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Gene Review

AWN  -  sperm associated AWN protein

Sus scrofa

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High impact information on AWN

  • Binding of ejaculated sperm to oviductal epithelium was inhibited by addition of AQN1 but not by AWN [1].
  • AQN1 showed a broad carbohydrate-binding pattern as it recognizes both alpha- and beta-linked galactose as well as Manalpha1-3(Manalpha1-6)Man structures, whereas AWN bound only the galactose species [1].
  • Clusters of AWN epitopes were occasionally found attached to the epithelium of the uterotubal junction and the adjacent lower isthmus [2].
  • In addition, the complete amino acid sequence of spermadhesin AWN was synthesized as overlapping peptides, and their ability to bind to a heparin-Sepharose column and to inhibit the interaction of soluble heparin with purified ELISA plate-coated AWN was tested [3].
  • Both approaches gave similar results and as a whole showed that different regions of AWN may converge in its tertiary structure to form a composite heparin-binding site [3].

Biological context of AWN


Anatomical context of AWN

  • Remarkably, AWN is the only spermadhesin that is also expressed in the uterus, the uterotubal junction, and the oviduct of the female genital tract as shown by RT-PCR, cDNA-sequencing, and immunological analysis [5].
  • Boar spermadhesins AQN-1, AQN-3 and AWN form a recently described protein family, synthesized by the sexual accessory glands, and become associated with the sperm head upon ejaculation [6].
  • The complete primary structure of the spermadhesin AWN, a zona pellucida-binding protein isolated from boar spermatozoa [7].
  • The strongest interaction was observed between biotinylated glycoproteins of porcine zona pellucida and AWN 1-containing aggregates and separated proteins [4].
  • Spermadhesins of the AQN and AWN families, DQH sperm surface protein and HNK protein in the heparin-binding fraction of boar seminal plasma [8].

Associations of AWN with chemical compounds


Other interactions of AWN

  • During sperm passage through the epididymis AQN-3 and AWN have been shown to bind tightly to the sperm surface by interaction with the phospholipids of the membrane bilayer [10].
  • HPLC analysis and N-terminal sequencing used to characterize the composition of the protein fractions obtained by gel chromatography revealed that all consisted of low (12-16 kDa) molecular weight components: the H+ fraction consisted of DQH sperm protein, AQN and AWN spermadhesins whereas the H- fraction consisted of PSPI and PSPII spermadhesins [11].
  • Boar spermadhesins AQN-1 and AWN are sperm-associated acrosin inhibitor acceptor proteins [12].
  • Biotinylated aggregates containing AWN, AQN, DQH, and PSP proteins (fractions I-IV) bound stronger to boar epididymal spermatozoa than to ejaculated spermatozoa [4].
  • Therefore, basic protein BHB-2 belongs to a new family of DQH sperm surface proteins that are homologous to the acidic proteins from bull and stallion seminal plasma, to the collagen binding domain II in fibronectin and to the leucocyte cell-cell adhesion regulator, but are not homologous to AQN or AWN spermadhesins [8].

Analytical, diagnostic and therapeutic context of AWN


  1. Spermadhesin AQN1 is a candidate receptor molecule involved in the formation of the oviductal sperm reservoir in the pig. Ekhlasi-Hundrieser, M., Gohr, K., Wagner, A., Tsolova, M., Petrunkina, A., Töpfer-Petersen, E. Biol. Reprod. (2005) [Pubmed]
  2. Monoclonal antibodies against boar sperm zona pellucida-binding protein AWN-1. Characterization of a continuous antigenic determinant and immunolocalization of AWN epitopes in inseminated sows. Calvete, J.J., Ensslin, M., Mburu, J., Iborra, A., Martínez, P., Adermann, K., Waberski, D., Sanz, L., Töpfer-Petersen, E., Weitze, K.F., Einarsson, S., Rodríguez-Martínez, H. Biol. Reprod. (1997) [Pubmed]
  3. Mapping the heparin-binding domain of boar spermadhesins. Calvete, J.J., Dostàlova, Z., Sanz, L., Adermann, K., Thole, H.H., Töpfer-Petersen, E. FEBS Lett. (1996) [Pubmed]
  4. Sperm surface proteins in mammalian fertilization. Jonáková, V., Manásková, P., Kraus, M., Liberda, J., Tichá, M. Mol. Reprod. Dev. (2000) [Pubmed]
  5. 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]
  6. 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]
  7. The complete primary structure of the spermadhesin AWN, a zona pellucida-binding protein isolated from boar spermatozoa. Sanz, L., Calvete, J.J., Mann, K., Schäfer, W., Schmid, E.R., Amselgruber, W., Sinowatz, F., Ehrhard, M., Töpfer-Petersen, E. FEBS Lett. (1992) [Pubmed]
  8. Spermadhesins of the AQN and AWN families, DQH sperm surface protein and HNK protein in the heparin-binding fraction of boar seminal plasma. Jonáková, V., Kraus, M., Veselský, L., Cechová, D., Bezouska, K., Tichá, M. J. Reprod. Fertil. (1998) [Pubmed]
  9. Identification by affinity chromatography of boar sperm membrane-associated proteins bound to immobilized porcine zona pellucida. Mapping of the phosphorylethanolamine-binding region of spermadhesin AWN. Ensslin, M., Calvete, J.J., Thole, H.H., Sierralta, W.D., Adermann, K., Sanz, L., Töpfer-Petersen, E. Biol. Chem. Hoppe-Seyler (1995) [Pubmed]
  10. Spermadhesins: a new protein family. Facts, hypotheses and perspectives. Töpfer-Petersen, E., Romero, A., Varela, P.F., Ekhlasi-Hundrieser, M., Dostàlovà, Z., Sanz, L., Calvete, J.J. Andrologia (1998) [Pubmed]
  11. Aggregated forms of heparin-binding and non-heparin-binding proteins of boar seminal plasma and their binding properties. Manásková, P., Mészárosová, A., Liberda, J., Voburka, Z., Tichá, M., Jonáková, V. Folia Biol. (Praha) (1999) [Pubmed]
  12. Boar spermadhesins AQN-1 and AWN are sperm-associated acrosin inhibitor acceptor proteins. Sanz, L., Calvete, J.J., Jonáková, V., Töpfer-Petersen, E. FEBS Lett. (1992) [Pubmed]
  13. Quantitation of boar spermadhesins in accessory sex gland fluids and on the surface of epididymal, ejaculated and capacitated spermatozoa. Dostàlovà, Z., Calvete, J.J., Sanz, L., Töpfer-Petersen, E. Biochim. Biophys. Acta (1994) [Pubmed]
  14. Immunohistochemical localization of spermadhesin AWN in the porcine male genital tract. Sinowatz, F., Amselgruber, W., Töpfer-Petersen, E., Calvete, J.J., Sanz, L., Plendl, J. Cell Tissue Res. (1995) [Pubmed]
  15. Immunohistochemical localization in the stallion genital tract, and topography on spermatozoa of seminal plasma protein SSP-7, a member of the spermadhesin protein family. Reinert, M., Calvete, J.J., Sanz, L., Töpfer-Petersen, E. Andrologia (1997) [Pubmed]
  16. Only low levels of spermadhesin AWN are detectable on the surface of live ejaculated boar spermatozoa. Petrunkina, A.M., Harrison, R.A., Töpfer-Petersen, E. Reprod. Fertil. Dev. (2000) [Pubmed]
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