C-terminal domain of WSSV VP37 is responsible for shrimp haemocytes binding which can be inhibited by sulfated galactan

Sotanon, Nantharat; Saleeart, Anchulee; Rattanarojpong, Triwit; Dong, Ha Thanh; Senapin, Saengchan; Wongprasert, Kanokpan; Sarikavanij, Sukuman; Khunrae, Pongsak

doi:10.1016/j.fsi.2018.03.043

Cited by 8 publications

(9 citation statements)

References 30 publications

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“…Interestingly, Sotanon et al (2018) [71] recently found that the binding of an envelope protein of the WSSV virion, namely, VP37, to shrimp hemocytes, was impaired by preincubation of VP37 with sulfated galactan, a sulfated polysaccharide derived from red algae (Gracillaria fisheri), and this is consistent with the report of Wongprasert et al (2014) [22], who discovered that shrimp were effectively protected from WSSV infection by sulfated galactan. Sotanon et al (2018) [71] also demonstrated that VP37 might be able to recognize sulfated galactan as its binding partner and that the binding of VP37 to shrimp hemocytes might target a molecule whose structure is related to sulfated galactan. For this reason, it is possible that the VP37 of WSSV can bind with the ulvan from green algae because sulfated galactan and ulvan are the same sulfated polysaccharide in marine algae.…”

Section: Discussionsupporting

confidence: 76%

Antibacterial and Antiviral Activities of Local Thai Green Macroalgae Crude Extracts in Pacific White Shrimp (Litopenaeus vannamei)

et al. 2020

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Macroalgae are potentially excellent sources of bioactive secondary metabolites useful for the development of new functional ingredients. This study was conducted to determine the antimicrobial efficacy of the hot water crude extracts (HWCEs) of three species of local Thai green macroalgae Ulva intestinalis (Ui), U. rigida (Ur), and Caulopa lentillifera (Cl) and a commercial ulvan from U. armoricana (Ua). Chemical analysis indicated that the HWCE of Ur showed the highest sulfate content (13.9% ± 0.4%), while that of Ua contained the highest uronic acid and carbohydrate contents (41.47% ± 4.98% and 64.03% ± 2.75%, respectively), which were higher than those of Ur (32.75% ± 1.53% and 51.02% ± 3.72%). Structural analysis of these extracts by Fourier-transform infrared (FTIR) spectroscopy revealed that these HWCEs are complex with a signal at 1250 cm−1 corresponding to S=O stretching vibrations, while the signals at 850 cm−1 were attributed to the C–O–S bending vibration of the sulfate ester in the axial position. These HWCEs showed the growth suppression against some pathogenic Vibrio spp. Interestingly, the HWCEs from Ui at concentrations of 5 and 10 mg/mL completely inhibited white spot syndrome virus (WSSV) in shrimp injected with HWCE–WSSV preincubated solutions. This inhibitory effect was further confirmed by the reduction in viral loads and histopathology of surviving and moribund shrimp.

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Section: Discussionsupporting

confidence: 76%

Antibacterial and Antiviral Activities of Local Thai Green Macroalgae Crude Extracts in Pacific White Shrimp (Litopenaeus vannamei)

et al. 2020

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“…In our previous studies, we demonstrated that C-terminal domain of VP37 was able to bind with shrimp haemocytes and porcine heparin, whose structural profile is similar to that found in shrimp [10]. Moreover, the binding of VP37 can be inhibited by sulphated galactan (SG) from red seaweed [11]. This result is consistent with the report by Kanokpan et al .…”

Section: Introductionsupporting

confidence: 88%

“…The previous studies have shown that VP37 could interact with heparin, and the binding of VP37 to both shrimp haemocytes and heparin can be inhibited by sulphated galactan (SG) in a similar dose-dependent manner. This result suggested that VP37 might utilize heparin-like molecules as target molecules for viral infection [11]. Meanwhile, both molecules of heparin and SG contain a large amount of sulphate molecules, and most proteins that can bind with such molecules usually have sulphate binding sites responsible for interacting with heparin or SG [14, 35].…”

Section: Resultsmentioning

confidence: 99%

“…We used surface plasmon resonance (SPR) to investigate the interaction of VP37 wild-type and mutants with heparin sodium salt from porcine intestinal mucosa (Sigma-Aldrich, Saint Louis, MO, USA) following the procedure described by Sotanon et al . [11]. Briefly, Heparin was dissolved to 5 mg ml −1 in 20 mM sodium phosphate (pH 7.4) and 150 mM NaCl.…”

Section: Methodsmentioning

confidence: 99%

“…Furthermore, it has been found that these viral infections can also be inhibited by SG [13, 14]. Regarding the evidences that VP37 can interact with heparin and the interaction can be inhibited by SG, we therefore hypothesized that WSSV might utilize the interaction between its V37 and heparin-like molecule on shrimp cell membrane for attacking the host cells [11].…”

Section: Introductionmentioning

confidence: 99%

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Crystal structure of the C-terminal domain of envelope protein VP37 from white spot syndrome virus reveals sulphate binding sites responsible for heparin binding

Somsoros

Sangawa

Takebe

et al. 2021

Journal of General Virology

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White spot syndrome virus (WSSV) is the most virulent pathogen causing high mortality and economic loss in shrimp aquaculture and various crustaceans. Therefore, the understanding of molecular mechanisms of WSSV infection is important to develop effective therapeutics to control the spread of this viral disease. In a previous study, we found that VP37 could bind with shrimp haemocytes through the interaction between its C-terminal domain and heparin-like molecules on the shrimp cells, and this interaction can also be inhibited by sulphated galactan. In this study, we present the crystal structure of C-terminal domain of VP37 from WSSV at a resolution of 2.51 Å. The crystal structure contains an eight-stranded β-barrel fold with an antiparallel arrangement and reveals a trimeric assembly. Moreover, there are two sulphate binding sites found in the position corresponding to R213 and K257. In order to determine whether these sulphate binding sites are involved in binding of VP37 to heparin, mutagenesis was performed to replace these residues with alanine (R213A and K257A), and the Surface Plasmon Resonance (SPR) system was used to study the interaction of each mutated VP37 with heparin. The results showed that mutants R213A and K257A exhibited a significant loss in heparin binding activity. These findings indicated that the sites of R213 and K257 on the C-terminal domain of envelope protein VP37 are essential for binding to sulphate molecules of heparin. This study provides further insight into the structure of C-terminal domain of VP37 and it is anticipated that the structure of VP37 might be used as a guideline for development of antivirus agent targeting on the VP37 protein.

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Seaweed polysaccharides as potential therapeutic agents against white spot syndrome virus (WSSV): a mini review

et al. 2020

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C-terminal domain of WSSV VP37 is responsible for shrimp haemocytes binding which can be inhibited by sulfated galactan

Cited by 8 publications

References 30 publications

Antibacterial and Antiviral Activities of Local Thai Green Macroalgae Crude Extracts in Pacific White Shrimp (Litopenaeus vannamei)

Antibacterial and Antiviral Activities of Local Thai Green Macroalgae Crude Extracts in Pacific White Shrimp (Litopenaeus vannamei)

Crystal structure of the C-terminal domain of envelope protein VP37 from white spot syndrome virus reveals sulphate binding sites responsible for heparin binding

Seaweed polysaccharides as potential therapeutic agents against white spot syndrome virus (WSSV): a mini review

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