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Difference between revisions of "User:Natalie Bamford"
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[[File:NatalieBamford.png|200px|right]] | [[File:NatalieBamford.png|200px|right]] | ||
| − | + | '''Natalie Bamford''' did her undergraduate degree at the [http://biochemistry.utoronto.ca/ University of Toronto in Biochemistry]. She then completed her graduate work supervised by [[User: Lynne Howell|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 <cite>Bamford2015 Snarr2017 Little2018 LeMauff2019 Bamford2019</cite>, carbohydrate esterases <cite>Little2014 Little2014b Little2015 Bamford2020</cite>, and a carbohydrate binding module <cite>Bamford2020</cite>. Natalie's studies helped in the creation of three GH families ([[Glycoside Hydrolase Family 135|GH135]], [[Glycoside Hydrolase Family 153|GH153]], [[GH166]]), one CE family (CE18) and one CBM family ([[Carbohydrate Binding Module Family 87|CBM87]]). She is now a postdoctoral fellow at the University of Dundee with [https://www.lifesci.dundee.ac.uk/people/nicola-stanley-wall Nicola Stanley-Wall]. | |
| − | '''Natalie Bamford''' did her undergraduate degree at the [http://biochemistry.utoronto.ca/ University of Toronto in Biochemistry]. She then completed her graduate work supervised by [[User: Lynne Howell|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 <cite>Bamford2015 Snarr2017 Little2018 LeMauff2019 Bamford2019</cite>, carbohydrate esterases <cite>Little2014 Little2014b Little2015 Bamford2020</cite>, and a carbohydrate binding module <cite>Bamford2020</cite>. Natalie's studies helped in the creation of three GH families ([[Glycoside Hydrolase Family 135|GH135]], [[Glycoside Hydrolase Family 153|GH153]], [ | ||
She has aided in the determination of crystal structures including: | She has aided in the determination of crystal structures including: | ||
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*[[Glycoside Hydrolase Family 153|GH153]] ''Bordetella bronchiseptica'' PgaB, a poly-β-1,6-D-glucosamine hydrolase <cite>Little2018</cite> | *[[Glycoside Hydrolase Family 153|GH153]] ''Bordetella bronchiseptica'' PgaB, a poly-β-1,6-D-glucosamine hydrolase <cite>Little2018</cite> | ||
*[[Carbohydrate Esterase Family 4|CE4]] ''Ammonifex degensii'' IcaB, a poly-β-1,6-''N''-acetyl-D-glucosamine deacetylase <cite>Little2014b</cite> | *[[Carbohydrate Esterase Family 4|CE4]] ''Ammonifex degensii'' IcaB, a poly-β-1,6-''N''-acetyl-D-glucosamine deacetylase <cite>Little2014b</cite> | ||
| − | *[ | + | *[[CE18]] and [[Carbohydrate Binding Module Family 87|CBM87]] ''Aspergillus fumigatus'' Agd3, an α-1,4-''N''-acetylgalactosaminidase deacetylase <cite>Bamford2020</cite> |
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---- | ---- | ||
<biblio> | <biblio> | ||
| − | #Bamford2015 pmid | + | #Bamford2015 pmid=26342082 |
| − | #Snarr2017 pmid | + | #Snarr2017 pmid=28634301 |
| − | #Little2018 pmid | + | #Little2018 pmid=29684093 |
| − | #LeMauff2019 pmid | + | #LeMauff2019 pmid=31167793 |
| − | #Bamford2019 pmid | + | #Bamford2019 pmid=31416836 |
| − | #Little2014 pmid | + | #Little2014 pmid=24994902 |
| − | #Little2014b pmid | + | #Little2014b pmid=25359777 |
| − | #Little2015 pmid | + | #Little2015 pmid=26203190 |
| − | #Bamford2020 pmid | + | #Bamford2020 pmid=32415073 |
</biblio> | </biblio> | ||
<!-- Do not remove this Category tag --> | <!-- Do not remove this Category tag --> | ||
[[Category:Contributors|Bamford,Natalie]] | [[Category:Contributors|Bamford,Natalie]] | ||
Latest revision as of 09:41, 29 May 2020
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]
- Bamford NC, Snarr BD, Gravelat FN, Little DJ, Lee MJ, Zacharias CA, Chabot JC, Geller AM, Baptista SD, Baker P, Robinson H, Howell PL, and Sheppard DC. (2015). Sph3 Is a Glycoside Hydrolase Required for the Biosynthesis of Galactosaminogalactan in Aspergillus fumigatus. J Biol Chem. 2015;290(46):27438-50. DOI:10.1074/jbc.M115.679050 |
- Snarr BD, Baker P, Bamford NC, Sato Y, Liu H, Lehoux M, Gravelat FN, Ostapska H, Baistrocchi SR, Cerone RP, Filler EE, Parsek MR, Filler SG, Howell PL, and Sheppard DC. (2017). Microbial glycoside hydrolases as antibiofilm agents with cross-kingdom activity. Proc Natl Acad Sci U S A. 2017;114(27):7124-7129. DOI:10.1073/pnas.1702798114 |
- Little DJ, Pfoh R, Le Mauff F, Bamford NC, Notte C, Baker P, Guragain M, Robinson H, Pier GB, Nitz M, Deora R, Sheppard DC, and Howell PL. (2018). PgaB orthologues contain a glycoside hydrolase domain that cleaves deacetylated poly-β(1,6)-N-acetylglucosamine and can disrupt bacterial biofilms. PLoS Pathog. 2018;14(4):e1006998. DOI:10.1371/journal.ppat.1006998 |
- Le Mauff F, Bamford NC, Alnabelseya N, Zhang Y, Baker P, Robinson H, Codée JDC, Howell PL, and Sheppard DC. (2019). Molecular mechanism of Aspergillus fumigatus biofilm disruption by fungal and bacterial glycoside hydrolases. J Biol Chem. 2019;294(28):10760-10772. DOI:10.1074/jbc.RA119.008511 |
- 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 |
- Little DJ, Li G, Ing C, DiFrancesco BR, Bamford NC, Robinson H, Nitz M, Pomès R, and Howell PL. (2014). Modification and periplasmic translocation of the biofilm exopolysaccharide poly-β-1,6-N-acetyl-D-glucosamine. Proc Natl Acad Sci U S A. 2014;111(30):11013-8. DOI:10.1073/pnas.1406388111 |
- Little DJ, Bamford NC, Pokrovskaya V, Robinson H, Nitz M, and Howell PL. (2014). Structural basis for the De-N-acetylation of Poly-β-1,6-N-acetyl-D-glucosamine in Gram-positive bacteria. J Biol Chem. 2014;289(52):35907-17. DOI:10.1074/jbc.M114.611400 |
- Little DJ, Milek S, Bamford NC, Ganguly T, DiFrancesco BR, Nitz M, Deora R, and Howell PL. (2015). The protein BpsB is a poly-β-1,6-N-acetyl-D-glucosamine deacetylase required for biofilm formation in Bordetella bronchiseptica. J Biol Chem. 2015;290(37):22827-40. DOI:10.1074/jbc.M115.672469 |
- Bamford NC, Le Mauff F, Van Loon JC, Ostapska H, Snarr BD, Zhang Y, Kitova EN, Klassen JS, Codée JDC, Sheppard DC, and Howell PL. (2020). Structural and biochemical characterization of the exopolysaccharide deacetylase Agd3 required for Aspergillus fumigatus biofilm formation. Nat Commun. 2020;11(1):2450. DOI:10.1038/s41467-020-16144-5 |