PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “Penaeus monodon”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 19 recordsLinked to original sources
PubMed1991

The midgut chymotrypsins of shrimps (Penaeus monodon, Penaeus japonicus and Penaeus penicillatus).

The midgut chymotrypsins (EC 3.4.4.5) of three species of shrimps, Penaeus monodon, Penaeus japonicus and Penaeus penicillatus were purified and studied in detail to clarify previous ambiguity in their identification. In each of the species there are two major forms of chymotrypsin, both single-chained with three disulfide bonds. One has a pI of 3.2 and Mr 27,000 or 28,000, while the other has a pI of 3.0 and Mr 25,000 or 26,000. The N-terminal amino acid sequences of the P. monodon enzymes are homologous to those of the crab (Uca pugilator) collagenase and to the other chymotrypsins. However, the active sites of the shrimp chymotrypsins are different from that of the well studied bovine alpha-chymotrypsin in some respects: (1) in spite of showing the typical specificity of chymotrypsin, the shrimp enzymes are more stringently selective for substrates with extended polypeptide chain; (2) some titration agents of alpha-chymotrypsin, including t-cinnamoylimidazole, 4-nitrophenyl guanidinobenzoate and its fluorescent derivative, do not react with the shrimp enzymes, neither do some of the alpha-chymotrypsin inhibitors: Tosyl-PheCH2Cl, methyl-4-nitrobenzenesulfonate and benzeneboronic acid; (3) the shrimp chymotrypsins are more reactive than the bovine enzyme toward native protein substrates including collagen; (4) the kinetic-salt-effects of the shrimp enzyme toward N-succinyl- and acetyl-Ala-Ala-Pro-Phe-4-nitroanilide mainly reflect electrostatic rather than hydrophobic interactions between the substrates and the enzyme. The shrimp enzymes are acid-labile but resistent to autolysis. Our results suggest that most Crustacea decapods contain chymotrypsins as one of the major digestive endopeptidases.

Amino Acid Sequence↗
PubMed1996

Toxic effects of blooms of marine species of Oscillatoriales on farmed prawns (Penaeus monodon, Penaeus japonicus) and brine shrimp (Artemia salina).

Benthic and planktonic blooms of species of Oscillatoriales coincided with mortalities of Penaeus monodon during four episodes at Australian prawn farms. Oscillatoria corakiana was the dominant planktonic species at 65-90,000 cells/ml, but Spirulina sp., Lyngbya sp., Oscillatoria sp. and Nodularia sp. were also identified from the water column, benthic layers or surface mats. The levels and variety of Vibrionaceae in prawn tissue, suggest that mortalities were caused by secondary infections of bacteria. However, experimental results indicate that toxicity of the blooms of Oscillatoriales was the primary cause of disease. Pond water and extracts from a tank culture of benthic Oscillatoriales caused mortalities when injected into P. monodon and P. japonicus. Immersion of artemia in extracts from the tank culture also caused mortalities, with L.D50 values for the supernatant extract of 70 mg/litre for artemia cysts and 50 mg/litre for adult artemia, and LD50 values for the pellet extract of 110 mg/litre for artemia cysts and 200 mg/litre for adult artemia. Experiments with artemia suggested the blooms of Oscillatoriales produced water-soluble, heat-labile toxin/s. Mortalities may have been caused by a neurotoxin because: (a) there was a lack of histopathological evidence of damage to the digestive tracts of prawns during each episode; and (b) artemia cysts immersed in extracts of Oscillatoriales died before they developed digestive tracts. PSP toxin, anatoxin-a, homoanatoxin-a and microcystins were not detected when pond water from a diseased pond was tested. It is proposed that sub-lethal levels of toxin weakened the prawns, causing reduced feeding behaviour and an impaired immune system. As a result, prawns were prone to secondary infection by pathogenic bacteria. Because Oscillatoriales are ubiquitous in prawn farms, the findings have significant implications for the assessment of disease in the prawn farming industry.

