Office : School of Biology, Institute of Science, Suranaree University of Technology 111 University Ave, Muang District, Nakhon Ratchsima, 30000 Thailand

Phone : +66 (0)44 22 6187

E-mail : wipa@sut.ac.th

Education :

1995-1999 Ph.D. (Biochemistry), The University of Edinburgh, UK.
1992-1994 M.Sc. (Biochemistry), Mahidol University
1987-1992 B.Sc. (Genetics), Chulalongkorn University                       

Work experience :

February 2015 – Present  Full Professor of Biochemistry (Awaiting official endorsement by His Majesty King Maha Vajiralongkorn)
2007 – Present Associate Professor, Suranaree University of Technology
2004 – 2007 Assistant Professor, Suranaree University of Technology
1999 – 2000 Post-Doctoral Research Fellow, Membrane Biology Group, The University of Edinburgh, U.K.
1994 – 2004 Lecturer, Suranaree University of Technology (Paid leave of absence for Ph.D. study and postdoctoral research in the UK from 1995-2000)

Scholarships/Awards : 

Research Interests : 

1. Recycling of chitin biomass by marine Vibrios. Chitin is the most abundant biopolymer in marine ecosystems. However, there is no accumulation of chitin in the ocean-floor sediments, since marine bacteria Vibrios are mainly responsible for a rapid turnover of chitin biomaterials. V. harveyi is a fast growing bioluminescent bacterium through its adaptive ability to grow under anaerobic and respiratory conditions. Therefore, V. harveyi contributes significantly to a rapid turnover of chitin in marine biosphere. The catabolic pathway of chitin by V. harveyi involves chitin attachment and degradation, followed by chitooligosaccharide uptake across the bacterial membranes, and catabolism of the transport products to fructose-6-phosphate, acetate and NH₃. The chitin utilization machinery of V. harveyi is expected to work efficiently and the controlled step for fast energy production by this bacterium is determined by how fast the chitin degradation products can be generated, and further transported into the cells. To understand the molecular mechanism of chitin degradation, and chitin transport will open up the knowledge to understand why V. harveyi can utilize chitin so efficiently. From biotechnological point of view, V. harveyi acts as an excellent candidate for bioconversion of the vast quantity of chitin wastes into multimillion tons of bioenergy or biofuel active compounds. My research carried out in the past decade is to try to understand structure-function relationship of molecular proteins/enzymes involved in recycling of chitin biomass in marine Vibrios. The protein targets are chitinases, chitoporin, N-acetyl-glucosamindase, chitin binding protein, lytic polysaccharide monooxygenase/GlcNAc₂ phosphorylase/chitin sensor, and GlcNAc-specific ABC transporter.
2. Development of diabetic biosensors/cancer-marker immunosensors Chitin biomaterials exhibit extremely biocompatible properties, which make them particularly useful for biomedical applications, such as wound healing, cartilage tissue engineering, drug delivery and nerve generation. More recently, we reviewed the prominent application of chitin, chitosan and their derivatives in the dynamic field of the electrochemical sensor design as immobilization matrix for biological recognition elements. Regarding biomedical applications, the advantage is taken from the biocompatibility of chitin-based electrode coatings that firmly entrap the biological macromolecules, on the other hand, provide a protective environment for them. In collaboration with an expert in the biosensor field, Dr. Albert Schulte, we have been working on chitin-based sensor development. We discover that chitin/chitosan biomaterials can act as efficient thin film surface modifiers of all sorts of electrodes, and they have been successfully applied to the realization of enzyme-, antibody/antigen and DNA-based biosensors with superb analytical performance. In our laboratory, we have specifically focused on the improvement of chitin/chitosan-based immunosensing as a diagnostic tool for sensitive detection of a cancer marker chitinase 3-like protein 1 (CHI3-L1 or hYKL-40) and an osteoarthritis marker chitinase3-like protein 2 CHI-L2 or hYKL-39)
3. Understanding of drug transport mechanism of a highly multidrug-resistant Melioidosis bacterium Burkholderia pseudomallei An infection with the bacterium Burkholderia pseudomallei (Bps) leads to melioidosis, a fatal disease with rapid progress and high mortality. In tropical Thailand, for example, Bps is prevalent in soil and ground water and blamed for up to 20% of community-acquired septicemia and related death tolls. Treatment of melioidosis has been difficult since Bps develops a high resistance against common antibiotics. The enzymatic destruction of antibiotics prior to action and a restriction of the drug flux into the interior of a bacterial cell have been proposed as tactics of bacteria for survival. However, the antibiotic resistance mechanisms of Bps are not discovered in detail yet and thus are in the focus of an intensive global research. In the past decade, we have been working on the investigation of the molecular mechanism of drug resistance that involves membrane permeability of Bps. We systematically employ various biophysical and microbiological approaches to examine the molecular passage of antimicrobial molecules of different classes through the outer membrane channel of Bps. Our study will help to understand the molecular nature of the antibiotic uptake by Bps, and ultimately pave the way for a rational design of effective anti-microbial agents against lethal melioidosis.

