Functional Divergence of the N-Lobe and C-Lobe of <i>Transferrin</i> Gene in <i>Pungitius sinensis</i> (Amur Stickleback)

Transferrin is an important iron-binding glycosylated protein and plays key roles in iron-binding and immune response. Here, a 2037-bp open reading frame was obtained from our previous transcriptome sequencing data of Amur stickleback, which encoded a 679 amino acid putative transferrin protein harb...

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Main Author: Jun Cao
Format: Article
Language:English
Published: MDPI AG 2022-12-01
Series:Animals
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Online Access:https://www.mdpi.com/2076-2615/12/24/3458
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author Jun Cao
author_facet Jun Cao
author_sort Jun Cao
collection DOAJ
description Transferrin is an important iron-binding glycosylated protein and plays key roles in iron-binding and immune response. Here, a 2037-bp open reading frame was obtained from our previous transcriptome sequencing data of Amur stickleback, which encoded a 679 amino acid putative transferrin protein harbored obvious N-lobe and C-lobe domains. The tissue-specific expression pattern showed that the transcript was detected in a variety of tissues, with the highest signal in liver. Moreover, <i>Streptococcus iniae</i> pathogen stimulation can increase the expression level of this transcript, implying important immune properties for organisms. Next, N-lobes and C-lobes were obtained from 45 fish species. The phylogenetic tree showed that N-lobes and C-lobes were in two different evolutionary branches, and they had different motif composition. Functional divergence indicated a higher evolutionary rate or site-specific alteration among the N-lobe and C-lobe groups. <i>Ka</i>/<i>Ks</i> value of C-lobe group was relatively higher than that of N-lobe group, indicating a faster change rate of C-lobe sequences in evolution. Moreover, some sites experiencing positive selection were also found, which may be involved in the iron- or anion-binding, pathogen resistance and diversification of transferrin protein. Differential iron-binding activity was also detected between N-lobe and C-lobe of Amur stickleback transferrin protein with Chrome Azurol S assay. Compared with the C-lobe, the N-lobe showed stronger growth inhibitory activity of <i>Escherichia coli</i>, implying their potential antibacterial properties. This study will give a reference for subsequent research of transferrin proteins.
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spelling doaj.art-b5143ebc2be944789e63d64a10d6dcca2023-11-24T12:50:04ZengMDPI AGAnimals2076-26152022-12-011224345810.3390/ani12243458Functional Divergence of the N-Lobe and C-Lobe of <i>Transferrin</i> Gene in <i>Pungitius sinensis</i> (Amur Stickleback)Jun Cao0School of Life Sciences, Jiangsu University, Zhenjiang 212013, ChinaTransferrin is an important iron-binding glycosylated protein and plays key roles in iron-binding and immune response. Here, a 2037-bp open reading frame was obtained from our previous transcriptome sequencing data of Amur stickleback, which encoded a 679 amino acid putative transferrin protein harbored obvious N-lobe and C-lobe domains. The tissue-specific expression pattern showed that the transcript was detected in a variety of tissues, with the highest signal in liver. Moreover, <i>Streptococcus iniae</i> pathogen stimulation can increase the expression level of this transcript, implying important immune properties for organisms. Next, N-lobes and C-lobes were obtained from 45 fish species. The phylogenetic tree showed that N-lobes and C-lobes were in two different evolutionary branches, and they had different motif composition. Functional divergence indicated a higher evolutionary rate or site-specific alteration among the N-lobe and C-lobe groups. <i>Ka</i>/<i>Ks</i> value of C-lobe group was relatively higher than that of N-lobe group, indicating a faster change rate of C-lobe sequences in evolution. Moreover, some sites experiencing positive selection were also found, which may be involved in the iron- or anion-binding, pathogen resistance and diversification of transferrin protein. Differential iron-binding activity was also detected between N-lobe and C-lobe of Amur stickleback transferrin protein with Chrome Azurol S assay. Compared with the C-lobe, the N-lobe showed stronger growth inhibitory activity of <i>Escherichia coli</i>, implying their potential antibacterial properties. This study will give a reference for subsequent research of transferrin proteins.https://www.mdpi.com/2076-2615/12/24/3458immune responseiron-bindingantibacterial propertymolecular evolutionfunctional divergenceselection pressure
spellingShingle Jun Cao
Functional Divergence of the N-Lobe and C-Lobe of <i>Transferrin</i> Gene in <i>Pungitius sinensis</i> (Amur Stickleback)
Animals
immune response
iron-binding
antibacterial property
molecular evolution
functional divergence
selection pressure
title Functional Divergence of the N-Lobe and C-Lobe of <i>Transferrin</i> Gene in <i>Pungitius sinensis</i> (Amur Stickleback)
title_full Functional Divergence of the N-Lobe and C-Lobe of <i>Transferrin</i> Gene in <i>Pungitius sinensis</i> (Amur Stickleback)
title_fullStr Functional Divergence of the N-Lobe and C-Lobe of <i>Transferrin</i> Gene in <i>Pungitius sinensis</i> (Amur Stickleback)
title_full_unstemmed Functional Divergence of the N-Lobe and C-Lobe of <i>Transferrin</i> Gene in <i>Pungitius sinensis</i> (Amur Stickleback)
title_short Functional Divergence of the N-Lobe and C-Lobe of <i>Transferrin</i> Gene in <i>Pungitius sinensis</i> (Amur Stickleback)
title_sort functional divergence of the n lobe and c lobe of i transferrin i gene in i pungitius sinensis i amur stickleback
topic immune response
iron-binding
antibacterial property
molecular evolution
functional divergence
selection pressure
url https://www.mdpi.com/2076-2615/12/24/3458
work_keys_str_mv AT juncao functionaldivergenceofthenlobeandclobeofitransferrinigeneinipungitiussinensisiamurstickleback