Abstract:
:Sensitization to Cupressaceae pollen has become one of the most important causes of pollinosis in Western countries during winter and early spring. However, the characterization of the extracts, the allergens involved and the cross-reactivity with other pollen sources still remain poorly studied; in the case of Cupressus arizonica only two allergens have been described so far. A new allergen from C. arizonica pollen, Cup a 4, was cloned and expressed in Escherichia coli as an N-terminally His-tag recombinant protein that was characterized biochemically, immunologically and by circular dichroism spectroscopy. The new allergen has high sequence identity with Prickly Juniper allergen Jun o 4 and contains four EF-hand domains. The recombinant protein has structural similarities with other calcium binding allergens such as Ole e 3, Ole e 8 and Phl p 7. Cup a 4 is expressed in mature pollen grains and shares antigenic properties with the recombinant form. Sera from 9.6% C. arizonica allergic patients contain specific IgE antibodies against recombinant Cup a 4.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Pico de Coaña Y,Parody N,Fuertes MÁ,Carnés J,Roncarolo D,Ariano R,Sastre J,Mistrello G,Alonso Cdoi
10.1016/j.bbrc.2010.09.079subject
Has Abstractpub_date
2010-10-22 00:00:00pages
451-7issue
3eissn
0006-291Xissn
1090-2104pii
S0006-291X(10)01776-6journal_volume
401pub_type
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