Published Articles :

1. Suginta W*, Sritho N, Ranok A, Bulmer D, Kitaoku Y, van den Berg B, and Fukamizo T. (2018) Structure and function of a novel periplasmic chitooligosaccharide-binding protein from marine Vibrio bacteria. J Biol Chem. In Press.
2. Aunkham A, Zahn M, Kesireddy A, Kleinekathöefer U, Suginta W*, van den Berg B*. (2018) Structural basis for chitin acquisition by marine Vibrio species. Nature-Commun. 9, 220.
3. Soysa HMS, Schulte A, Suginta W*. Functional analysis of an unusual porin-like channel that imports chitin for alternative carbon metabolism in Escherichia coli. J Biol Chem. 292, 19328-19337.
4. Thongsom S, Suginta W, Lee KJ, Choe H*, Talabnin C*. Piperlongumine induces G2/M phase arrest and apoptosis in cholangiocarcinoma cells through the ROS-JNK-ERK signaling pathway. Apoptosis. 2,1473-1484.
5. Meekrathok P, Kukic P, Nielsen JE, Suginta W*. (2017) Investigation of Ionization Pattern of the Adjacent Acidic Residues in the DXDXE Motif of GH-18 Chitinases Using Theoretical pKa Calculations. J Chem Inf Model. 57,572-583.
6. Chaocharoen W, Schulte A*, Suginta W*. (2017) hYKL-40 cancer biomarker electroanalysis in serum samples and model cell lysates: capacitive immunosensing compared with enzyme label immunosorbent assays (ELISA). 142, 503-510.
7. Suginta W*, Sirimontree P, Sritho N, Ohnuma T, Fukamizo T. (2016) The chitin-binding domain of a GH-18 chitinase from Vibrio harveyi is crucial for chitin-chitinase interactions. Int J Biol Macromol. 93, 1111-1117.
8. Suginta W, Winterhalter M, Smith MF*. (2016) Correlated trapping of sugar molecules by the trimeric protein channel chitoporin. Biochim Biophys Acta-Biomembr. 1858, 3032-3040.
9. Soysa HMS, Suginta W*. (2016) Identification and functional characterization of a novel OprD-like chitin uptake channel in non-chitonolytic bacteria. J Biol Chem. 29, 13622-13633.
10. Talabnin C*, Janthavon P, Thongsom S, Suginta W, Talabnin K, Wongkham S. (2016) Ring finger protein 43 (RNF43) expression is associated with genetic alteration status and poor prognosis among patients with intrahepatic cholangiocarcinoma. Hum Pathol. 52,47-54.
11. Thongsom S, Chaocharoen W, Silsirivanit A, Wongkham S, Sripa B, Choe H, Suginta W*, Talabnin C*. (2016) YKL-40/Chitinase-3-Like-Protein-1 is Associated with Poor Prognosis and Promotes Cell Growth and Migration of Cholangiocarcinoma. Tumor Biol. 37,9451-9463.
12. Meekrathok P, Suginta W.* (2016) Probing the Catalytic Mechanism of Vibrio harveyi GH20 β-N-Acetylglucosaminidase by Chemical Rescue. PLoS One. 11, e0149228.
13. Chaocharoen W, Ranok A, Suginta W*, Schulte A* (2015) A microfluidic capacitive immunosensor system for human cartilage chitinase-3-like protein 2 (hYKL-39) quantification as an osteoarthritis marker in synovial joint fluid. RSC Adv. 5, 85410-85416.
14. Sirimontree P, Fukamizo T, Suginta W*. (2015) Azide anions inhibit GH-18 endochitinase and GH-20 Exo β-N-acetylglucosaminidase from the marine bacterium Vibrio harveyi. J Biochem. first published online September 1, 2015 doi:10.1093/jb/mvv087.
15. Chumjan W, Winterhalter M, Schulte A, Benz R, Suginta W*. (2015) Chitoporin from the Marine Bacterium Vibrio harveyi: Probing the Essential Roles of Trp136 at the Surface of the Constriction Zone. J Biol Chem. 290, 19184-19196.
16. Meekrathok P, Bürger M, Porfetye AT, Vetter IR, Suginta W*. (2015) Expression, purification, crystallization and preliminary crystallographic analysis of a GH20 β-N-acetylglucosaminidase from the marine bacterium Vibrio harveyi. Acta Crystallogr F Struct Biol Commun. 71:427-433.
