Suppression of Shrimp Melanization during White Spot Syndrome Virus Infection

Sutthangkul, Jantiwan; Amparyup, Piti; Charoensapsri, Walaiporn; Senapin, Saengchan; Phiwsaiya, Kornsunee; Tassanakajon, Anchalee

doi:10.1074/jbc.m114.605568

Cited by 54 publications

(22 citation statements)

References 44 publications

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“…Melanin has many important roles in the human body including UV-radiation absorbent (Brenner and Hearing 2008), antioxidant (Vate and Benjakul 2013), and heavy-metal absorbent properties (Cuong et al 2018). Melanization and melanin secretion help shrimp protect themselves by encapsulating pathogens and excreting them into the environment (Charoensapsri et al 2014;Sutthangkul et al 2015;Harikrishnan et al 2011). However, no studies have examined the role of melanin as a supplement in protecting shrimp from pathogen attacks.…”

Section: Introductionmentioning

confidence: 99%

Melanin-containing feedstuffs protect Litopenaeus vannamei from white spot syndrome virus

Thắng

et al. 2019

Int Aquat Res

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Viral diseases are a serious issue for the shrimp aquaculture industry. White spot syndrome virus (WSSV) has been considered one of the most dangerous pathogens infecting cultured shrimp, causing a mortality rate as high as 100% within 7-10 days of viral infection. So far, several protocols have been applied to protect shrimp against virus attacks, but their protection efficiency is very limited. In this study, for the first time, three melanin-containing feedstuffs (F1, F2, and F3) were formulated and fed to cultured shrimp to investigate the ability of melanin to protect shrimp from WSSV. The obtained results showed that F2 had a protection rate of 64% at day 7 and 62% at day 10 after virus challenge. The protection ability of the feedstuff depended on the amount of melanin consumed by shrimp. Moreover, our results also demonstrated that the transcription level of the VP28 gene, which codes for the VP28 protein, a representative for the presence of WSSV, was significantly decreased in shrimp fed F2. Taken together, our study suggests that melanincontaining diets may be applied in aquaculture to protect shrimp against WSSV infection; further, combined protocols with the simultaneous use of melanin-containing diets and other protectants should be studied and applied to increase the protection efficiency.

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Section: Introductionmentioning

confidence: 99%

Melanin-containing feedstuffs protect Litopenaeus vannamei from white spot syndrome virus

Thắng

et al. 2019

Int Aquat Res

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“…Their function has been particularly studied in the context of the melanization response, which, in insects, plays important roles in several physiological processes, including cuticle sclerotization or tanning ( 2 ), hardening of wound clots ( 3 ), and resistance to microbial infections ( 4 – 7 ). There is also convincing evidence for an antiviral role of melanization ( 8 , 9 ). The infection-induced melanotic response is initiated when pattern recognition receptors (PRRs) bind to microbial cell components, triggering the activation of a cascade of serine proteases, constituted mostly of CLIPs, which culminates in the limited proteolytic cleavage of the zymogen prophenoloxidase (PPO) into active phenoloxidase (PO), the rate-limiting enzyme in melanin biosynthetic pathways.…”

Section: Introductionmentioning

confidence: 99%

The serine protease homolog CLIPA14 modulates the intensity of the immune response in the mosquito Anopheles gambiae

Nakhleh

Christophides

Osta

2017

Journal of Biological Chemistry

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Clip domain serine protease homologs (SPHs) are positive and negative regulators of Anopheles gambiae immune responses mediated by the complement-like protein TEP1 against Plasmodium malaria parasites and other microbial infections. We have previously reported that the SPH CLIPA2 is a negative regulator of the TEP1-mediated response by showing that CLIPA2 knockdown (kd) enhances mosquito resistance to infections with fungi, bacteria, and Plasmodium parasites. Here, we identify another SPH, CLIPA14, as a novel regulator of mosquito immunity. We found that CLIPA14 is a hemolymph protein that is rapidly cleaved following a systemic infection. CLIPA14 kd mosquitoes elicited a potent melanization response against Plasmodium berghei ookinetes and exhibited significantly increased resistance to Plasmodium infections as well as to systemic and oral bacterial infections. The activity of the enzyme phenoloxidase, which initiates melanin biosynthesis, dramatically increased in the hemolymph of CLIPA14 kd mosquitoes in response to systemic bacterial infections. Ookinete melanization and hemolymph phenoloxidase activity were further increased after cosilencing CLIPA14 and CLIPA2, suggesting that these two SPHs act in concert to control the melanization response. Interestingly, CLIPA14 RNAi phenotypes and its infection-induced cleavage were abolished in a TEP1 loss-of-function background. Our results suggest that a complex network of SPHs functions downstream of TEP1 to regulate the melanization reaction.

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“…glabrata snails, the AG produces lectins also in response to parasitic infection [51]. Thus, Hcl-1 may play a role as an innate immune factor; some copper type 3 proteins possess PO activity towards melanization of pathogens [52, 53]. At the same time, protein components in the EMF of egg masses of B .…”

Section: Discussionmentioning

confidence: 99%

The Planorbid Snail Biomphalaria glabrata Expresses a Hemocyanin-Like Sequence in the Albumen Gland

Peña

Adema

2016

PLoS ONE

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The parasitic flatworm Schistosoma mansoni, causative agent of human intestinal schistosomiasis in South America, relies importantly on the freshwater snail Biomphalaria glabrata as intermediate host to achieve development of cercariae that infect humans. The recommendation from the World Health Organization (WHO) to integrate snail control in efforts to counter schistosomiasis transmission provides impetus for in depth study of B. glabrata biology. Our analysis indicates that two distinct hemocyanin-like genes (hcl-1 and hcl-2) are present in B. glabrata, a snail that uses hemoglobin for oxygen transport. Characterization of BAC clones yielded the full length hcl-1 gene, which is comprised of three functional unit (FU) domains at the amino acid level. Database searches and in silico analyses identified the second hcl gene (hcl-2), composed of six FU domains. Both genes are unusual for lacking canonical residues and having fewer FU domains than typical molluscan hemocyanins that contain 7–8 FUs. Reverse transcription PCR demonstrated that Hcl-1 is expressed in a manner that correlates with reproductive maturity in the albumen gland (AG), an immune- and reproduction-relevant organ. Immune cross-reactivity with anti-keyhole limpet hemocyanin (α-KLH) antiserum and tandem-mass spectrometry validated the presence of Hcl-1 protein in the AG and egg mass fluid (EMF). The evolutionary conservation of hemocyanin-like sequences in B. glabrata in the presence of the oxygen carrier hemoglobin, combined with our results, suggest that the Hcl-1protein has a functional role in general and/or reproductive biology. Further investigations are needed to explore Hcl-1 as a potential target for snail control.

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Suppression of Shrimp Melanization during White Spot Syndrome Virus Infection

Cited by 54 publications

References 44 publications

Melanin-containing feedstuffs protect Litopenaeus vannamei from white spot syndrome virus

Melanin-containing feedstuffs protect Litopenaeus vannamei from white spot syndrome virus

The serine protease homolog CLIPA14 modulates the intensity of the immune response in the mosquito Anopheles gambiae

The Planorbid Snail Biomphalaria glabrata Expresses a Hemocyanin-Like Sequence in the Albumen Gland

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