Vatanavicharn, Tipachai

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Alpha-2-macroglobulin is a modulator of prophenoloxidase system in pacific white shrimp Litopenaeus vannamai
(2017-03-01)
Ponprateep, Sirikwan
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Vatanavicharn, Tipachai
;
Lo, Chu Fang
;
Tassanakajon, Anchalee
;
Rimphanitchayakit, Vichien
The shrimp multifunctional protein alpha-2-macroglobulin (A2M) is abundantly expressed in plasma, highly up-regulated upon microbial infection and involved in several immune pathways such as blood clotting system, phagocytosis and melanization. Herein, the function of LvA2M from Litopenaeus vannamei on the prophenoloxidase (proPO) system is reported. The recombinant (r)LvA2M produced strongly and specifically inhibited trypsin and the PO activity in shrimp plasma in a dose-dependent manner. Silencing of LvA2M led to an increase in the PO activity in shrimp plasma although the expression of proPO-associated genes, proPO-activating enzyme (PPAE) and prophenoloxidase (proPO) but not the proPO-activating factor (PPAF) was down-regulated. In Vibrio parahaemolyticus AHPND-infected shrimp, the LvA2M activity was suppressed in an early phase of infection while the PO activity was increased. Thus, the proPO-activating system was regulated by the LvA2M.
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Plasmolipin, PmPLP1, from Penaeus monodon is a potential receptor for yellow head virus infection
(2018-11-01)
Matjank, Watchalaya
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Ponprateep, Sirikwan
;
Rimphanitchayakit, Vichien
;
Tassanakajon, Anchalee
;
Somboonwiwat, Kunlaya
Plasmolipin has been characterized as a cell entry receptor for mouse endogenous retrovirus. In black tiger shrimp, two isoforms of plasmolipin genes, PmPLP1 and PmPLP2, have been identified from the Penaeus monodon EST database. The PmPLP1 is highly up-regulated in yellow head virus (YHV)-infected shrimp. Herein, the function of PmPLP1 is shown to be involved in YHV infection. The immunoblotting and immunolocalization showed that the PmPLP1 protein was highly expressed and located at the plasma membrane of gills from YHV-infected shrimp. Moreover, the PmPLP1 expressed in the Sf9 insect cells resided at the cell membrane rendering the cells more susceptible to YHV infection. Using the ELISA binding and mortality assays, the synthetic external loop of PmPLP1 was shown to bind the purified YHV and neutralize the virus resulting in the decrease in YHV infection. Our results suggested that the PmPLP1 was likely a receptor of YHV in shrimp.
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PmVRP15, a novel viral responsive protein from the black tiger shrimp, Penaeus monodon, promoted white spot syndrome virus replication
(2014-03-17)
Vatanavicharn, Tipachai
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Prapavorarat, Adisak
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Jaree, Phattarunda
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Somboonwiwat, Kunlaya
;
Tassanakajon, Anchalee
Suppression subtractive hybridization of Penaeus monodon hemocytes challenged with white spot syndrome virus (WSSV) has identified the viral responsive gene, PmVRP15, as the highest up-regulated gene ever reported in shrimps. Expression analysis by quantitative real time RT-PCR revealed 9410-fold up-regulated level at 48 h post WSSV injection. Tissue distribution analysis showed that PmVRP15 transcript was mainly expressed in the hemocytes of shrimp. The full-length cDNA of PmVRP15 transcript was obtained and showed no significant similarity to any known gene in the GenBank database. The predicted open reading frame of PmVRP15 encodes for a deduced 137 amino acid protein containing a putative transmembrane helix. Immunofluorescent localization of the PmVRP15 protein revealed it accumulated around the nuclear membrane in all three types of shrimp hemocytes and that the protein was highly up-regulated in WSSV-infected shrimps. Double-stranded RNA interference-mediated gene silencing of PmVRP15 in P. monodon significantly decreased WSSV propagation compared to the control shrimps (injected with GFP dsRNA). The significant decrease in cumulative mortality rate of WSSV-infected shrimp following PmVRP15 knockdown was observed. These results suggest that PmVRP15 is likely to be a nuclear membrane protein and that it acts as a part of WSSV propagation pathway. Copyright: © 2014 Vatanavicharn et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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Two plasmolipins from the black tiger shrimp, Penaeus monodon and their response to virus pathogens
(2012-01-01)
Vatanavicharn, Tipachai
;
Pongsomboon, Siriporn
;
Tassanakajon, Anchalee
Two isoforms of plasmolipin were initially identified from the black tiger shrimp (Penaeus monodon) EST database and completed using 5' RACE to reveal complete cDNAs of 558. bp (PmPLP1) and 537. bp (PmPLP2) with 87% nucleotide sequence identity. The deduced amino acid sequences contained four-transmembrane domains and showed the highest amino acid identity (49% and 51%, respectively) to the honey bee (Apis mellifera) chemokine-like factor (CKLF), with a very similar hydrophobic pattern to other plasmolipins. Transcripts of PmPLP1 and PmPLP2 were observed in all tested shrimp tissues with the highest expression levels in the gill and epipodite for PmPLP1 and in the hemocytes and antennal gland for PmPLP2. PmPLP1 transcript levels were significantly upregulated in hemocytes at 24 and 72. h post infection (hpi) with yellow head virus (YHV) (7.4- and 14.7- fold, respectively), but only after 72. hpi by white spot syndrome virus (WSSV). In contrast, PmPLP2 was only slightly (but statistically significant) up-regulated with YHV and WSSV. Thus, PmPLPs have the potential to be a part of viral infection mechanism or defense response. This is the first characterization of a plasmolipin gene in crustaceans. © 2012 Elsevier Ltd.

Vatanavicharn, Tipachai

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