Haptenic Side Chains as Posttranslational IgE-Binding Determinants among Pollen Protein Allergens

Berrens, L.; Luis, Angel-Chvez

doi:10.1159/000237556

Cited by 1 publication

(1 citation statement)

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“…Landsteiner and Jacobs have shown in 1935 that guinea pigs are easily sensitized by injections or skin contact of nitrated aromatics such as 1,2,4-chlorodinitrobenzene, which can form covalent conjugates with proteins (17). Berrens et al showed that posttranslational modification of pollen allergens significantly increased their IgE binding capacity; even nonallergenic proteins were rendered active by a conjugation reaction (18). Petersen et al found significantly enhanced IgE binding to posttranslational modifications of the grass pollen allergen Phl p 1 (19), and Huby reported that posttranslational modifications appear generally to enhance allergenicity (20).…”

Section: Introductionmentioning

confidence: 99%

Protein Nitration by Polluted Air

Franze

Weller

Nießner

et al. 2005

Environ. Sci. Technol.

200

175

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The effects of air pollution on allergic diseases are not yetwell-understood. Here, we show that proteins, in particular birch pollen proteins including the allergen Bet v 1, are efficiently nitrated by polluted air. This posttranslational modification of proteins is likely to trigger immune reactions and provides a molecular rationale for the promotion of allergies bytraffic-related air pollution. Enzyme immunoassays have been used to determine equivalent degrees of nitration (EDN) for protein samples exposed to urban outdoor air and synthetic gas mixtures. The observed rates of nitration were governed by the abundance of nitrogen oxides and ozone, and concentration levels typical for summer smog conditions led to substantial nitration within a few hours to days (EDN up to 20%). Moreover, nitrated proteins were detected in urban road dust, window dust, and fine air particulate matter (EDN up to 0.1%).

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