Proteomics analysis of two heat shock proteins in insects

Abstract

Heat shock proteins (HSPs) are found in all living organisms, from bacteria to humans, are expressed under stress. In this study, characterization of two families of HSP including HSP60 and HSP70 protein was compared in different insect species from different orders. According to the conserved motifs analysis, none of the motifs were shared by all insects of two protein families but each family had their own common motifs. Functional and structural analyses were carried out on seven different insect species from each protein family as the representative samples. These analyses were performed via ExPASy database tools. The tertiary structure of Drosophila melanogater as the sample of each protein family were predicted by the Phyre2 and TM-score servers then their qualities were verified by SuperPose and PROCHECK. The tertiary structures were predicted through the "c4pj1E" model (PDB Accession Code: 4pj1) in HSP60 family and "c3d2fC" model (PDB Accession Code: 3d2f) in HSP70 family. The protein phylogenetic tree was constructed using the Neighbor-joining (NJ) method by Molecular Evolutionary Genetic Analysis (MEGA) 6.06. According to the results, there was a high identity of HSP60 and HSP70 families so that they should be derived from a common ancestor however they belonged to separate groups. In protein-protein interaction analysis by STRING 10.0, 10 common enriched pathways of biological process, molecular function and Kyoto Encyclopedia of Genes and Genomes (KEGG) were identified in D. melanogaster in both families. The obtained data provide a background for bioinformatic studies of the function and evolution of insects and other organisms. Communicated by Mark Joshua Valencia.

Los genes y proteínas Hsp frente al estrés térmico en insectos

“…Esta identificación fue facilitada por la descripción de Ferruco Ritossa, quien en 1962 notó que el incremento de temperatura provocó la presencia de abultamientos (puffs) en los cromosomas de las glándulas salivales de las larvas de Drosophila melanogaster. Posteriormente, estos fueron estudiados por Tissieres (Puerta et al 2007;Seddigh 2019).…”

In-depth analysis of amino acid and nucleotide sequences of Hsp60: how conserved is this protein?

“…The average content of aliphatic (Ala, Val, Gly, and Ile), charged (Glu, Lys, and Asp), and polar (Thr) amino acid residues in Hsp60 sequences is not only high, but also higher than the average proteomic values for almost all phyla (Figure 3b). The high content of aliphatic amino acid residues may indicate the structural stability of these proteins 15 . The content of Pro, aromatic (Phe, Tyr, His, and Trp) and polar (Ser and Cys) amino acid residues was low and lower compared to the average proteomic values.…”

“…At present, in-depth analysis of Hsp60 sequences in silico is quite rare, although it is a very interesting object for research. Since Hsp60 is ubiquitous, it can be used in evolutionary analysis of organisms belonging to different taxonomic groups [12][13][14][15] . Using bioinformatics, epitopes in Hsp60 can be predicted 16,17 .…”

In‐depth analysis of amino acid and nucleotide sequences of Hsp60: How conserved is this protein?

“…At present, in‐depth analysis of Hsp60 sequences in silico is quite rare, although it is a very interesting object for research. Since Hsp60 is ubiquitous, it can be used in evolutionary analysis of organisms belonging to different taxonomic groups 12–15 . Using bioinformatics, epitopes in Hsp60 can be predicted 16,17 .…”

“…Since Hsp60 is ubiquitous, it can be used in evolutionary analysis of organisms belonging to different taxonomic groups. [12][13][14][15] Using bioinformatics, epitopes in Hsp60 can be predicted. 16,17 In particular, an epitopebased vaccine containing Hsp60 epitopes from Helicobacter pylori was tested in a model of a Mongolian gerbil infected with H. pylori.…”