Publications by authors named "Rungrat Jitvaropas"

5 Publications

  • Page 1 of 1

Comparative genome characterization of Leptospira interrogans from mild and severe leptospirosis patients.

Genomics Inform 2021 Sep 30;19(3):e31. Epub 2021 Sep 30.

Department of Biochemistry, Faculty of Medicine, Chulalongkorn University, Bangkok 10330, Thailand.

Leptospirosis is a zoonotic disease caused by spirochetes from the genus Leptospira. In Thailand, Leptospira interrogans is a major cause of leptospirosis. Leptospirosis patients present with a wide range of clinical manifestations from asymptomatic, mild infections to severe illness involving organ failure. For better understanding the difference between Leptospira isolates causing mild and severe leptospirosis, illumina sequencing was used to sequence genomic DNA in both serotypes. DNA of Leptospira isolated from two patients, one with mild and another with severe symptoms, were included in this study. The paired-end reads were removed adapters and trimmed with Q30 score using Trimmomatic. Trimmed reads were constructed to contigs and scaffolds using SPAdes. Cross-contamination of scaffolds was evaluated by ContEst16s. Prokka tool for bacterial annotation was used to annotate sequences from both Leptospira isolates. Predicted amino acid sequences from Prokka were searched in EggNOG and David gene ontology database to characterize gene ontology. In addition, Leptospira from mild and severe patients, that passed the criteria e-value < 10e-5 from blastP against virulence factor database, were used to analyze with Venn diagram. From this study, we found 13 and 12 genes that were unique in the isolates from mild and severe patients, respectively. The 12 genes in the severe isolate might be virulence factor genes that affect disease severity. However, these genes should be validated in further study.
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http://dx.doi.org/10.5808/gi.21037DOI Listing
September 2021

An investigation of antimicrobial and wound healing potential of Allium ascalonicum Linn.

J Med Assoc Thai 2015 Mar;98 Suppl 2:S22-7

Background: The pharmacological properties of Allium ascalonicum Linn., commonly called shallot, have been reported as including those that are antibacterial and antioxidant.

Objective: The present study aimed to evaluate the antimicrobial effect and wound-healing activity ofthe ethanolic extracts of Allium ascalonicum Linn. (AAE).

Material And Method: The antimicrobial activity of AAE was tested in vitro against using the disc diffusion method and a broth micro-dilution technique to determine the minimal inhibition concentrations (MIC) and the minimal microbicidal concentrations (MMC). Wound-healing activity of the extract was performed on rat test subjects.

Results: The AAE showed potential antimicrobial activity by inhibiting gram-positive bacteria Staphylococcus epidermidis and Bacillus subtilis ATCC 6633. MIC and MMC varied from 25-50 mg/ml and 25-200 mg/ml, respectively. After surgery 14 days, wound contractions oftreated groups and standard group were 78.61 +/- 1.20%, 78.55 +/- 1.93% and 100%, respectively; but, in the control group, wound contraction was 64.90 +/- 3.55%. Histological studies showed the complete epidermis and found the collagen fibers and fibroblasts as similar appearance as standard group in dermis. The results of histological evaluation have confirmed remarkable wound-healing activities of AAE.

Conclusion: Taken together the present study provides evidence that AAE extract processes antimicrobial and wound-healing activities.
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March 2015

Antioxidant, antimicrobial and wound healing activities of Boesenbergia rotunda.

Nat Prod Commun 2012 Jul;7(7):909-12

Department of Preclinical Science, Faculty of Medicine, Thammasat University, Rangsit Campus, Khlong Luang, Pathum Thani, 12120 Thailand.

The ethanolic extract of Boesenbergia rotunda (L.) Mansf was studied for its wound-healing potential. Since wound healing is interrelated with microbial infection and reactive oxygen species (ROS), this study was conducted to evaluate the antimicrobial and antioxidant activity of B. rotunda. The antimicrobial activity of B. rotunda was studied against six bacterial and two yeast strains using disc diffusion, minimum inhibitory concentration (MIC), and minimum microbicidal concentration (MMC). The B. rotunda extract displayed potential antimicrobial and antifungal activities by inhibiting the Gram-positive bacteria Staphylococcus aureus (ATCC 25923), S. epidermidis, and Bacillus subtilis (ATCC 6633), and the yeasts Candida albicans (ATCC 10231), and Saccharomyces cerevisiae. MIC and MMC values varied from 0.04 to 25 mg/mL and from 0.16 to 25 mg/mL, respectively. The antioxidant activity of B. rotunda was evaluated by measuring the Ferric Reducing/Antioxidant Power (FRAP) and DPPH free radical scavenging activity. The FRAP and DPPH values were 22.2 microM/microg and 76.3 mg/mL, respectively. In the wound-healing studies, the topical application of the B. rotunda extract indicated a significantly increased percentage of wound contraction on day 12 compared with the control group. Histological studies showed the complete epidermis and found collagen fibers and hair follicles in the dermis. The results of the present study support the continued and expanded utilization of B. rotunda in Thai folk medicine.
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July 2012

