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Clinical and Molecular Allergy
BioMedCentral
Research
Open Access
Sequence homology: A poor predictive value for profilins
cross-reactivity
Mojtaba Sankian1, Abdolreza Varasteh*1, Nazanin Pazouki1 and
Mahmoud Mahmoudi2
Address: 1Immunobiochemistry Lab, Immunology Research Center, Bu-Ali Research Institute, Mashhad, Iran and 2Molecular biology Lab,
Immunology Research Center, Bu-Ali Research Institute, Mashhad, Iran
Email: Mojtaba Sankian - m_sankian@; Abdolreza Varasteh* - a-varasteh@mums.ac.ir;
Nazanin Pazouki - npazouki@; Mahmoud Mahmoudi - Mahmoudi@mums.ac.ir
* Corresponding author
Published: 10 September 2005
Received: 28 June 2005
Accepted: 10 September 2005
Clinical and Molecular Allergy 2005, 3:13
doi:10.1186/1476-7961-3-13
This article is available from: /1476-7961/3/13
? 2005 Sankian et al; licensee BioMed Central Ltd.
This is an Open Access article distributed under the terms of the Creative Commons Attribution License (/licenses/by/2.0),
which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
food allergymelonprofilincross-reactivityepitope
Summary
Background: Profilins are highly cross-reactive allergens which bind IgE antibodies of almost 20% of
plant-allergic patients. This study is aimed at investigating cross-reactivity of melon profilin with other plant
profilins and the role of the linear and conformational epitopes in human IgE cross-reactivity.
Methods: Seventeen patients with melon allergy were selected based on clinical history and a positive
skin prick test to melon extract. Melon profilin has been cloned and expressed in E. coli. The IgE binding
and cross-reactivity of the recombinant profilin were measured by ELISA and inhibition ELISA. The amino
acid sequence of melon profilin was compared with other profilin sequences. A combination of chemical
cleavage and immunoblotting techniques were used to define the role of confo
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