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The complete primary structure of the spermadhesin AWN, a zona pellucida-binding protein isolated from boar spermatozoa.

FEBS Lett.1992 Apr 06;300(3):213-8
L Sanz 1 , J J Calvete , K Mann , W Schäfer , E R Schmid , W Amselgruber , F Sinowatz , M Ehrhard , E Töpfer-Petersen
L Sanz 1 , J J Calvete , K Mann , W Schäfer , E R Schmid , W Amselgruber , F Sinowatz , M Ehrhard , E Töpfer-Petersen
+ et al

[No authors listed]

Author information
  • 1 Dermatologische Klinik, Andrology Unit, München, Germany.

摘要


AWN is a boar protein which originates in secretions of the male accessory glands and which becomes sperm surface-associated upon ejaculation. It is one of the components thought to mediate sperm adhesion to the egg's zona pellucida through a carbohydrate-recognition mechanism. AWN may, thus, participate in the initial events of fertilization in the pig. In this report we describe its complete primary structure by combination of protein-chemical and mass spectrometric methods. AWN exists as two isoforms, AWN-1 and AWN-2, which differ in that AWN-2 is N-terminally acetylated. The amino acid sequence of AWN contains 133 amino acid residues and two disulphide bridges between nearest-neighbour cysteine residues. Analysis of the amino acid sequence of the AWN proteins showed significant similarity only to AQN-1 and AQN-3, two other boar spermadhesins.