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Gene Review

PSP-I  -  porcine seminal protein I

Sus scrofa

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High impact information on PSP-I

  • We report the crystal structures of porcine seminal plasma PSP-I/PSP-II, a heterodimer of two glycosylated spermadhesins, and bovine aSFP at 2.4 A and 1.9 A resolution respectively [1].
  • The crystal structure of porcine seminal plasma spermadhesin PSP-I/PSP-II heterodimer has been determined in two crystal forms by multiple isomorphous replacement in an hexagonal crystal (space group P6(1)22) and molecular replacement in a trigonal crystal of space group P3(2)21 [2].
  • Only the innermost N-acetylglucosamine of PSP-I is defined in the crystal structure [2].
  • Thus, the modulation of the structural organization and heparin-binding ability of PSP-I by Zn2+ might be a physiological phenomenon in seminal plasma [3].
  • Moreover, the viability, motility, and mitochondrial activity all decreased on incubation of spermatozoa with mixtures of PSP-I/PSP-II and heparin-binding spermadhesins as the concentration of the latter increased [4].

Biological context of PSP-I


Anatomical context of PSP-I


Associations of PSP-I with chemical compounds


Physical interactions of PSP-I

  • The complex of porcine seminal plasma heterodimers I and II (PSP-I/PSP-II), which are heterodimers of glycosylated spermadhesins, is the major component of porcine seminal fluid [12].
  • PSP-I was found to bind a number of proteins including endo-beta-galactosidase digested ZP3, soybean trypsin inhibitor, IgA, IgG and alpha-casein, indicating that it may have multiple functions [14].

Other interactions of PSP-I


Analytical, diagnostic and therapeutic context of PSP-I


  1. The crystal structures of two spermadhesins reveal the CUB domain fold. Romero, A., Romão, M.J., Varela, P.F., Kölln, I., Dias, J.M., Carvalho, A.L., Sanz, L., Töpfer-Petersen, E., Calvete, J.J. Nat. Struct. Biol. (1997) [Pubmed]
  2. The 2.4 A resolution crystal structure of boar seminal plasma PSP-I/PSP-II: a zona pellucida-binding glycoprotein heterodimer of the spermadhesin family built by a CUB domain architecture. Varela, P.F., Romero, A., Sanz, L., Romão, M.J., Töpfer-Petersen, E., Calvete, J.J. J. Mol. Biol. (1997) [Pubmed]
  3. Zinc ions induce the unfolding and self-association of boar spermadhesin PSP-I, a protein with a single CUB domain architecture, and promote its binding to heparin. Campanero-Rhodes, M.A., Menéndez, M., Saiz, J.L., Sanz, L., Calvete, J.J., Solís, D. Biochemistry (2006) [Pubmed]
  4. Influence of porcine spermadhesins on the susceptibility of boar spermatozoa to high dilution. Centurion, F., Vazquez, J.M., Calvete, J.J., Roca, J., Sanz, L., Parrilla, I., Garcia, E.M., Martinez, E.A. Biol. Reprod. (2003) [Pubmed]
  5. Molecular cloning and sequence analysis of two porcine seminal proteins, PSP-I and PSP-II: new members of the spermadhesin family. Kwok, S.C., Yang, D., Dai, G., Soares, M.J., Chen, S., McMurtry, J.P. DNA Cell Biol. (1993) [Pubmed]
  6. Purified porcine seminal plasma protein enhances in vitro immune activities of porcine peripheral lymphocytes. Yang, W.C., Kwok, S.C., Leshin, S., Bollo, E., Li, W.I. Biol. Reprod. (1998) [Pubmed]
  7. Boar spermadhesin PSP-II: location of posttranslational modifications, heterodimer formation with PSP-I glycoforms and effect of dimerization on the ligand-binding capabilities of the subunits. Calvete, J.J., Mann, K., Schäfer, W., Raida, M., Sanz, L., Töpfer-Petersen, E. FEBS Lett. (1995) [Pubmed]
  8. Purification and characterization of PSP-I and PSP-II, two major proteins from porcine seminal plasma. Rutherfurd, K.J., Swiderek, K.M., Green, C.B., Chen, S., Shively, J.E., Kwok, S.C. Arch. Biochem. Biophys. (1992) [Pubmed]
  9. Characterization of two glycosylated boar spermadhesins. Calvete, J.J., Solís, D., Sanz, L., Díaz-Mauriño, T., Schäfer, W., Mann, K., Töpfer-Petersen, E. Eur. J. Biochem. (1993) [Pubmed]
  10. Does seminal plasma PSP-I/PSP-II spermadhesin modulate the ability of boar spermatozoa to penetrate homologous oocytes in vitro? Caballero, I., Vazquez, J.M., Gil, M.A., Calvete, J.J., Roca, J., Sanz, L., Parrilla, I., Garcia, E.M., Rodriguez-Martinez, H., Martinez, E.A. J. Androl. (2004) [Pubmed]
  11. Expression of spermadhesin genes in porcine male and female reproductive tracts. Ekhlasi-Hundrieser, M., Sinowatz, F., Greiser De Wilke, I., Waberski, D., Töpfer-Petersen, E. Mol. Reprod. Dev. (2002) [Pubmed]
  12. Porcine spermadhesin PSP-I/PSP-II stimulates macrophages to release a neutrophil chemotactic substance: modulation by mast cells. Assreuy, A.M., Alencar, N.M., Cavada, B.S., Rocha-Filho, D.R., Feitosa, R.F., Cunha, F.Q., Calvete, J.J., Ribeiro, R.A. Biol. Reprod. (2003) [Pubmed]
  13. Binding of mannose-6-phosphate and heparin by boar seminal plasma PSP-II, a member of the spermadhesin protein family. Solís, D., Romero, A., Jiménez, M., Díaz-Mauriño, T., Calvete, J.J. FEBS Lett. (1998) [Pubmed]
  14. Binding characteristics and immunolocalization of porcine seminal protein, PSP-I. Kwok, S.C., Soares, M.J., McMurtry, J.P., Yurewicz, E.C. Mol. Reprod. Dev. (1993) [Pubmed]
  15. Crystallization and preliminary X-ray diffraction analysis of boar seminal plasma spermadhesin PSP-I/PSP-II, a heterodimer of two CUB domains. Romero, A., Varela, P.F., Sanz, L., Töpfer-Petersen, E., Calvete, J.J. FEBS Lett. (1996) [Pubmed]
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