scholarly journals Chemical synthesis of the outer core oligosaccharide of Escherichia coli R3 and immunological evaluation

2015 ◽  
Vol 13 (14) ◽  
pp. 4321-4330 ◽  
Author(s):  
Wenjing Shang ◽  
Zhongying Xiao ◽  
Zaikuan Yu ◽  
Na Wei ◽  
Guohui Zhao ◽  
...  

An all α-linked Escherichia coli R3 outer core pentasaccharide was first synthesized. Its corresponding glycoconjugate can elicit specific anti-pentasaccharide antibodies with in vitro bactericidal activity.

2012 ◽  
Vol 134 (34) ◽  
pp. 14255-14262 ◽  
Author(s):  
Thomas J. Boltje ◽  
Wei Zhong ◽  
Jin Park ◽  
Margreet A. Wolfert ◽  
Wangxue Chen ◽  
...  

2004 ◽  
Vol 54 (5) ◽  
pp. 897-903 ◽  
Author(s):  
Shigeharu Oie ◽  
Junko Ishitobi ◽  
Akihiro Sawa ◽  
Masaaki Tomita ◽  
Akira Kamiya

Author(s):  
Xiaoliang Liu ◽  
Ling Hu ◽  
Yuan Zhang ◽  
Hongtao Li

Abstract Ubiquitination, is involved in the regulation of numerous cellular functions. Researches in the ubiquitin realm rely heavily on ubiquitination assays in vitro and require large amounts of ubiquitin-activating enzyme (UBA1) and keep ATP supplies. But UBA1 is hard to be obtained with large quantities using reported methods. We fused Escherichia coli adenylate kinase (adk) and mouse UBA1 obtained fusion protein adk-mUBA1. The expression level of adk-mUBA1 increased about 8-fold than that of mUBA1 in Escherichia coli expression system, and adk-mUBA1 was easily purified to 90% purity via two purification steps. The purified adk-mUBA1 protein was functional for ubiquitination and could use ATP in addition to ADP as energy supply and had a higher catalytic activity than mUBA1 in cell lysis. Adk-mUBA1 can be applied to preparing ubiquitin modified substrates and kinds of ubiquitin chains in chemical synthesis process and is preferable application than mUBA1 in vitro ubiquitination.


2011 ◽  
Vol 186 (4S) ◽  
pp. 1678-1683 ◽  
Author(s):  
Douglas W. Storm ◽  
Stephen A. Koff ◽  
Dennis J. Horvath ◽  
Birong Li ◽  
Sheryl S. Justice

Microbiology ◽  
2011 ◽  
Vol 157 (6) ◽  
pp. 1750-1760 ◽  
Author(s):  
Katarzyna A. Duda ◽  
Buko Lindner ◽  
Helmut Brade ◽  
Andreas Leimbach ◽  
Elżbieta Brzuszkiewicz ◽  
...  

Mastitis represents one of the most significant health problems of dairy herds. The two major causative agents of this disease are Escherichia coli and Staphylococcus aureus. Of the first, its lipopolysaccharide (LPS) is thought to play a prominent role during infection. Here, we report the O-antigen (OPS, O-specific polysaccharide) structure of the LPS from bovine mastitis isolate E. coli 1303. The structure was determined utilizing chemical analyses, mass spectrometry, and 1D and 2D NMR spectroscopy methods. The O-repeating unit was characterized as -[→4)-β-d-Quip3NAc-(1→3)-α-l-Fucp2OAc-(1→4)-β-d-Galp-(1→3)-α-d-GalpNAc-(1→]- in which the O-acetyl substitution was non-stoichiometric. The nucleotide sequence of the O-antigen gene cluster of E. coli 1303 was also determined. This cluster, located between the gnd and galF genes, contains 13 putative open reading frames, most of which represent unknown nucleotide sequences that have not been described before. The O-antigen of E. coli 1303 was shown to substitute O-7 of the terminal ld-heptose of the K-12 core oligosaccharide. Interestingly, the non-OPS-substituted core oligosaccharide represented a truncated version of the K-12 outer core – namely terminal ld-heptose and glucose were missing; however, it possessed a third Kdo residue in the inner core. On the basis of structural and genetic data we show that the mastitis isolate E. coli 1303 represents a new serotype and possesses the K-12 core type, which is rather uncommon among human and bovine isolates.


2014 ◽  
Vol 151 (3) ◽  
pp. 1147-1154 ◽  
Author(s):  
Kenneth G. Ngwoke ◽  
Olivier Chevallier ◽  
Venasius K. Wirkom ◽  
Paul Stevenson ◽  
Christopher T. Elliott ◽  
...  

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