Chenopodium album pollen profilin (Che a 2): homology modeling and evaluation of cross-reactivity with allergenic profilins based on predicted potential IgE epitopes and IgE reactivity analysis

  title={Chenopodium album pollen profilin (Che a 2): homology modeling and evaluation of cross-reactivity with allergenic profilins based on predicted potential IgE epitopes and IgE reactivity analysis},
  author={Akram Amini and Mojtaba Sankian and Mohammad-Ali Assarehzadegan and Fatemeh Vahedi and Abdolreza Varasteh},
  journal={Molecular Biology Reports},
The inhalation of Chenopodium album (C. album) pollen has been reported as an important cause of allergic respiratory symptoms. The aim of this study was to produce the recombinant profilin of C. album (rChe a 2) pollen and to investigate its cross-reactivity with other plant-derived profilins based on potential conformational epitopes and IgE reactivity analysis. Che a 2-coding sequence was cloned, expressed, and purified using one step metal affinity chromatography to recover high-purity… 

Immunochemical and molecular characterization of allergenic profilin (Koc s 2) from Kochia scoparia pollen

High degree of homology was found among amino acid sequences of Kochia profilin and several Profilin molecules from unrelated plant families.

Pro j 2 is mesquite profilin: molecular characteristics and specific IgE binding activity.

Pro j 2, as a new allergen from mesquite pollen, was produced in E. coli with an IgE-reactivity similar to that of its natural counterpart, and amino acid sequences homology analysis of mesquite profilin and several Profilin molecules from other plants showed high degree of cross-reactive among plant-derived profilins from unrelated families.

Diagnosis of Chenopodium album allergy with a cocktail of recombinant allergens as a tool for component-resolved diagnosis

It is confirmed that the allergenic cocktail with high diagnostic potential could be replaced with natural C. album allergen extracts in skin prick test and serologic tests.

Immunochemical Characterization of Acacia Pollen Allergens and Evaluation of Cross-Reactivity Pattern with the Common Allergenic Pollens

The findings suggest that several proteins such as 15, 23, 45, and 50 kDa proteins could be used as diagnostic and therapeutic reagents for patients allergic to A. farnesiana and P. juliflora.

Molecular Cloning and Expression of a New Allergen of Acacia farnesiana (Aca f 2).

The amino acid sequence homology analysis showed high cross-reactivity between Aca f 2 and other profilins from botanically unrelated common allergenic plants.

Cloning and expression of Aca f 1: a new allergen of Acacia farnesiana pollen

A high degree of homology was found among amino acid sequences of Aca f 1 and several allergenic members of Ole e 1-like protein family.

Construction of a recombinant allergen-producing probiotic bacterial strain: Introduction of a new line for a live oral vaccine against Chenopodium album pollen allergy.

Immunoblot analyses demonstrated that recombinant Che a 2 is expressed as a 32 kDa dimeric protein immunological studies showed it can bind human IgE.

Amaranthaceae pollens: review of an emerging allergy in the mediterranean area.

An extensive overview of Amaranthaceae pollen allergens is provided, focusing on their physicochemical, and immunological properties and on their clinical significance in allergic patients, and studies where these recombinant allergens and their hypoallergenic derivatives have been used in clinical diagnosis and their potential use in personalized therapy are reviewed.



Recombinant expression, purification and cross-reactivity of chenopod profilin: rChe a 2 as a good marker for profilin sensitization

The immunological analysis of rChe a 2 showed IgG- and IgE-binding capabilities equivalent to those of its natural counterpart, Che a 2, isolated from the pollen, andhibition experiments showed high cross-reactivity degrees with different allergenic sources.

Identification and Characterization of Che a 1 Allergen from Chenopodium album Pollen

Che a 1, a relevant allergen from chenopod pollen, is structurally related to the Ole e 1-like protein family, but exhibits significant differences on its polypeptide sequence that could explain its different antigenic behavior and limited cross-reactivity.

Sal k 4, a New Allergen of Salsola kali, Is Profilin: A Predictive Value of Conserved Conformational Regions in Cross-Reactivity with Other Plant-Derived Profilins

Investigation of a new allergen of S. kali allergic patients and Amino acid sequence homology analysis showed that a high degree of IgE cross-reactivity among plant-derived profilins might depend on the predicted conserved conformational regions.

Mango profilin: cloning, expression and cross-reactivity with birch pollen profilin Bet v 2

In this study, two isoforms of mango fruits profilin were amplified by RT-PCR and 3′RACE from total RNA and deduced amino acid sequence of the corresponding protein show high identity with other allergenic profilins.

Sequence homology: A poor predictive value for profilins cross-reactivity

Comparison of three-dimensional models of watermelon and melon profilin indicated amino acid differences influence the electric potential and accessibility of the solvent-accessible surface of profilins that may markedly affect conformational epitopes.

Che a 1: Recombinant Expression, Purification and Correspondence to the Natural Form

Structural and in vitro immunological properties of rChe a 1 produced in P. pastoris were equivalent to those of the natural form of the allergen and, thus, it could be used in testing patients allergic to chenopod pollen.

Profilins constitute a novel family of functional plant pan-allergens

The presence of profilin and possibly related proteins as crossreacting allergenic components in various plants therefore provides an explanation as to why certain allergic patients display type I allergic reactions with pollens and even food from distantly related plants.

Expression of the recombinant major allergen of Salsola kali pollen (Sal k 1) and comparison with its low-immunoglobulin E-binding mutant.

It is demonstrated that purified rSal k 1 is comprised of IgE-epitopes similar to that of its natural counterpart and that the mutated variant showed a reduced Ig E-binding capacity based on in vitro assays and in vivo provocation testing.

Allergy to Salsola Kali in a Salsola incanescens-rich area: role of extensive cross allergenicity.

The results suggest that in S. incanescens-rich areas, S. kali pollen extracts could be used as a diagnostic reagent for allergic patients to S. difficile pollen allergens, and several IgE binding components that shows a close allergenic relationship with S.Kali pollen.