Abstract

Profilin is a small actin-binding protein that is essential in all organisms. While the wheat genome sequence database is not currently available, the exploration of bioinformatics is very important. Therefore, this article predicted the structure and function of profilin in wheat by bioinformatics methods. The amino acid sequence of profilin was searched in GeneBack. While its signal peptides were analyzed through CBS prediction server, the hydrophobicities were analyzed by bioedit software, we used EMBnet server and DNAstar to analyse the transmembrane domains and the B-cell epitopes of the profilin respectively. Finally, the tertiary structure of the protein was predicted through Swiss-Model. This information will help develop rational strategies to improve the component-resolving diagnosis and immunotherapy of profilin allergy.

Highlights

  • Profilins are ubiquitous and abundant cytosolic proteins of 12 - 15 kDa, found in all eukaryotic cells [1] [2] [3] and virus [4]

  • While its signal peptides were analyzed through CBS prediction server, the hydrophobicities were analyzed by bioedit software, we used EMBnet server and DNAstar to analyse the transmembrane domains and the B-cell epitopes of the profilin respectively

  • The amino acid sequence of the wheat profilin protein can be found in the NCBI website; the signal peptide is analyzed by CBS prediction server login and the hydrophobic protein is predicted by bioedit Sequence Alignment Editer

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Summary

Introduction

Profilins are ubiquitous and abundant cytosolic proteins of 12 - 15 kDa, found in all eukaryotic cells [1] [2] [3] and virus [4] They are key regulators of actin cytoskeleton dynamics through their interaction to monomeric actin (G-actin), and to a plethora of actin-binding proteins, which involve poly-L-proline (PLP) stretches [5]. The wide spread cross-reactivity of profilins has led to the designation of profilins as “pan-allergens” [9]. The sensitization to these allergens has been considered as a risk factor for allergic reactions [10]. The knowledge provided in this study will help develop rational strategies to improve the component-resolving diagnosis and immunotherapy of profilin allergy

Method
Analysis of Gene Function
Analysis Structure
Findings
Conclusions
Full Text
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