Animals↗
PubMed2002

Joint action of elevated ambient nitrite and nitrate on hemolymph nitrogenous compounds and nitrogen excretion of tiger shrimp Penaeus monodon.

Penaeus monodon (12.13+/-1.14 g) exposed individually to six different nitrite and nitrate regimes (0.002, 0.36 and 1.46 mM nitrite combined with 0.005 and 7.32 mM nitrate), at a salinity of 25 ppt, were examined for hemolymph nitrogenous compounds and whole shrimp's nitrogen excretions after 24 h. Nitrogen excretion increased directly with ambient nitrite and nitrate. Hemolymph nitrite, nitrate, urea and uric acid levels increased, while hemolymph ammonia, oxyhemocyanin and protein were inversely related to ambient nitrite. Exposure of P. monodon to elevated nitrite in the presence of 7.32 mM nitrate did not alter hemolymph nitrite, ammonia, uric acid, oxyhemocyanin and protein levels, but caused an increase in hemolymph nitrate and a decrease in hemolymph urea as compared to exposure to elevated nitrite only. Following exposure to elevated nitrite, nitrite was oxidized to nitrate and P. monodon showed uricogenesis and uricolysis. The shrimp also used strategies to avoid joint toxicities of nitrite and metabolic ammonia by removing ammonia or reducing ammonia production under the stress of elevated nitrite.

Ammonia↗
PubMed1998

Colourimetric PCR-based detection of monodon baculovirus in whole Penaeus monodon postlarvae.

The development of a nested polymerase chain reaction (PCR) assay is described to detect low concentrations of monodon baculovirus (MBV) DNA from total Penaeus monodon postlarval DNA. A modified DNA extraction procedure was also developed to circumvent problems associated with co-purification of PCR inhibitors in total DNA extracted from whole postlarvae. This method involved mechanical disruption of frozen prawn material immediately followed by phenol extraction at high temperature. An assessment of the sensitivity of the assay demonstrated detection down to eight viral genome equivalents. The PCR was shown to be specific for MBV DNA by not amplifying prawn DNA or DNA preparations of Baculovirus penaei (BP), white spot baculovirus (WSBV), bennettae baculovirus and insect Autographica californica nuclear polyhedrosis virus (NPV). A colourimetric method of PCR product detection was used to simplify final analysis.

Animals↗
PubMed2006

Influence of Vibrio parahaemolyticus MTCC 451 on the levels of ascorbic acid and histamine in Penaeus monodon (Fabricius).

Juvenile shrimps (Penaeus monodon) weighing about 15-20 gms were procured from the grow-out ponds and reared under laboratory conditions. They were challenged with Vibrio parahaemolyticus MTCC 451 and their LD50 value was evaluated. The ascorbic acid and the histamine activity of both the control and experimental groups were assessed. The results showed a marked decline in both the parameters at all intervals. This reveals the pathogenesis of the inoculated bacterial strain, which affects the defense mechanism by reducing the glutathione content by the decreased level of ascorbic acid and letharginess by the decreased histamine content of the experimental prawns.

Animals↗
PubMedDate not supplied

Penaeus monodon (tiger shrimp) hemocyanin: subunit composition and thermostability.

Penaeus monodon (class Crustacea, order Decapoda) is one of the largest shrimps of the Penaeidea family from the Indo-West Pacific region. The dioxygen-transporting protein hemocyanin, isolated from the hemolymph of this invertebrate, is composed of three 75-76 kDa structural/functional subunits designated as Pm1, Pm2 and Pm3. The N-terminal sequences of the chains were determined and compared with those of other decapodan hemocyanin subunits. Pm2 and Pm3 are highly homologous and electrophoretically undistinguishable polypeptides. In comparison to Pml, they have an extension of six residues. Pm1 is closely related to the subunit Pv2 of the Penaeus vannamei hemocyanin. Probably, subunits like Pm1 and Pv2 are family-specific for the Penaeidea hemocyanins and the other subunits are species-specific. Comparison of N-terminal sequences of respiratory proteins from the sub-orders Natantia and Reptantia demonstrated family- and sub-order-specific sequences. A melting point of 69 degrees C, lower than those for the di-hexameric decapodan hemocyanins, was determined from the temperature dependence of ellipticity of the mono-hexameric Penaeus monodon hemocyanin. Thermostability of decapodan hemocyanins depends on their aggregation state.

