Recombinant allergen Lol p II: Expression, purification and characterization

Elena Tamborini, Anna Brandazza, Claudia De Lalla, Giovanna Musco, Antonio G. Siccardi, Paolo Arosio, Alessandro Sidoli

Research output: Contribution to journalArticlepeer-review


Pollen from perennial rye grass (Lolium perenne) is a major cause of type I allergies worldwide. It contains complex mixtures of proteins, among which Lol p II is a major allergen. Previously, we have reported the cloning and sequencing of Lol p II and its expression in fusion with the heavy chain of human ferritin as carrier polypeptide (Sidoli et al. 1993, J. biol. Chem. 268, 21819-21825.). Here, we describe the expression, purification and characterization of a recombinant Lol p II overproduced as a non-fusion protein in the periplasm of E. coli. The recombinant allergen was expressed in high yields and was easily purified in milligram amounts. It competed with the natural Lol p II for binding to specific IgE, and it induced allergic responses in skin prick tests, indicating to be immunologically analogous to the natural protein. Biochemical analyses indicate that recombinant Lol p II is a highly stable and soluble monomeric molecule which behaves like a small globular protein.

Original languageEnglish
Pages (from-to)505-513
Number of pages9
JournalMolecular Immunology
Issue number7
Publication statusPublished - 1995


  • allergens
  • IgE
  • perennial rye grass
  • recombinant proteins

ASJC Scopus subject areas

  • Molecular Biology
  • Immunology


Dive into the research topics of 'Recombinant allergen Lol p II: Expression, purification and characterization'. Together they form a unique fingerprint.

Cite this