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Protein Engineering, Vol. 15, No. 8, 635-642, August 2002
© 2002 Oxford University Press

A major IgE epitope-containing grass pollen allergen domain from Phl p 5 folds as a four-helix bundle

Ornella Maglio1,2, Jose W. Saldanha1, Susanne Vrtala3, Susanne Spitzauer4, Rudolf Valenta3 and Annalisa Pastore1,5

1 NIMR, The Ridgeway, Mill Hill, London NW7 1AA, UK, 2 Department of Chemistry, University of Napoli Federico II, Via Cynthia, I-80134 Naples, Italy, 3 Department of Pathophysiology, Vienna General Hospital. Vienna and 4 Clinical Institute for Medical and Chemical Laboratory Diagnostics, Vienna, Austria

Phl p 5, a 29 kDa major allergen from timothy grass pollen, is one of the most reactive members of group 5 allergens. Its sequence comprises two repeats of a novel alanine-rich motif (AR) whose structure and allergenic response are still mostly unkown. We report here a structural characterization of an immunodominant fragment of Phl p 5, Phl p 5(56–165) which comprises the first AR repeat. Recombinant (r)Phl p 5(56–165) was expressed in Escherichia coli, purified to homogeneity and shown to be sufficient to react with serum IgE from 90% of grass pollen allergic patients. Using NMR spectroscopy, we show conclusively that the fragment forms a compact globular domain which is, however, prone to degradation with time. The rPhl p 5(56–165) fold consists of a four-helix bundle held together by hydrophobic interactions between the aromatic rings and aliphatic side chains. This evidence gives clear indications about the structure of the full-length Phl p 5 and provides a rational basis for finding ways to stabilize the fold and designing therapeutic vaccines against grass pollen allergy.


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