Allergen motifs and the prediction of allergenicity

Marti, Pamela; Truffer, Renato; Stadler, Michael B; Keller-Gautschi, Elsbeth; Crameri, Reto; Mari, Adriano; Schmid-Grendelmeier, Peter; Miescher, Sylvia M; Stadler, Beda M; Vogel, Monique (2007). Allergen motifs and the prediction of allergenicity. Immunology letters, 109(1), pp. 47-55. Amsterdam: Elsevier 10.1016/j.imlet.2007.01.002

Full text not available from this repository. (Request a copy)

We have recently shown that the majority of allergens can be represented by allergen motifs. This observation prompted us to experimentally investigate the synthesized peptides corresponding to the in silico motifs with regard to potential IgE binding and cross-reactions with allergens. Two motifs were selected as examples to conduct in vitro studies. From the first motif, derived from allergenic MnSOD sequences, the motif stretch of the allergen Asp f 6 was selected and synthesized as a peptide (MnSOD Mot). The corresponding full-length MnSOD was also expressed in Escherichia coli and both were compared for IgE reactivity with sera of patients reacting to the MnSOD of Aspergillus fumigatus or Malassezia sympodialis. For the second motif, the invertebrate tropomyosin sequences were aligned and a motif consensus sequence was expressed as a recombinant protein (Trop Mot). The IgE reactivity of Trop Mot was analyzed in ELISA and compared to that of recombinant tropomyosin from the shrimp Penaeus aztecus (rPen a 1) in ImmunoCAP. MnSOD Mot was weakly recognized by some of the tested sera, suggesting that the IgE binding epitopes of a multimeric globular protein such as MnSOD cannot be fully represented by a motif peptide. In contrast, the motif Trop Mot showed the same IgE reactivity as shrimp full-length tropomyosin, indicating that the major allergenic reactivity of a repetitive structure such as tropomyosin can be covered by a motif peptide. Our results suggest that the motif-generating algorithm may be used for identifying major IgE binding structures of coiled-coil proteins.

Item Type:

Journal Article (Original Article)

Division/Institute:

04 Faculty of Medicine > Department of Haematology, Oncology, Infectious Diseases, Laboratory Medicine and Hospital Pharmacy (DOLS) > Institute for Immunology (discontinued)

UniBE Contributor:

Miescher-Granger, Sylvia M.; Stadler, Beda Martin and Vogel, Monique

ISSN:

0165-2478

ISBN:

17303251

Publisher:

Elsevier

Language:

English

Submitter:

Factscience Import

Date Deposited:

04 Oct 2013 14:57

Last Modified:

06 Dec 2013 13:49

Publisher DOI:

10.1016/j.imlet.2007.01.002

PubMed ID:

17303251

Web of Science ID:

000245772900006

URI:

https://boris.unibe.ch/id/eprint/24640 (FactScience: 52181)

Actions (login required)

Edit item Edit item
Provide Feedback