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Resolving the α-glycosidic linkage of arginine-rhamnosylated translation elongation factor P triggers generation of the first Arg^Rha specific antibody

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Resolving the α-glycosidic linkage of arginine-rhamnosylated translation elongation factor P triggers generation of the first Arg^Rha specific antibody

Content Provider	Royal Society of Chemistry (RSC)
Author	Macošek, Jakub Hennig, Janosch Jung, Kirsten Wu, Qiu-Ye Lassak, Jürgen Hu, Hong-Gang Simon, Bernd Yan, Fang Li, Yu-Lei Zou, Yan Krafczyk, Ralph Li, Shan Pan, Xing Li, Xiang
Copyright Year	2016
Abstract	A previously discovered posttranslational modification strategy – arginine rhamnosylation – is essential for elongation factor P (EF-P) dependent rescue of polyproline stalled ribosomes in clinically relevant species such as Pseudomonas aeruginosa and Neisseria meningitidis. However, almost nothing is known about this new type of N-linked glycosylation. In the present study we used NMR spectroscopy to show for the first time that the α anomer of rhamnose is attached to Arg32 of EF-P, demonstrating that the corresponding glycosyltransferase EarP inverts the sugar of its cognate substrate dTDP-β-L-rhamnose. Based on this finding we describe the synthesis of an α-rhamnosylated arginine containing peptide antigen in order to raise the first anti-rhamnosyl arginine specific antibody (anti-ArgRha). Using ELISA and Western Blot analyses we demonstrated both its high affinity and specificity without any cross-reactivity to other N-glycosylated proteins. Having the anti-ArgRha at hand we were able to visualize endogenously produced rhamnosylated EF-P. Thus, we expect the antibody to be not only important to monitor EF-P rhamnosylation in diverse bacteria but also to identify further rhamnosyl arginine containing proteins. As EF-P rhamnosylation is essential for pathogenicity, our antibody might also be a powerful tool in drug discovery.
Starting Page	6995
Ending Page	7001
Page Count	7
File Format	HTM / HTML PDF
ISSN	20416520
Volume Number	7
Issue Number	12
Journal	Chemical Science
DOI	10.1039/c6sc02889f
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Subscribed
Subject Keyword	Post-translational modification Western blot Glycosyltransferase Glycosylation Antigen Elongation factor P Arginine Neisseria Nuclear magnetic resonance spectroscopy of proteins Rhamnose Pseudomonas aeruginosa Bacteria Carbohydrate Drug discovery Peptide
Content Type	Text
Resource Type	Article
Subject	Chemistry

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Structural Basis for EarP-Mediated Arginine Glycosylation of Translation Elongation Factor EF-P.

Structural Basis for EarP-Mediated Arginine Glycosylation of Translation Elongation Factor EF-P

Synthesis of rhamnosylated arginine glycopeptides and determination of the glycosidic linkage in bacterial elongation factor P

Switching the Post-translational Modification of Translation Elongation Factor EF-P

Cyclic Rhamnosylated Elongation Factor P Establishes Antibiotic Resistance in Pseudomonas aeruginosa.

Cyclic Rhamnosylated Elongation Factor P Establishes Antibiotic Resistance in Pseudomonas aeruginosa

Cyclic Rhamnosylated Elongation Factor P Establishes Antibiotic Resistance in Pseudomonas aeruginosa

nosylated arginine glycopeptides and determination of the glycosidic linkage in bacterial elongation factor P †

Substrate recognition by the Pseudomonas aeruginosa EF-Tu–modifying methyltransferase EftM

Resolving the α-glycosidic linkage of arginine-rhamnosylated translation elongation factor P triggers generation of the first Arg^Rha specific antibody

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Resolving the α-glycosidic linkage of arginine-rhamnosylated translation elongation factor P triggers generation of the first ArgRha specific antibody

Resolving the α-glycosidic linkage of arginine-rhamnosylated translation elongation factor P triggers generation of the first Arg^Rha specific antibody