Identification and functional characterization of the putative polysaccharide biosynthesis protein (CapD) of Enterococcus faecium U0317

2016 ◽  
Vol 37 ◽  
pp. 215-224 ◽  
Author(s):  
Liaqat Ali ◽  
Meike Spiess ◽  
Dominique Wobser ◽  
Marta Rodriguez ◽  
Hubert E. Blum ◽  
...  
2013 ◽  
Vol 169 (3) ◽  
pp. 1001-1015 ◽  
Author(s):  
Paulraj Kanmani ◽  
K. Suganya ◽  
R. Satish kumar ◽  
N. Yuvaraj ◽  
V. Pattukumar ◽  
...  

SpringerPlus ◽  
2015 ◽  
Vol 4 (1) ◽  
Author(s):  
Deepansh Sharma ◽  
Baljeet Singh Saharan ◽  
Nikhil Chauhan ◽  
Suresh Procha ◽  
Sohan Lal

2021 ◽  
Author(s):  
Vanessa Wiltsie ◽  
Skye Travis ◽  
Madeline R. Shay ◽  
Zachary Simmons ◽  
Patrick Frantom ◽  
...  

2007 ◽  
Vol 189 (7) ◽  
pp. 2590-2598 ◽  
Author(s):  
Kerstin Steiner ◽  
René Novotny ◽  
Kinnari Patel ◽  
Evgenij Vinogradov ◽  
Chris Whitfield ◽  
...  

ABSTRACTThe glycan chain of the S-layer glycoprotein ofGeobacillus stearothermophilusNRS 2004/3a is composed of repeating units [→2)-α-l-Rhap-(1→3)-β-l-Rhap-(1→2)-α-l-Rhap-(1→], with a 2-O-methyl modification of the terminal trisaccharide at the nonreducing end of the glycan chain, a core saccharide composed of two or three α-l-rhamnose residues, and a β-d-galactose residue as a linker to the S-layer protein. In this study, we report the biochemical characterization of WsaP of the S-layer glycosylation gene cluster as a UDP-Gal:phosphoryl-polyprenol Gal-1-phosphate transferase that primes the S-layer glycoprotein glycan biosynthesis ofGeobacillus stearothermophilusNRS 2004/3a. Our results demonstrate that the enzyme transfers in vitro a galactose-1-phosphate from UDP-galactose to endogenous phosphoryl-polyprenol and that the C-terminal half of WsaP carries the galactosyltransferase function, as already observed for the UDP-Gal:phosphoryl-polyprenol Gal-1-phosphate transferase WbaP fromSalmonella enterica. To confirm the function of the enzyme, we show that WsaP is capable of reconstituting polysaccharide biosynthesis in WbaP-deficient strains ofEscherichia coliandSalmonella entericaserovar Typhimurium.


2020 ◽  
Vol 477 (7) ◽  
pp. 1261-1286 ◽  
Author(s):  
Marie Anne Richard ◽  
Hannah Pallubinsky ◽  
Denis P. Blondin

Brown adipose tissue (BAT) has long been described according to its histological features as a multilocular, lipid-containing tissue, light brown in color, that is also responsive to the cold and found especially in hibernating mammals and human infants. Its presence in both hibernators and human infants, combined with its function as a heat-generating organ, raised many questions about its role in humans. Early characterizations of the tissue in humans focused on its progressive atrophy with age and its apparent importance for cold-exposed workers. However, the use of positron emission tomography (PET) with the glucose tracer [18F]fluorodeoxyglucose ([18F]FDG) made it possible to begin characterizing the possible function of BAT in adult humans, and whether it could play a role in the prevention or treatment of obesity and type 2 diabetes (T2D). This review focuses on the in vivo functional characterization of human BAT, the methodological approaches applied to examine these features and addresses critical gaps that remain in moving the field forward. Specifically, we describe the anatomical and biomolecular features of human BAT, the modalities and applications of non-invasive tools such as PET and magnetic resonance imaging coupled with spectroscopy (MRI/MRS) to study BAT morphology and function in vivo, and finally describe the functional characteristics of human BAT that have only been possible through the development and application of such tools.


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