as Fab 2 domains and not to the Fc domain of human IgG (to be published). Interestingly, similar binding characteristics have been reported in binding of protein G, a cell surface protein from Streptococcus, with IgG.…”

Section: Psp94-igg Interactionmentioning

confidence: 95%

“…9 Crystals were grown by hanging drop vapor diffusion as reported earlier. 27 Briefly, drops were prepared by mixing 2 μl of protein solution (10 mg ml − 1 in water) with 2 μl reservoir solution [0.1 M sodium acetate, pH 4.5, 0.2 M lithium sulfate, and 44-47% (v/v) PEG 400] and 0.4 ml additive solution (γ-butyrolactone) and equilibrated against 1 ml reservoir solution at 293 K in a sealed well.…”

Section: Methodsmentioning

confidence: 99%

“…7 It was suggested that a high amount of PSP94 present in the human semen might be involved in regulation of immune response in the female reproductive tract against the allogeneic sperm. [7][8][9] PSP94 has also been shown to be a motility inhibitor of sperm 10 and an inhibitor of sperm acrosome reaction. 11 Apart from reproductive tissues, PSP94 has also been detected in several nonreproductive tissues, such as the respiratory and gastric tract tissues, and in both males and females.…”

Section: Introductionmentioning

confidence: 99%

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Crystal Structure of Prostate Secretory Protein PSP94 Shows an Edge-to-Edge Association of two Monomers to Form a Homodimer

Kumar

Jagtap

Mahale

et al. 2010

Journal of Molecular Biology

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Disulphide bond reduction and S-carboxamidomethylation of PSP94 affects its conformation but not the ability to bind immunoglobulin

Cited by 12 publications

References 26 publications

Identification of novel immunodominant epididymal sperm proteins using combinatorial approach

Identification of novel immunodominant epididymal sperm proteins using combinatorial approach

Prostate Secretory Protein of 94 Amino Acids (PSP94) Binds to Prostatic Acid Phosphatase (PAP) in Human Seminal Plasma

Crystal Structure of Prostate Secretory Protein PSP94 Shows an Edge-to-Edge Association of two Monomers to Form a Homodimer

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