Food grade expression system using L. plantarumAntibody Engineering
Molecular and Cellular Mechanisms of Neutraceuticals
Development of Biologics Production Platforms
Generation and Manufacturing of Bioactive oligosaccharides
Molecular biology
Phage display technolgy
Protein, Expression Engineering
Current Research
Food grade expression system using L. plantarumAntibody Engineering
Molecular and Cellular Mechanisms of Neutraceuticals
Development of Biologics Production Platforms
Generation and Manufacturing of Bioactive oligosaccharides
Molecular biology
Phage display technolgy
Protein, Expression Engineering
Year
Month
Title
Journal
Information
2008
Immune responses of selected phagotopes from monoclonal antibodies of Burkholderia pseudomallei Na-ngam N., Kalambaheti T., Ekpo P., Pitaksajjakul A., Jamornthanyawat N., Chantratita N., Sirisinha S., Thamlikitkul V., Chaicumpa W., Yamabhai M., Ramasoota P.
Southeast Asian Journal of Tropical Medicine and Public Health
Abstract: Random peptide libraries displayed by bacteriophage T7 and M13 were employed to identify mimotopes from 4 monoclonal antibodies (MAbs) specific to Burkholderia pseudomallei. Insert DNA sequences of bound phages selected from four rounds of panning with each MAb revealed peptide sequences corresponding to B. pseudomallei K96243 hypothetical protein BPSL2046, hypothetical protein BpseP_02000035, B. pseudomallei K96243 hypothetical protein BPSS0784, B. pseudomallei 1710b hypothetical protein BURPS1710b_1104, and 6. cenocepacia H12424 TonB-dependent siderophore receptor, all located at the outer membrane. The immune responses from all selected phagotopes were significantly higher than that of lipopolysaccharide. The study demonstrates the feasibility of identifying mimotopes through screening of phage-displayed random peptide libraries with B. pseudomallei MAbs.
Secretion of recombinant Bacillus hydrolytic enzymes using Escherichia coli expression systems Yamabhai M., Emrat S., Sukasem S., Pesatcha P., Jaruseranee N., Buranabanyat B.
Cloning and expression of the β-galactosidase genes from Lactobacillus reuteri in Escherichia coli Nguyen T.-H., Splechtna B., Yamabhai M., Haltrich D., Peterbauer C.
Formation of galacto-oligosaccharides during lactose hydrolysis by a novel β-galactosidase from the moderately thermophilic fungus Talaromyces thermophilus Nakkharat P., Kulbe K.D., Yamabhai M., Haltrich D.
A convenient method for the screening of compounds that inhibit specific molecular interactions using the alkaline phosphatase fusion system Yamabhai M.
A role for epsin N-terminal homology/AP180 N-terminal homology (ENTH/ANTH) domains in tubulin binding Hussain N.K., Yamabhai M., Bhakar A.L., Metzler M., Ferguson S.S.G., Hayden M.R., McPherson P.S., Kay B.K.
Journal of Biological Chemistry
Abstract: The epsin N-terminal homology (ENTH) domain is a protein module of ∼150 amino acids found at the N terminus of a variety of proteins identified in yeast, plants, nematode, frog, and mammals. ENTH domains comprise multiple α-helices folded upon each other to form a compact globular structure that has been implicated in interactions with lipids and proteins. In characterizing this evolutionarily conserved domain, we isolated and identified tubulin as an ENTH domain-binding partner. The interaction, which is direct and has a dissociation constant of ∼1 μM, was observed with ENTH domains of proteins present in various species. Tubulin is co-immunoprecipitated from rat brain extracts with the ENTH domain-containing proteins, epsins 1 and 2, and punctate epsin staining is observed along the microtubule cytoskeleton of dissociated cortical neurons. Consistent with a role in microtubule processes, the over-expression of epsin ENTH domain in PC12 cells stimulates neurite outgrowth. These data demonstrate an evolutionarily conserved property of ENTH domains to interact with tubulin and microtubules.
Second cysteine-rich region of epidermal growth factor receptor contains targeting information for caveolae/rafts Yamabhai M., Anderson R.G.W.
Journal of Biological Chemistry
Abstract: Previous studies have shown that ∼60% of the epidermal growth factor receptors (EGFRs) in quiescent fibroblasts are concentrated in the caveolae/raft fraction from purified plasma membranes. This high degree of localization suggests the EGFR contains targeting information for lipid domains. We have used mutagenesis to determine that the region of the receptor that controls targeting to caveolae/rafts resides in the juxtamembrane, second cysteine-rich region. A 60-amino acid-long sequence within this region that is continuous with the transmembrane domain was sufficient to target the transmembrane and cytoplasmic tails of both EGFR and the low density lipoprotein receptor to caveolae/rafts. Two N-linked sugars in this segment were not required for proper targeting, although unglycosylated wild-type receptors did not localize properly. We conclude that, in contrast to signals for coated pit localization that are in the cytoplasmic tail, the targeting information for caveolae/rafts is on the extracellular side of the EGFR very close to the membrane.
Molecular mechanism of NPF recognition by EH domains De Beer T., Hoofnagle A.N., Enmon J.L., Bowers R.C., Yamabhai M., Kay B.K., Overduin M.
Nature Structural Biology
Abstract: Eps15 homology (EH) domains are protein interaction modules that recognize Asn-Pro-Phe (NPF) motifs in their biological ligands to mediate critical events during endocytosis and signal transduction. To elucidate the structural basis of the EH-NPF interaction, the solution structures of two EH-NPF complexes were solved using NMR spectroscopy. The first complex contains a peptide representing the Hrb C-terminal NPFL motif; the second contains a peptide in which an Arg residue substitutes the C-terminal Leu. The NPF residues are almost completely embedded in a hydrophobic pocket on the EH domain surface and the backbone of NPFX adopts a conformation reminiscent of the Asx-Pro type I β-turn motif. The residue directly following NPF is crucial for recognition and is required to complete the β-turn. Five amino acids on the EH surface mediate specific recognition of this residue through hydrophobic and electrostatic contacts. The complexes explain the selectivity of the second EH domain of Eps15 for NPF over DPF motifs and reveal a critical aromatic interaction that provides a conserved anchor for the recognition of FW, WW, SWG and HTF ligands by other EH domains.
