The genetics of glycosylation in Gram-negative bacteria

by: Power, Jennings

FEMS Microbiology Letters, Vol. 218, No. 2. (2003), pp. 211-222.

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Abstract

Abstract In recent years there has been a dramatic increase in reports of glycosylation of proteins in various Gram-negative systems including Neisseria meningitidis, Neisseria gonorrhoeae, Campylobacter jejuni, Pseudomonas aeruginosa, Escherichia coli, Caulobacter crescentus, Aeromonas caviae and Helicobacter pylori. Although this growing list contains many important pathogens (reviewed by Benz and Schmidt [Mol. Microbiol. 45 (2002) 267-276]) and the glycosylations are found on proteins important in pathogenesis such as pili, adhesins and flagella the precise role(s) of the glycosylation of these proteins remains to be determined. Furthermore, the details of the glycosylation biosynthetic process have not been determined in any of these systems. The definition of the precise role of glycosylation and the mechanism of biosynthesis will be facilitated by a detailed understanding of the genes involved.

@article{citeulike:2733224, abstract = {Abstract In recent years there has been a dramatic increase in reports of glycosylation of proteins in various Gram-negative systems including Neisseria meningitidis, Neisseria gonorrhoeae, Campylobacter jejuni, Pseudomonas aeruginosa, Escherichia coli, Caulobacter crescentus, Aeromonas caviae and Helicobacter pylori. Although this growing list contains many important pathogens (reviewed by Benz and Schmidt [Mol. Microbiol. 45 (2002) 267-276]) and the glycosylations are found on proteins important in pathogenesis such as pili, adhesins and flagella the precise role(s) of the glycosylation of these proteins remains to be determined. Furthermore, the details of the glycosylation biosynthetic process have not been determined in any of these systems. The definition of the precise role of glycosylation and the mechanism of biosynthesis will be facilitated by a detailed understanding of the genes involved.}, author = {Power and Jennings}, citeulike-article-id = {2733224}, doi = {http://dx.doi.org/10.1111/j.1574-6968.2003.tb11520.x}, journal = {FEMS Microbiology Letters}, keywords = {glycosylation, microbiology, review}, number = {2}, pages = {211--222}, posted-at = {2008-04-29 10:25:14}, priority = {2}, title = {The genetics of glycosylation in Gram-negative bacteria}, url = {http://dx.doi.org/10.1111/j.1574-6968.2003.tb11520.x}, volume = {218}, year = {2003} }

RIS record

TY - JOUR ID - citeulike:2733224 L3 - citeulike-article-id:2733224 TI - The genetics of glycosylation in Gram-negative bacteria JF - FEMS Microbiology Letters VL - 218 IS - 2 SP - 211 EP - 222 N2 - Abstract In recent years there has been a dramatic increase in reports of glycosylation of proteins in various Gram-negative systems including Neisseria meningitidis, Neisseria gonorrhoeae, Campylobacter jejuni, Pseudomonas aeruginosa, Escherichia coli, Caulobacter crescentus, Aeromonas caviae and Helicobacter pylori. Although this growing list contains many important pathogens (reviewed by Benz and Schmidt [Mol. Microbiol. 45 (2002) 267-276]) and the glycosylations are found on proteins important in pathogenesis such as pili, adhesins and flagella the precise role(s) of the glycosylation of these proteins remains to be determined. Furthermore, the details of the glycosylation biosynthetic process have not been determined in any of these systems. The definition of the precise role of glycosylation and the mechanism of biosynthesis will be facilitated by a detailed understanding of the genes involved. KW - glycosylation KW - microbiology KW - review AU - Power AU - Jennings PY - 2003/// UR - http://dx.doi.org/10.1111/j.1574-6968.2003.tb11520.x ER -

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