Functional characterization of a masquerade-like serine proteinase homologue from the black tiger shrimp Penaeus monodon.

Comp Biochem Physiol B Biochem Mol Biol 2009 Jul 26;153(3):236-43. Epub 2009 Mar 26.

Shrimp Molecular Biology and Genomics Laboratory, Department of Biochemistry, Faculty of Science, Chulalongkorn University, Bangkok 10330, Thailand.

A cDNA encoding a masquerade-like serine proteinase homologue (PmMasSPH) from the black tiger shrimp, Penaeus monodon, has been cloned and characterized. The transcript of PmMasSPH is induced in response to Vibrio harveyi infection. To further characterize the function(s) of the protein, (i) the N-terminal region comprising the glycine-rich repeats and the clip domain, and (ii) the C-terminal SP-like domain of the PmMasSPH were separately cloned into the pET-28b(+) expression vector and transformed into Escherichia coli Rosetta (DE3). The two recombinant proteins were then assayed for various biological functions; proteinase activity, hemocyte adhesion, bacterial binding, bacterial clearance and antimicrobial activity. The C-terminal SP-like domain lacks proteolytic activity but mediates hemocyte adhesion and displays binding activity to the shrimp pathogenic bacterium, V. harveyi and specific binding to the bacterial cell wall component, lipopolysaccharide (LPS). The N-terminal region exhibited in vitro antimicrobial activity against Gram-positive bacteria. In addition, the in vivo study revealed the opsonic activity of the PmMasSPH protein as shown by a higher bacterial clearance rate of V. harveyi coated with the recombinant proteins as compared with V. harveyi only. The results suggest that the PmMasSPH protein is a multifunctional immune molecule in shrimp defense.
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http://dx.doi.org/10.1016/j.cbpb.2009.03.007DOI Listing
July 2009

Molecular cloning, characterization and expression of a masquerade-like serine proteinase homologue from black tiger shrimp Penaeus monodon.

Fish Shellfish Immunol 2007 May 1;22(5):535-46. Epub 2006 Aug 1.

National Center for Genetic Engineering and Biotechnology (BIOTEC), National Science and Technology Development Agency (NSTDA), 113 Paholyothin Road, Klong1, Klong Luang, Pathumthani 12120, Thailand.

A full-length cDNA of a masquerade-like serine proteinase homologue (PmMasSPH) of Penaeus monodon was cloned and characterized by rapid amplification cDNA end (RACE) method. The complete cDNA sequence of 1958bp contains an open reading frame (ORF) of 1572bp, encoding a 523 amino acid protein including a 19 amino acid signal peptide. The calculated molecular mass of the mature protein (504 amino acids) is 51.58kDa with an estimated pI of 4.86. PmMasSPH has most of the structural characteristics of insect prophenoloxidase activating factors (PPAFs) (the N-terminal clip domain and the C-terminal serine proteinase-like domain) but in the N-terminal region there are extensive glycine-rich repeats (LGGQGGG). Sequence comparison showed that the deduced amino acid of PmMasSPH has an overall similarity of 69%, 68% and 61% to those of Apis mellifera PPAF, Callinectes sapidus PPAF and Tenebrio molitor PPAF, respectively. A neighbour-joining tree revealed a clear differentiation of each species and also indicated that PmMasSPH and C. sapidus PPAF are closely related phylogenetically. In situ hybridisation and real-time RT-PCR analyses showed that PmMasSPH transcript in haemocytes of P. monodon increased within 24h after Vibrio harveyi injection.
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http://dx.doi.org/10.1016/j.fsi.2006.07.004DOI Listing
May 2007
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