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Proteomic approaches for the detecti...

Schirm, Michael.

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Proteomic approaches for the detection of unusual post-translational modifications in simple and complex bacterial protein mixtures.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Proteomic approaches for the detection of unusual post-translational modifications in simple and complex bacterial protein mixtures./
作者:	Schirm, Michael.
面頁冊數:	140 p.
附註:	Source: Dissertation Abstracts International, Volume: 66-08, Section: B, page: 4200.
Contained By:	Dissertation Abstracts International66-08B.
標題:	Chemistry, Analytical. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=NR05541
ISBN:	9780494055410

Proteomic approaches for the detection of unusual post-translational modifications in simple and complex bacterial protein mixtures.
Schirm, Michael.

Proteomic approaches for the detection of unusual post-translational modifications in simple and complex bacterial protein mixtures. - 140 p.

Source: Dissertation Abstracts International, Volume: 66-08, Section: B, page: 4200.

Thesis (Ph.D.)--Universite de Montreal (Canada), 2005.

The research conducted in this dissertation is separated in three parts. In the first part the flagellin proteins from different human pathogens were analyzed for protein glycosylation. Studies on flagellin from Helicobacter pylori, Listeria monocytogenes, Aeromonas caviae, Pseudomonas aeruginosa and Campylobacter jejuni showed that prokaryotic protein glycosylation is a common theme and much more prevalent than previously thought. A novel approach using targeted capillary liquid chromatography coupled to tandem mass spectrometry (capLC/MS/MS) was developed and revealed that the flagellin from these bacteria were all post-translationally modified with O-linked glycans. Extensive structural analyses of these flagellin glycans showed the occurrence of different carbohydrate residues, indicating the use of different biosynthetic substrates and glycosyl transferases. It is noteworthy that H. pylori, A. caviae and C. jejuni all used substrates structurally related to pseudaminic acid, a novel nine-carbon sugar related to sialic acid, while in L. monocytogenes the flagellin was glycosylated with a single N-acetyl glucosamine. The nature of the glycosyl modifications varied significantly between different strains of P. aeruginosa, with a heterogeneous glycan comprising up to 11 monosaccharide units for strain PAK while in strains JJ692 and PAO, the glycans were identified as rhamnose and an unknown carbohydrate residue having a mass of 356 Da, respectively. Furthermore, genes involved in this flagellar glycosylation process were identified for H. pylori, P. aeruginosa and L. monocytogenes and their functional relationships were elucidated from mass spectrometry analyses.

ISBN: 9780494055410Subjects--Topical Terms:

586156
Chemistry, Analytical.

Proteomic approaches for the detection of unusual post-translational modifications in simple and complex bacterial protein mixtures.
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520 $a The research conducted in this dissertation is separated in three parts. In the first part the flagellin proteins from different human pathogens were analyzed for protein glycosylation. Studies on flagellin from Helicobacter pylori, Listeria monocytogenes, Aeromonas caviae, Pseudomonas aeruginosa and Campylobacter jejuni showed that prokaryotic protein glycosylation is a common theme and much more prevalent than previously thought. A novel approach using targeted capillary liquid chromatography coupled to tandem mass spectrometry (capLC/MS/MS) was developed and revealed that the flagellin from these bacteria were all post-translationally modified with O-linked glycans. Extensive structural analyses of these flagellin glycans showed the occurrence of different carbohydrate residues, indicating the use of different biosynthetic substrates and glycosyl transferases. It is noteworthy that H. pylori, A. caviae and C. jejuni all used substrates structurally related to pseudaminic acid, a novel nine-carbon sugar related to sialic acid, while in L. monocytogenes the flagellin was glycosylated with a single N-acetyl glucosamine. The nature of the glycosyl modifications varied significantly between different strains of P. aeruginosa, with a heterogeneous glycan comprising up to 11 monosaccharide units for strain PAK while in strains JJ692 and PAO, the glycans were identified as rhamnose and an unknown carbohydrate residue having a mass of 356 Da, respectively. Furthermore, genes involved in this flagellar glycosylation process were identified for H. pylori, P. aeruginosa and L. monocytogenes and their functional relationships were elucidated from mass spectrometry analyses.
520 $a The complete characterization of post-translational modifications and characterization of genes involved in this process is, a tedious and time consuming process even for simple protein mixtures that can take from several months to years. To simplify this approach, the second part of this thesis focused on developing a novel "top down" mass spectrometry approach to allow the rapid identification and characterization of post-translational modifications on intact proteins from simple protein mixtures. Furthermore, it enabled the rapid assignment of unknown gene functions by monitoring changes imparted to the sugar modifications in isogenic mutants derived from insertional inactivation of the individual genes involved in the flagellin glycosylation process. Compared to the traditional "bottom up" approach, the analysis time was significantly reduced. (Abstract shortened by UMI.)
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