Table of Contents
Journal of Allergy
Volume 2016 (2016), Article ID 4092817, 8 pages
Research Article

Cloning and Expression of Ama r 1, as a Novel Allergen of Amaranthus retroflexus Pollen

1Department of Immunology, Faculty of Medicine, Ahvaz Jundishapur University of Medical Sciences, Ahvaz 1478736714, Iran
2Department of Immunology, School of Medicine, Iran University of Medical Sciences, Tehran, Iran

Received 6 August 2015; Accepted 28 December 2015

Academic Editor: Desiderio Passali

Copyright © 2016 Payam Morakabati et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Sensitisation to Amaranthus retroflexus pollen is very common in tropical and subtropical countries. In this study we aimed to produce a recombinant allergenic Ole e 1-like protein from the pollen of this weed. To predict cross-reactivity of this allergen (Ama r 1) with other members of the Ole e 1-like protein family, the nucleotide sequence homology of the Ama r 1 was investigated. The expression of Ama r 1 in Escherichia coli was performed by using a pET-21b(+) vector. The IgE-binding potential of recombinant Ama r 1 (rAma r 1) was evaluated by immunodetection and inhibition assays using 26 patients’ sera sensitised to A. retroflexus pollen. The coding sequence of the Ama r 1 cDNA indicated an open reading frame of 507 bp encoding for 168 amino acid residues which belonged to the Ole e 1-like protein family. Of the 26 serum samples, 10 (38.46%) had significant specific IgE levels for rAma r 1. Immunodetection and inhibition assays revealed that the purified rAma r 1 might be the same as that in the crude extract. Ama r 1, the second allergen from the A. retroflexus pollen, was identified as a member of the family of Ole e 1-like protein.