Amino Acid Sequence↗
PubMed2005

Quaternary structure and functional properties of Penaeus monodon hemocyanin.

The hemocyanin of the tiger shrimp, Penaeus monodon, was investigated with respect to stability and oxygen binding. While hexamers occur as a major component, dodecamers and traces of higher aggregates are also found. Both the hexamers and dodecamers were found to be extremely stable against dissociation at high pH, independently of the presence of calcium ions, in contrast to the known crustacean hemocyanins. This could be caused by only a few additional noncovalent interactions between amino acids located at the subunit-subunit interfaces. Based on X-ray structures and sequence alignments of related hemocyanins, the particular amino acids are identified. At all pH values, the p50 and Bohr coefficients of the hexamers are twice as high as those of dodecamers. While the oxygen binding of hexamers from crustaceans can normally be described by a simple two-state model, an additional conformational state is needed to describe the oxygen-binding behaviour of Penaeus monodon hemocyanin within the pH range of 7.0 to 8.5. The dodecamers bind oxygen according to the nested Monod-Whyman-Changeaux (MWC) model, as observed for the same aggregation states of other hemocyanins. The oxygen-binding properties of both the hexameric and dodecameric hemocyanins guarantee an efficient supply of the animal with oxygen, with respect to the ratio between their concentrations. It seems that under normoxic conditions, hexamers play the major role. Under hypoxic conditions, the hexamers are expected not to be completely loaded with oxygen. Here, the dodecamers are supposed to be responsible for the oxygen supply.

Allosteric Regulation↗
PubMed1999

Molecular cloning and characterization of prophenoloxidase in the black tiger shrimp, Penaeus monodon.

A cDNA encoding shrimp, Penaeus monodon, prophenoloxidase (proPO) was obtained by screening a hemocyte library by plaque hybridization using a proPO cDNA fragment from freshwater crayfish, Pacifastaceus leniusculus, as a probe. The 3,002 bp cDNA contains an open reading frame of 2,121 bp and a 881 bp 3'-untranslated region. The molecular mass of the deduced amino acid sequence (688 amino acids) is 78,700 Da with an estimated pI of 5.8. Two putative copper binding sites are present and they have a highly conserved sequence around these sites. No signal peptide was detected in the shrimp proPO, as has been previously shown to be the case for all arthropod proPOs cloned so far. The cleavage site of zymogen activation is likely to be between Arg 44 and Val 45. A tentative complement-like motif (GCGWPQHM) is also present. Shrimp proPO mRNA is synthesized in the hemocytes and not in the hepatopancreas. Comparison of amino acid sequences showed that shrimp proPO is more closely related to another crustacean proPO, namely crayfish, than to the insect proPOs.

Amino Acid Sequence↗
PubMed1993

Specific phosphorylation of membrane proteins of Mr 44,000 and Mr 32,000 by the autophosphorylated insulin receptor from the hepatopancreas of the shrimp Penaeus monodon (Crustacea: Decapoda).

The insulin receptor, purified from the hepatopancreas of the shrimp Penaeus monodon, is a hydrophobic heterodimer of subunits with relative masses (Mr) of 70,000 and 58,000, as estimated by FPLC on Superose 12 and SDS-PAGE. Only the subunit of Mr 70,000 was autophosphorylated after the addition of insulin. The autophosphorylation occurred specifically at Tyr residues, as demonstrated by the specific subsequent dephosphorylation by the phosphotyrosyl protein phosphatase from the hepatopancreas of the shrimp Penaeus monodon. Proteins of Mr 44,000 and Mr 32,000 on the plasma membrane from the hepatopancreas of the shrimp Panaeus monodon were phosphorylated by the autophosphorylated insulin receptor from the shrimp hepatopancreas, but not by that from the human placenta. The detergent, Triton X-100, caused noticeable enhancement of the autophosphorylation of both shrimp and human insulin receptors.

