Phenoloxidase activity in humoral plasma, hemocyanin and hemocyanin separated proteins of the giant freshwater prawn Macrobrachium rosenbergii

Ramasamy, Sivakumar Mullaivanam; Denis, Maghil; Sivakumar, Shanthi; Arumugam, Muthu

doi:10.1016/j.ijbiomac.2017.04.088

Cited by 23 publications

(11 citation statements)

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“…The results of the present study suggest that MrHc2 belongs to the γ-type of hemocyanin, as it exhibits a close relationship with Hc-1, a γ-type hemocyanin of M. nipponense (Todorovska et al 2021). Ramasamy et al (2017) reported that hemocyanin proteins of M. rosenbergii can be divided into four proteins:…”

Section: Discussionmentioning

confidence: 52%

“…Phenoloxidase activity of gastrolith hemocyanins has been reported in the crayfish Cherax quadricarinatus (Glazer et al 2013). In the prawn Macrobrachium rosenbergii , exogenous elicitors, such as trypsin, sodium dodecyl sulfate, bacterial cell wall components, and polysaccharide laminarin, can activate phenoloxidase activity in four different hemocyanin proteins (Ramasamy et al 2017). The recombinant hemocyanin proteins of the crayfish Procambarus clarkii displayed strong antibacterial activity against Vibrio parahaemolyticus and Staphylococcus aureus in bacterial growth inhibition, phenoloxidase, and phagocytosis assays (Qin et al 2018).…”

Section: Introductionmentioning

confidence: 99%

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Molecular isolation and expression analysis of hemocyanin isoform 2 of Macrobrachium rosenbergii

et al. 2022

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Objective Hemocyanin is a copper‐bearing protein in the hemolymph of many arthropods and mollusks and functions as an oxygen transport and important nonspecific immune protein. Methods In this study, complementary DNA of hemocyanin isoform 2 of the prawn Macrobrachium rosenbergii (MrHc2) was isolated by rapid amplification of cDNA ends and mRNA expression was characterized to elucidate molecular basis of its function. Result With a molecular mass of 77.3 kDa, MrHc2 contained three domains: hemocyanin‐all‐alpha, hemocyanin‐copper‐containing, and hemocyanin‐immunoglobulin‐like domains. Molecular phylogenetic analysis revealed that MrHc2 belongs to the γ‐type subunit and is closely related to hemocyanin subunit 1 of the palaemonid shrimp Macrobrachium nipponense. In addition, MrHc2 resided in a different clade relative to hemocyanin (MrHc) of M. rosenbergii (α‐type subunit) and in a different subclade relative to the hemocyanin proteins of penaeid shrimp. The messenger RNA transcript of MrHc2 was highly expressed in the hepatopancreas and weakly expressed in the gills, intestine, stomach, muscle, and hemocytes. Upon challenge with M. rosenbergii nodavirus (MrNV), the expression of MrHc2 was 1.96‐, 2.93‐, and 1.96‐fold on days 3, 4, and 5, respectively, and then gradually declined to basal levels on day 7. Conclusion This study suggests that MrHc2 plays an important role in the innate immune response of M. rosenbergii to MrNV.

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Section: Discussionmentioning

confidence: 52%

Section: Introductionmentioning

confidence: 99%

Molecular isolation and expression analysis of hemocyanin isoform 2 of Macrobrachium rosenbergii

et al. 2022

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“…From the foregoing, it could be inferred that in addition to the proPO system, there seems to be another pathway that enhances PO activity. This alternative or additional pathway might be related to haemocyanin, which also has PO activity (Decker & Rimke, 1998; Mullaivanam Ramasamy et al, 2017).…”

