Bacterially expressed and optimized recombinant Phl p 1 is immunobiochemically equivalent to natural Phl p 1

Biochim Biophys Acta. 2006 Nov;1764(11):1701-9. doi: 10.1016/j.bbapap.2006.09.015. Epub 2006 Sep 30.


Recombinant production in bacteria of soluble and monomeric Phl p 1, a major allergen of Timothy grass pollen, has proved to be very problematic. In order to facilitate expression and purification of this allergen, a recombinant variant was designed with a single amino acid substitution. Several comparative analyses with natural counterparts using electrophoretic and HPLC separations, together with immunological assays, demonstrated high equivalence. This is the first description of an approach aiming at an improvement of a natural like recombinant allergen.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Allergens / chemistry
  • Allergens / genetics
  • Allergens / metabolism*
  • Amino Acid Sequence
  • Chromatography, High Pressure Liquid
  • Circular Dichroism
  • Electrophoresis, Polyacrylamide Gel
  • Immunohistochemistry
  • Molecular Sequence Data
  • Molecular Weight
  • Peptide Mapping
  • Plant Proteins / chemistry
  • Plant Proteins / genetics
  • Plant Proteins / metabolism*
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Sequence Homology, Amino Acid


  • Allergens
  • Plant Proteins
  • Recombinant Proteins
  • PHLPI protein, Phleum pratense