A major IgE epitope-containing grass pollen allergen domain from Phl p 5 folds as a four-helix bundle(623 views) Maglio O, Saldanha JW, Vrtala S, Spitzauer S, Valenta R, Pastore A
Protein Eng (ISSN: 0269-2139print, 0269-2139linking), 2002 Aug; 15(8): 635-642.
NIMR, The Ridgeway, Mill Hill, London NW7 1AA, UK.,
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A major IgE epitope-containing grass pollen allergen domain from Phl p 5 folds as a four-helix bundle
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 unknown. 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.
A major IgE epitope-containing grass pollen allergen domain from Phl p 5 folds as a four-helix bundle
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A major IgE epitope-containing grass pollen allergen domain from Phl p 5 folds as a four-helix bundle
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