Section: Effects Of Ammonia Stress On Shrimp Physiology and Biochemistrymentioning

confidence: 99%

“…Since the first report on the phenoloxidase activity of haemocyanin from Eurypelma californicum (Decker & Rimke, 1998), a number of studies have since revealed that haemocyanin and phenoloxidase are hexameric type 3 copper proteins (Masuda et al, 2018), with the geometry and coordination environment of the active site of arthropodan PO very similar to that of arthropodan haemocyanin (Masuda et al, 2014). In addition, haemocyanin exhibits phenoloxidase activity under some conditions, such as treatment with sodium dodecyl sulphate (SDS), polysaccharide laminarin and lipopolysaccharide (LPS) of Gram‐negative bacteria, trypsin or a trypsin‐like protease in shrimp hepatopancreas (Adachi et al, 2005; Kawabata et al, 2009; Fujieda et al, 2010; Mullaivanam Ramasamy et al, 2017; Li et al, 2018a).…”

Section: Shrimp Haemocyanin and Ammonia Stress In Immune Responsementioning

confidence: 99%

“…Numerous studies have shown that shrimp haemocyanin has many immune‐related functions, including antiviral (Zhang et al, 2004; Chongsatja et al, 2007; Lei et al, 2008), phenoloxidase (Coates et al, 2013; Bris et al, 2016), agglutination (Fang et al, 2011), antibacterial (Zhang et al, 2006; Fang et al, 2011; Zhang et al, 2017), haemolytic (Zhang et al, 2009; Yan et al, 2011), anti‐tumour (Zheng et al, 2016; Liu et al, 2017) and many other immunological functions, which could be one of the reasons for its high abundance in shrimp haemolymph (Depledge & Bjerregaard, 1989; Mullaivanam Ramasamy et al, 2017). Thus, it is believed that when shrimp are invaded by pathogens under high ammonia stress, some haemocyanin degrades into antimicrobial peptides by proteases such as trypsin (Destoumieux‐Garzon et al, 2001; Li et al, 2018a) to protect shrimp from the pathogens.…”

Section: Shrimp Haemocyanin and Ammonia Stress In Immune Responsementioning

confidence: 99%

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Effects of ammonia on shrimp physiology and immunity: a review

Zhao

Yao

et al. 2020

Reviews in Aquaculture

103

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The rapid expansion in shrimp farming comes with problems such as inadequate culture technology, disease outbreak, water pollution and other environmental degradation‐related problems. Prominent among these is the level of ammonia, which has been rising steadily in the last couple of years, mainly due to farming practices and other anthropogenic activities, and therefore has had consequent effects on marine life, especially shrimp. While optimal ammonia levels are a good source of nitrogen for marine phytoplankton that increases the level of dissolved oxygen in water as well serves as food for shrimp, high levels of ammonia are harmful to shrimp. When shrimp pond ammonia levels go beyond the tolerance limits, it inhibits chitinase expression, moulting, growth, phenoloxidase and haemolymph antimicrobial activity, thereby attenuating shrimp innate immune response. In this review, we bring together recent information on the effects of ammonia stress on the growth, physiology, biochemistry, ammonia‐metabolizing enzymes and immunity of shrimp. We also propose areas of research that can be explored in the breeding of new ammonia‐tolerant and disease‐resistant shrimp with robust immune and/or physiological systems that could withstand environmental stress and pathogens.

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Biofloc-based farming of Indian white shrimp, Penaeus indicus, in recirculating aquaculture system (RAS) enriched with rotifers as feed supplement

et al. 2022

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Phenoloxidase activity in humoral plasma, hemocyanin and hemocyanin separated proteins of the giant freshwater prawn Macrobrachium rosenbergii

Cited by 23 publications

References 86 publications

Molecular isolation and expression analysis of hemocyanin isoform 2 of Macrobrachium rosenbergii

Molecular isolation and expression analysis of hemocyanin isoform 2 of Macrobrachium rosenbergii

Effects of ammonia on shrimp physiology and immunity: a review

Biofloc-based farming of Indian white shrimp, Penaeus indicus, in recirculating aquaculture system (RAS) enriched with rotifers as feed supplement

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