17. Ranok A, Wongsantichon J, Robinson RC, Suginta W* (2015) Structural and thermodynamic insights into chitooligosaccharide binding to human cartilage chitinase 3-Like Protein 2 (CHI3L2 or YKL-39). J Biol Chem, 290:2617-2629.
18. Theanponkrang S, Suginta W, Weingart H, Winterhalter M, Schulte A* (2015) Robotic voltammetry with carbon nanotube-based sensors: A superb blend for convenient high-quality antimicrobial trace analysis. Int J Nanomedicine, 10:859-868.
19. Chaocharoen W, Suginta W, Ranok A, Limbut W, Numnuam A, Khunkaewla P, Kanatharana P, Thavarungkul P, Schulte A* (2015) Electrochemical immunosensing of human YKL-40, a mammalian chitinase-like protein and disease marker. 101:106-113.
20. Chotinantakul K, Suginta W*, Schulte A* (2014) An Advanced amperometric respiration assay for antibiotic susceptibility testing. Anal Chem. 86:10315-10322.
21. Sirimontree P, Suginta W*, Sritho N, Kanda Y, Shinya S, Ohnuma T, and Fukamzo T*. (2014) Mutation strategies for obtaining chitooligosaccharides with longer chains by transglycosylation reaction of a family GH18 chitinase. Biosci Biotech Biochem. 78:2014-2021.
22. Aunkham A, Schulte A, Winterhalter M, Suginta W*. (2014) BpsOmp38 porin involvement in cephalosporin and carbapenem resistance of the ultraresistant melioidosis bacterium Burkholderia pseudomallei. PLoS One. 9:e95918.
23. Ranok A, Khunkaewla P, Suginta W* (2013) Human cartilage chitinase 3-like protein 2: Cloning, expression, production of polyclonal and monoclonal antibodies for osteoarthritis detection and identification of potential binding partners. Monoclon Antib Immunodiagn Immunother (formerly Hybridoma). 32, 317-325.
24. Suginta W, Smith MF* (2013) Single-molecule trapping dynamics of sugar-uptake channels in marine bacteria. Phys Rev Lett. 110, 238102.
25. Suginta W, Khunkaewla P, Schulte A* (2013) Electrochemical biosensor applications of polysaccharides chitin and chitosan. Chem Rev. 113, 5458-5479.
26. Suginta W*, Chumjan W, Mahendran KR, Schulte A, Winterhalter M. (2013) Chitoporin from Vibrio harveyi: A Channel with Exceptional Sugar Specificity. J Biol Chem. 288, 11038-11046.
27. Suginta W*, Chumjan W, Mahendran KR, Janning P, Schulte A, Winterhalter M. (2013) Molecular uptake of chitooligosaccharides through chitoporin from the marine bacterium Vibrio harveyi. PLoS One. 8:e55126.
28. Suginta W*, Sritho N. (2012) Multiple roles of Asp313 in the refined catalytic cycle of chitin degradation by Vibrio harveyi chitinase A. Biosci Biotech Biochem. 76, 2275-2281.
29. Sritho N & Suginta W* (2012) Role of Tyr-435 of Vibrio harveyi chitinase A in chitin utilization. App Biochem Biotech. 166, 1192–1202.
30. Pantoom S, Vetter I*, Prinz, H*, Suginta W* (2011) Potent family-18 chitinase inhibitors: X-ray structures, affinities and binding mechanisms. J Biol Chem. 286, 24312-24323.
31. Suginta W*, Mahendran KR, Chumjan W, Hajjar E, Schulte A, Winterhalter M, Weingart H*. (2011) Molecular analysis of antimicrobial agent translocation through the membrane porin BpsOmp38 from an ultraresistant Burkholderia pseudomallei BBA-Biomembr. 1808, 1552-1559.
32. Suginta W*, Chuenark D, Masuhara M, Fukamizo T (2010) Novel β-N-acetylglucosaminidases from Vibrio harveyi 650: Cloning, expression, enzymatic properties, and subsite identification. BMC Biochem. 11:40. (Highly accessed)
33. Schulte A, Ruamchan S, Khunkaewla P, Suginta W* (2009) The outer membrane protein VhOmp from Vibrio harveyi: The pore-forming properties in black lipid membranes. J Membr Biol. 230, 101-111.
34. Suginta W*, Pantoom S, Prinz H (2009) Substrate binding modes and anomer selectivity of chitinase A from Vibrio harveyi. J Chem Biol. 2, 191-202.
