User:Natalie Bamford

Natalie Bamford did her undergraduate degree at the University of Toronto in Biochemistry. She then completed her graduate work supervised by Lynne Howell conducting research out of the Hospital for Sick Children. This led to her obtaining her PhD in Biochemistry from the University of Toronto in 2019. Her research focused on the carbohydrate active enzymes involved in exopolysaccharide production used by microbes in biofilm formation. This included structural and biochemical characterization of glycoside hydrolases [1, 2, 3, 4, 5], carbohydrate esterases [6, 7, 8, 9], and a carbohydrate binding module [9]. Natalie's studies helped in the creation of three GH families (GH135, GH153, GH166), one CE family (CE18) and one CBM family (CBM87). She is now a postdoctoral fellow at the University of Dundee with Nicola Stanley-Wall.

She has aided in the determination of crystal structures including:

• GH114 Aspergillus fumigatus Ega3, an α-1,4-galactosaminidase [5]
• GH135 Aspergillus clavatus Sph3, an α-1,4-N-acetylgalactosaminidase [1]
• GH153 Bordetella bronchiseptica PgaB, a poly-β-1,6-D-glucosamine hydrolase [3]
• CE4 Ammonifex degensii IcaB, a poly-β-1,6-N-acetyl-D-glucosamine deacetylase [7]
• [[[CE18]] and CBM87 Aspergillus fumigatus Agd3, an α-1,4-N-acetylgalactosaminidase deacetylase [9]

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5. Bamford NC, Le Mauff F, Subramanian AS, Yip P, Millán C, Zhang Y, Zacharias C, Forman A, Nitz M, Codée JDC, Usón I, Sheppard DC, and Howell PL. (2019). Ega3 from the fungal pathogen Aspergillus fumigatus is an endo-α-1,4-galactosaminidase that disrupts microbial biofilms. J Biol Chem. 2019;294(37):13833-13849. DOI:10.1074/jbc.RA119.009910 |