Amino Acid Sequence↗
PubMed2005

A new RNA virus found in black tiger shrimp Penaeus monodon from Thailand.

A new, apparently innocuous virus was found while investigating the cause of monodon slow growth syndrome (MSGS) in cultured black tiger shrimp (Penaeus monodon). It was identified via plasmid vector clones of E. coli containing randomly amplified cDNA fragments produced from total nucleic acid extracts of hemolymph from MSGS shrimp. Of 421 clones, 30 that failed to give positive dot blot hybridization with a digoxigenin (DIG)-labeled shrimp DNA probe were sequenced and compared to GenBank records. Of these, 22 corresponded to known shrimp DNA records. Of eight that did not, one (20A) showed significant deduced amino acid sequence similarity to RNA-dependent RNA polymerases (RdRp) of the viruses in the family Luteoviridae and alignment revealed commonly conserved amino acids including a GDD motif believed to be at the enzyme active site. However, phylogenetic analysis showed that the virus sequence did not cluster with the Luteoviridae or other known RNA virus sequences. Thus, in accordance with frequent practice, it was named according to the area where it was first collected as Laem-Singh virus (LSNV). In situ hybridization with a DIG-labeled 20A insert revealed strong cytoplasmic staining confined to the lymphoid organ (LO), the heart and hepatopancreatic connective tissue in both normal and MSGS shrimp. RT-PCR assays based on the 20A clone sequence also gave positive results with both normal and MSGS shrimp. Transmission electron microscopy (TEM) of LO tissue revealed viral-like particles of approximately 27 nm diameter (within the Luteoviridae size range) in locations that matched those of positive in situ hybridization reactions in parallel samples. Although not directly associated with MSGS in Penaeus monodon, the presence or effect of this virus with other crustacean species is presently unknown.

Amino Acid Sequence↗
PubMed2005

Monoclonal antibodies specific to haemocytes of black tiger prawn Penaeus monodon.

Monoclonal antibodies specific to haemocytes of Penaeus monodon were generated from a mouse immunized with a mixture of SDS-treated and formalin-fixed haemocytes. Hybridoma clones were selected by immunohistochemistry against fixed haemocytes, heart, lymphoid organ, and haemopoietic tissue, and Western blot against haemocyte extract and haemolymph. Sixteen monoclonal antibodies specific to haemocytes were obtained and could be divided into six groups according to their binding capacities to various haemocyte proteins in Western blot analyses, 102, 43, approximately 20, 61, 175 and approximately 230 kDa, and their differences in recognition of haemocyte sub-populations. The first group of antibodies strongly recognized a small subset of semi-granulocytes (SG) and hyalinocytes (H) but occasionally stained lightly a very small population of granulocytes (G). The antibodies also bound to a group of cells in haemopoietic tissue as well as cells located at the inner layers of the tubules in the lymphoid organ but not in the spheroid. The second group of antibodies strongly bound to a large sub-population of G and SG with coarse granules but did not bind to most of the H. This group of antibodies also cross-reacted with cells in the outer layer of the tubules in the lymphoid organ. The third group of antibodies recognized all G and only a small portion of SG. The fourth, fifth and sixth groups bound to sub-populations of G, SG and H in similar proportions. None of the antibodies showed any cross-reactivity to other components in haemolymph. The common antigens recognized by the first and the second groups of antibodies in the haemopoietic tissue and the lymphoid organ may reflect relationships among these organs in the development of the sub-populations of G and SG. Haemopoietic tissue may be the site for haemocyte production and the lymphoid organ may be the site for further differentiation of at least two different lines of haemocytes.