35. Songsiriritthigul C, Pantoom S, Aguda AH, Robinson RC, Suginta W* (2008) Crystal structures of Vibrio harveyi chitinase A complexed with chitooligosaccharides: Implications for the catalytic mechanism. J Struct Bio 162, 491-499.
36. Pantoom S, Songsiriritthigul C, Suginta W* (2008) The effects of the surface-exposed residues on the binding and hydrolytic activities of Vibrio carchariae chitinase A. BMC-Biochem. 9:2.
37. Suginta W*, Songsiriritthigul C, Kobdaj A, Opassiri R, Svasti J (2007) Mutations of Trp275 and Trp397 altered the binding selectivity of Vibrio carchariae chitinase A. BBA-General Subjects. 1770, 1151-1160.
38. Suginta W* (2007) Identification of chitin binding proteins and characterization of two chitinase isoforms from Vibrio alginolyticus Enzyme Microb Tech. 41, 212-220.
39. Songsiriritthigul C, Yuvaniyama J, Robinson RC, Vongsuwan A, Prinz H, Suginta W* (2005) Expression, purification, crystallization and preliminary crystallographic analysis of chitinase A from Vibrio carchariae. Acta Cryst. Section F. 61, 895-898.
40. Suginta W*, Vongsuwan A, Songsiriritthigul C, Svasti J, Prinz H (2005) Enzymatic properties of wild-type and active site mutants of chitinase A from Vibrio carchariae, as revealed by HPLC-MS. FEBS J. 272, 3376-3386.
41. Siritapetawee J, Prinz H, Krittanai C, Suginta W* (2004) Expression, refolding of Omp38 from Burkholderia pseudomallei and B. thailandensis, and its function as a diffusion porin. Biochem J. 384, 609–617.
42. Suginta W*, Vongsuwan A, Songsiriritthigul C, Prinz H, Estibeiro P, Duncan RR, Svasti J, Fothergill-Gilmore LA (2004) An endochitinase A from Vibrio carchariae: gene isolation, modelled structure topology, cloning and functional expression. Arch Biochem Biophys. 424, 171-180.
43. Siritapetawee J, Prinz H, Samosornsuk W, Ashley RH, Suginta W* (2004) Functional  reconstitution, gene isolation and topology modelling of porins from Burkholderia pseudomallei and thailandensis. Biochem J. 377, 579-587.
44. Suginta W, Karoulias N, Aitkin A, Ashley RH* (2001) Brain dynamin-1 interacts directly with the chloride intracellular channel protein CLIC4 in a complex containing actin and 14-3-3 proteins. Biochem J. 359, 55-64.
45. Suginta W, Robertson PAW, Austin B, Fry SC, Fothergill-Gilmore LA* (2000) Chitinases from Vibrio: activity screening and purification of chi A from Vibrio carchariae. J Appl Microbiol. 89, 76-84.
46. Svasti J*, Srisomsap C, Surarit R, Benjavongkulchai E, Suginta W, Khunyoshyeng S, Champattanachai V, Nilwarangkoon S, Rungvirayudx S (1996) Potential Applications of Plant Glycohydrolases for Oligosaccharide Synthesis. In Protein Structure-Function Relationship (Zaidi, Z.H. and Smith, D.L., eds.), Plenum Press. pp.249-257.
47. Surarit R, Svasti MR J, Srisomsap C, Suginta W, Khunyoshyeng S, Nilwarangkoon S, Harnsakul P, Benjavongkulchai E* (1995) Possible Use of Glycosidase Enzymes from Thai Plant Seeds for Oligosaccharide Synthesis. In Biopolymers and Bioproducts: structure, function and applications (Svasti, J. et al., eds.), Samakkhisan Public Co. Ltd., Bangkok, 251-255.
48. Suginta W, Svasti MRJ* (1995) Purification and Properties of β-Galactosidase from Hibiscus  sabdariffa  var.  altissima. Science Asia (Formerly J Sci Soc Thai) 21, 183-186.
49. Suginta W, Svasti J* (1995) Beta-Galactosidase from Thai Jute: Purification and Characterization. In Biopolymers and Bioproducts: Structure, Function and Applications (Svasti, J. et al., eds.), Samakkhisan Public Co. Ltd., Bangkok, 256-260.
50. Surarit R, Svasti MRJ, Srisomsap C, Suginta W, Khunyoshyeng S, Nilwarangkoon S, Harnsakul P, Benjavongkulchai E (1995) Screening of Glycohydrolase Enzymes in Thai Plant Seeds for Potential Use in Oligosaccharide Synthesis.  Science Asia (Formerly J Sci Soc Thai) 21, 293-303.