Structural basis of antigen recognition: crystal structure of duck egg lysozyme

Acta Crystallogr D Struct Biol. 2017 Nov 1;73(Pt 11):910-920. doi: 10.1107/S2059798317013730. Epub 2017 Oct 25.

Abstract

Duck egg lysozyme (DEL) is a widely used model antigen owing to its capacity to bind with differential affinity to anti-chicken egg lysozyme antibodies. However, no structures of DEL have so far been reported, and the situation had been complicated by the presence of multiple isoforms and conflicting reports of primary sequence. Here, the structures of two DEL isoforms from the eggs of the commonly used Pekin duck (Anas platyrhynchos) are reported. Using structural analyses in combination with mass spectrometry, non-ambiguous DEL primary sequences are reported. Furthermore, the structures and sequences determined here enable rationalization of the binding affinity of DEL for well documented landmark anti-lysozyme antibodies.

Keywords: antigen recognition; duck egg lysozyme; glycosyl hydrolase; hen egg lysozyme.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antigen Presentation*
  • Avian Proteins / chemistry*
  • Crystallization
  • Crystallography, X-Ray
  • Ducks*
  • Egg Proteins / chemistry*
  • Egg White / chemistry
  • Models, Molecular
  • Muramidase / chemistry*
  • Protein Conformation
  • Sequence Homology

Substances

  • Avian Proteins
  • Egg Proteins
  • Muramidase