Animals↗
PubMed1992

Estimation of the dietary riboflavin required to maximize tissue riboflavin concentration in juvenile shrimp (Penaeus monodon).

The riboflavin requirements of marine shrimp (Penaeus monodon) were evaluated in a 15-wk feeding trial. Juvenile shrimp (initial mean weight, 0.13 +/- 0.05 g) were fed purified diets containing seven levels (0, 8, 12, 16, 20, 40 and 80 mg/kg diet) of supplemental riboflavin. There were no significant differences in weight gains, feed efficiency ratios and survival of shrimp over the dietary riboflavin range. The riboflavin concentrations in shrimp bodies increased with the increasing vitamin supplementation. Hemolymph (blood) glutathione reductase activity coefficient was not a sensitive and specific indicator of riboflavin status of the shrimp. The dietary riboflavin level required for P. monodon was found to be 22.3 mg/kg diet, based on the broken-line model analysis of body riboflavin concentrations. Shrimp fed unsupplemented diet (riboflavin concentration of 0.48 mg/kg diet) for 15 wk showed signs of deficiency: light coloration, irritability, protuberant cuticle at intersomites and short-head dwarfism.

Animals↗
PubMed2002

Identification of two distinct molt-inhibiting hormone-related peptides from the giant tiger prawn Penaeus monodon.

Six peptides belonging to the crustacean hyperglycemic hormone (CHH) family were isolated from extracts of the sinus glands of the giant tiger prawn Penaeus monodon by reverse-phase high-performance liquid chromatography. These were designated Pem-SGP-A to Pem-SGA-F (Pem, Penaeus monodon; SGP, sinus gland peptide) and their amino-terminal amino acid sequences were analyzed. Five of the 6 peptides (Pem-SGP-A, -B, -D, -E, and -F) exhibited similar amino acid sequences to those of CHH peptides that had been characterized previously from the same prawn species by the other research groups, while 1 peptide (Pem-SGP-C) exhibited a novel sequence. Pem-SGP-C showed sequence similarity to known putative molt-inhibiting hormones (MIHs), particularly to an MIH from the kuruma prawn Penaeus japonicus, and less similarity to the CHHs determined thus far. Two similar complementary DNAs encoding Pem-SGP-C were cloned and found to encode very similar but distinct peptides, which were named Pem-SGP-C1 and Pem-SGA-C2. The open reading frame of each cDNA consisted only of a signal peptide and an MIH-like peptide. We also cloned 2 corresponding genes, both of which consisted of 3 exons and 2 introns. Analyses by reverse transcriptase polymerase chain reaction demonstrated that both Pem-SGP-C1 and Pem-SGP-C2 transcripts were detected only in cDNA synthesized using total RNA from the eyestalk but not in that from brain, thoracic ganglia, abdominal ganglia, abdominal muscle, hepatopancreas, or heart tissue of P. monodon.

Journal Article↗
PubMed2000

The Penaeus monodon Chitinase 1 Gene Is Differentially Expressed in the Hepatopancreas During the Molt Cycle.

We have isolated a full-length chitinase complementary DNA from the tiger shrimp Penaeus monodon that encodes a 621 amino acid protein possessing the functional domains of the chitinase protein family. The Penaeus monodon chitinase 1 (PmChi-1) gene product is 81.8% identical to a chitinase 1 protein expressed in the hepatopancreas of Penaeus japonicus. Analysis by reverse transcription-polymerase chain reaction (RT-PCR) indicates that PmChi-1 messenger RNA is detectable in the hepatopancreas and the gut. PmChi-1 expression during the molt cycle fluctuates markedly, with lowest mRNA levels at stages A(1), C, and D(3); there is a dramatic increase in transcript abundance at the D(2) stage. Using the same tissues and molt stages, RT-PCR analyses of genes encoding other digestive enzymes (trypsin, chymotrypsin, and cathepsin L), a muscle structural protein (tropomyosin II), and housekeeping proteins (elongation factor II and GTP-binding protein) indicate that PmChi-1 is expressed in a distinct tissue-specific and stage-specific manner. The other digestive enzyme genes are expressed in a similar spatiotemporal pattern, but none exhibited a dramatic increase in transcript abundance at stage D(2). Increased expression of PmChi-1 at D(2) suggests that hepatopancreas-expressed chitinase is involved in the degradation of endogenous chitin in the gut peritrophic membrane prior to molting.

