Cloning and characterization of the hemocyanin gene of prawn Macrobrachium nipponense

Wang, Wenfeng; Xia, Xuan; Liu, Fang; Chen, Xiangli; Yang, Hong; Ning, Qianji

doi:10.5505/tjb.2012.02996

Cited by 9 publications

(11 citation statements)

References 21 publications

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“…The result is the same as the findings in other crustaceans, such as H. americanus [17], Fenneropenaeus chinensis [36], and E. sinensis [15], and consistent with the report that hemocyanin synthesis occurs mainly in the hepatopancreas [37]. MnHc-1 expression was detected in all the examined tissues except for muscle, which is different from another subunit of hemocyanin in M. nipponense (MnHc-2) expressed in the muscle [26]. We also found that MnHc-1 was expressed in ovary, whereas MnHc-2 was hardly expressed in ovary [26].…”

Section: Discussionsupporting

confidence: 90%

“…MnHc-1 expression was detected in all the examined tissues except for muscle, which is different from another subunit of hemocyanin in M. nipponense (MnHc-2) expressed in the muscle [26]. We also found that MnHc-1 was expressed in ovary, whereas MnHc-2 was hardly expressed in ovary [26]. The discrepant expression patterns of these two subunits of hemocyanin may be owing to their functional specialization in different tissues.…”

Section: Discussionmentioning

confidence: 99%

“…As a result, the investigation on the M. nipponense innate immune mechanism against A. hydrophila has become a key issue of health management in crustacean farming. The hemocyanin subunit is a functional group for crustacean immunity, and a hemocyanin subunit has been cloned and characterized in the freshwater prawn M. nipponense [26]. In this study, we discovered another hemocyanin subunit in M. nipponense (MnHc-1).…”

Section: Introductionmentioning

confidence: 88%

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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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Section: Discussionsupporting

confidence: 90%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 88%

See 1 more Smart Citation

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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“…Sequence similarity between these respiratory proteins was assessed by their comparisons. However, the primary structures of only few representatives of hemocyanins from the subphylum crustacea, namely Macrobrachium nipponense, Homarus americanus, P. interruptus, Palinurus vulgaris, C. magister, and CaSS2 of C. aestuarii, are known (Wang et al 2012;Kusche and Burmester 2001). Structural comparison of crustacean hemocyanin polypeptide chains by sequence alignments (Burmester 2004;Marxen et al 2013) and immunochemistry (Markl et al 1984) showed a discrimination between different subunit types within infraorders.…”

Section: Introductionmentioning

confidence: 97%

Structure and Characterization of Eriphia verrucosa Hemocyanin

et al. 2015

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Arthropod hemocyanins (Hcs) are a family of large extracellular oxygen-transporting proteins with high molecular mass and hexameric or multi-hexameric molecular assembly. This study reports for the first time the isolation and characterization of the structure of an arthropod hemocyanin from crab Eriphia verrucosa (EvH) living in the Black Sea. Its oligomeric quaternary structure is based on different arrangements of a basic 6 × 75 kDa hexameric unit, and four of them (EvH1, EvH2, EvH3, and EvH4) were identified using ion-exchange chromatography. Subunit 3 (EvH3) shows high similarity scores (75.0, 87.5, 91.7, and 75.0 %, respectively) by comparison of the N-terminal sequence of subunit 1 from Cancer pagurus of the North Sea (Cp1), subunits 3 and 6 of Cancer magister (Cm3 and Cm6), and subunit 2 of Carcinus aestuarii (CaSS2), respectively. Moreover, a partial cDNA sequence (1309 bp) of E. verrucosa hemocyanin encoding a protein of 435 amino acids was isolated. The deduced amino acid sequence shows a high degree of similarity with subunits 3, 4, 5, and 6 of C. magister (81-84 %). Most of the hemocyanins are glycosylated, and three putative O-linkage sites were identified in the partial amino acid sequence of EvH at positions 444-446, 478-480, and 547-549, respectively. The higher stability of native Hc in comparison to its subunit EvH4 as determined by circular dichroism (CD) could be explained with the formation of a stabilizing quaternary structure.

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“…The sequence similarity between these respiratory proteins was assessed by their comparisons. However, the primary structures of only few representatives of hemocyanins from the subphylum crustacea, namely, Macrobrachium nipponense, Homarus americanus, Astacus leptodactylus, P. interruptus, Palinurus vulgaris, C. magister, and CaSS2 of C. aestuarii are known (Wang et al 2012;Schneider et al 1986;Kusche and Burmester 2001). Structural comparison of crustacean hemocyanin polypeptide chains by sequence alignments (Neuteboom et al 1989;Burmester 2004;Marxen et al 2013) and immunochemistry (Markl et al 1984) showed a discrimination between different subunit types within infraorders.…”

Section: Introductionmentioning

confidence: 98%