SNPs of hemocyanin C‐terminal fragment in shrimp <i>Litopenaeus vannamei</i>

Zhao, Xianliang; Guo, Lingling; Zhang, Yueling; Liu, Yao; Zhang, Xiaoyu; Lun, Jingsheng; Chen, Jiehui; Li, Yuanyou

doi:10.1016/j.febslet.2011.12.038

Cited by 41 publications

(13 citation statements)

References 28 publications

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“…Previous studies have shown that hemocyanin exerted its antimicrobial function based on different mechanisms including glycosylation modification (Zhang et al 2017) and molecular polymorphism (Zhao et al 2016; Lu et al 2015; Guo et al 2013; Zhao et al 2012, 2013). Here, we predicted and characterized a novel hemocyanin-derived antimicrobial peptide L1 using bioinformatics, followed by experimental validation.…”

Section: Discussionmentioning

confidence: 99%

Prediction and characterization of a novel hemocyanin-derived antimicrobial peptide from shrimp Litopenaeus vannamei

et al. 2018

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Hemocyanin, the multifunctional glycoprotein in the hemolymph of invertebrates, can generate various antimicrobial peptides (AMPs). Given the rising interest in the use of natural therapeutic agents such as AMPs, alternative and more efficient methods for their generation are being explored. In this work, free online software was first applied to predict the generation of antimicrobial peptides from the large subunit of Litopenaeus vannamei hemocyanin. Twenty potential antimicrobial peptides ranging from 1.5 to 1.9 kDa were predicted, five of which had α-helical structures and were selected for antibacterial activity testing. The results indicated that these five peptides had antibacterial activity against seven different bacteria. Of the five peptides, one peptide, designated L1, had the strongest antibacterial activity against both Gram-negative and Gram-positive bacteria. Moreover, CD and NMR data showed that L1 had both α-helical and β-turns structural composition, and that these structures were essential for L1’s antibacterial activity. Furthermore, SEM analysis revealed that peptide L1 had broad-spectrum activity against both Gram-positive and Gram-negative bacteria, as it could destroy the bacterial cell walls and kill the bacteria. Thus, L1 is a very potent antimicrobial peptide that can be exploited and used in antibacterial therapeutics.Electronic supplementary materialThe online version of this article (10.1007/s00726-018-2575-x) contains supplementary material, which is available to authorized users.

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Section: Discussionmentioning

confidence: 99%

Prediction and characterization of a novel hemocyanin-derived antimicrobial peptide from shrimp Litopenaeus vannamei

et al. 2018

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“…Zhang et al [38] found that the main protein directly bound to the Vibrio alginolyticus , Vibrio harveyi , A. hydrophila , and Staphylococcus aureus in L. vannamei serum was hemocyanin, suggesting that hemocyanin possesses antibacterial functions. The C-terminus of L. vannamei hemocyanin is possibly related to the immunity in shrimp to different pathogens [39]. Gram-negative bacteria A. hydrophila are a common species of the Aeromonas genus in water and water habitants [40].…”

Section: Discussionmentioning

confidence: 99%

Molecular Cloning, Characterization, and mRNA Expression of Hemocyanin Subunit in Oriental River PrawnMacrobrachium nipponense

Kong

Chen

Ding

et al. 2016

International Journal of Genomics

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Hemocyanin is a copper-containing protein with immune function against disease. In this study, a hemocyanin subunit named MnHc-1 was cloned from Macrobrachium nipponense. The full-length cDNA of MnHc-1 was 2,163 bp with a 2,028-bp open reading frame (ORF) encoding a polypeptide of 675 amino acids. The MnHc-1 mRNA was expressed in the hepatopancreas, gill, hemocytes, intestine, ovary, and stomach, with the highest level in the hepatopancreas. In the infection trial, the MnHc-1 mRNA transcripts in the hemocytes were significantly downregulated at 3 h after injection of Aeromonas hydrophila and then upregulated at 6 h and 12 h, followed by a gradual recovery from 24 to 48 h. The MnHc-1 transcriptional expression in the hepatopancreas was measured after M. nipponense were fed seven diets with 2.8, 12.2, 20.9, 29.8, 43.1, 78.9, and 157.1 mg Cu kg−1 for 8 weeks, respectively. The level of MnHc-1 mRNA was significantly higher in the prawns fed 43.1–157.1 mg Cu kg−1 diet than in that fed 2.8–29.8 mg Cu kg−1 diet. This study indicated that the MnHc-1 expression can be affected by dietary copper and the hemocyanin may potentially participate in the antibacterial defense of M. nipponense.

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“…These amino acid substitutions likely confer alternate functionality to newly synthesised Hbs. Similarly, 13 Hc-associated SNPs have been identified in shrimp ( L. vannamei ) infected with the same pathogens [142, 143]. These molecular alterations were located in the immunoglobulin-like domain and C-terminal region of the shrimp Hc resulting in improved microbial agglutination properties.…”

Section: An Emerging Role For Invertebrate (Bivalve) Hemoglobin In Inmentioning

confidence: 99%

Immunological properties of oxygen-transport proteins: hemoglobin, hemocyanin and hemerythrin

Coates

Decker

2016

Cell. Mol. Life Sci.

128

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It is now well documented that peptides with enhanced or alternative functionality (termed cryptides) can be liberated from larger, and sometimes inactive, proteins. A primary example of this phenomenon is the oxygen-transport protein hemoglobin. Aside from respiration, hemoglobin and hemoglobin-derived peptides have been associated with immune modulation, hematopoiesis, signal transduction and microbicidal activities in metazoans. Likewise, the functional equivalents to hemoglobin in invertebrates, namely hemocyanin and hemerythrin, act as potent immune effectors under certain physiological conditions. The purpose of this review is to evaluate the true extent of oxygen-transport protein dynamics in innate immunity, and to impress upon the reader the multi-functionality of these ancient proteins on the basis of their structures. In this context, erythrocyte–pathogen antibiosis and the immune competences of various erythroid cells are compared across diverse taxa.Electronic supplementary materialThe online version of this article (doi:10.1007/s00018-016-2326-7) contains supplementary material, which is available to authorized users.

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SNPs of hemocyanin C‐terminal fragment in shrimp Litopenaeus vannamei

Cited by 41 publications

References 28 publications

Prediction and characterization of a novel hemocyanin-derived antimicrobial peptide from shrimp Litopenaeus vannamei

Prediction and characterization of a novel hemocyanin-derived antimicrobial peptide from shrimp Litopenaeus vannamei

Molecular Cloning, Characterization, and mRNA Expression of Hemocyanin Subunit in Oriental River PrawnMacrobrachium nipponense

Immunological properties of oxygen-transport proteins: hemoglobin, hemocyanin and hemerythrin

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