Journal Article↗
PubMed1991

The carotenoids of wild and blue disease affected farmed tiger shrimp (Penaeus monodon, Fabricus).

1. The main carotenoids in wild Penaeus monodon exoskeleton were astaxanthin di- and mono-esters, astaxanthin, and beta-carotene. 2. Wild P. monodon exoskeleton contained on average 26.3 ppm total carotenoid; normally pigmented farmed shrimp had a similar concentration (25.3 ppm). 3. Exoskeletons of farmed "blue" P. monodon (i.e. blue-coloured, as opposed to the normally red-blue/black banded shrimp) contained significantly less total carotenoid (4.3-7 ppm). The only major carotenoid being astaxanthin. 4. Commercially available diets contained only trace quantities of canthaxanthin. 5. Nutritional deficiency with respect to carotenoids is suggested as the cause of blue disease in farmed P. monodon.

Animals↗
PubMed2000

Study on the free amino acid levels in the hemolymph, gill, hepatopancreas and muscle of Penaeus monodon exposed to elevated ambient ammonia.

Tiger shrimp Penaeus monodon following 24 h exposure to 0.002 (control), 0.072 and 0.718 mM ammonia were examined for the free amino acid (FAA), ammonia and urea levels in the hemolymph, gill, hepatopancreas and muscle. Control shrimps contained total FAA in hemolymph (1.19 µmol ml(-1)), gill (21.81 µmol g(-1)), hepatopancreas (100.81 µmol g(-1)) and muscle (239.54 µmol g(-1)). Glycine and arginine were the major contributors to the total FAA pool, and made up of 90% of the total FAA in the muscle of P. monodon. The total FAA level in the hemolymph increased directly with ambient ammonia, whereas the total FAA level in the hepatopancreas was inversely related to ambient ammonia. No significant difference of total FAA was observed in the gill and muscle among the shrimps in three treatments. Ammonia level increased by 160% in hemolymph, 105% in gill, 236% in hepatopancreas and 68% in muscle for the shrimps exposed to 0.718 mM ammonia. Urea and ornithine in the hepatopancreas increased by 107 and 1446%, whereas arginine level in the hepatopancreas decreased by 50% for the 0.718 mM ammonia-exposed shrimps. Decreases of arginine and other FAA with a concomitant increase of ornithine and urea level in the hepatopancreas indicated catabolism of FAA and ureogenesis. Increases of ammonia, urea, taurine, glutamine, proline, alanine, glycine and asparagine in the hemolymph revealed a intracellular osmoregulation for P. monodon under the stress of ambient ammonia at 0.718 mM.

Journal Article↗
PubMed2002

Multiple viral infection in Penaeus monodon shrimp postlarvae in an Indian hatchery.

Moribund Penaeus monodon postlarvae (PL8-PL10) in a hatchery in India were found to be simultaneously infected by 3 different viruses. They were highly infected with monodon baculovirus (MBV) and hepatopancreatic parvovirus (HPV) by histology and with white spot syndrome virus (WSSV) by non-nested polymerase chain reaction (PCR). Apparently healthy postlarvae tested from the same hatchery were positive for MBV and WSSV by nested PCR only. Tissue sections of such postlarvae did not show any histopathological changes. The simultaneous occurrence of these 3 viruses in hatchery-reared postlarval P. monodon is being reported for the first time.

Animals↗