Objective: Many pathogenesis-related (PR) proteins from plants are allergen
ic. We review the evidence that PR proteins represent an increasingly impor
tant group of plant-derived allergens.
Data Sources: A detailed literature search was conducted through PubMed and
GenBank databases.
Study Selection: All reports in PubMed and GenBank related to PR protein al
lergens for which at least partial amino acid sequence is known were includ
ed.
Results: Production of PR proteins by plants is induced in plants by stress
. Members of PR-protein groups 2, 3, 4, 5, 8, 10, and 14 have demonstrated
allergenicity. PR2-, 3-, 4-, and 8-homologous allergens are represented by
the latex allergens. Cross-reactivity of PR3 latex allergen, Hev b 6.02, wi
th some fruit allergens may be a reflection of the representation of homolo
gous PR proteins among varied plants. The expression of one of the represen
tative PR5-homologous cedar pollen allergens, Jun a 3, is highly variable a
cross years and geographic areas, possibly because of variable induction of
this PR protein by environmental factors. PR10-homologous birch pollen all
ergen, Bet v 1, is structurally similar to and cross-reacts with PR10 prote
ins from fruits (eg, Mal d 1) which cause oral allergy syndrome. PR14 aller
gens (eg, Zea m 14) consist of lipid transfer proteins found in grains and
fruits and are inducers of anaphylaxis.
Conclusions: PR-homologous allergens are pervasive in nature. Similarity in
the amino acid sequences among members of PR proteins may be responsible f
or cross-reactivity among allergens from diverse plants. Induced expression
of PR-homologous allergens by environmental factors may explain varying de
grees of allergenicity. Man-made environmental pollutants may also alter th
e expression of some PR protein allergens.