Exploring the Synthetic Application of Helicobacter pylori α1,3/4-Fucosyltransferase FucTIII toward the Syntheses of Fucosylated Human Milk Glycans and Lewis Antigens

ACS Catalysis ◽  
2019 ◽  
Vol 9 (12) ◽  
pp. 10712-10720 ◽  
Author(s):  
Teng-Wei Tsai ◽  
Jia-Lin Fang ◽  
Chin-Yu Liang ◽  
Chi-Jen Wang ◽  
Yu-Ting Huang ◽  
...  



2005 ◽  
Vol 58 (5) ◽  
pp. 897-902 ◽  
Author(s):  
Maria Weyermann ◽  
Cathleen Borowski ◽  
Günter Bode ◽  
Bilge Gürbüz ◽  
Guido Adler ◽  
...  


2012 ◽  
Vol 2012 ◽  
pp. 1-4 ◽  
Author(s):  
Ken-ichi Amano ◽  
Shin-ichi Yokota ◽  
Mario A. Monteiro

We compared the serological reactivity of lipopolysaccharides (LPS) isolated from Japanese and Western strains of Helicobacter pylori against anti-Lewis antigen monoclonal antibodies and H. pylori-positive Japanese sera. The two LPS from Western strains (26695 and O:2) did not react with any sera from Japanese patients, while all LPS from Japanese strains and the Sydney strain reacted with these sera. We propose that LPS of all Japanese smooth strains share either one of two epitopes, which are termed highly antigenic and weakly antigenic epitopes, present in the O-polysaccharide portion, and these epitopes are independent the Lewis antigens. The present findings indicated that the two Western strains lacked the two epitopes, which are shared by all Japanese strains.



Author(s):  
Ming Tan ◽  
Xi Jiang

Noroviruses (NoVs) and rotaviruses (RVs), the two most important causes of viral acute gastroenteritis, are found to recognise histo-blood group antigens (HBGAs) as receptors or ligands for attachment. Human HBGAs are highly polymorphic containing ABO, secretor and Lewis antigens. In addition, both NoVs and RVs are highly diverse in how they recognise these HBGAs. Structural analysis of the HBGA-binding interfaces of NoVs revealed a conserved central binding pocket (CBP) interacting with a common major binding saccharide (MaBS) of HBGAs and a variable surrounding region interacting with additional minor binding saccharides. The conserved CBP indicates a strong selection of NoVs by the host HBGAs, whereas the variable surrounding region explains the diverse recognition patterns of different HBGAs by NoVs and RVs as functional adaptations of the viruses to human HBGAs. Diverse recognition of HBGAs has also been found in bacterial pathogenHelicobacter pylori. Thus, exploratory research into whether such diverse recognitions also occur for other viral and bacterial pathogens that recognise HBGAs is warranted.



2000 ◽  
Vol 118 (4) ◽  
pp. A1254
Author(s):  
Kenji Kamiya ◽  
Tomiyasu Arisawa ◽  
Hidemi Goto ◽  
Tetsuo Hayakawa ◽  
Michio Ohta


Toxins ◽  
2021 ◽  
Vol 13 (7) ◽  
pp. 485
Author(s):  
Dalla Doohan ◽  
Yudith Annisa Ayu Rezkitha ◽  
Langgeng Agung Waskito ◽  
Yoshio Yamaoka ◽  
Muhammad Miftahussurur

Helicobacter pylori is a pathogenic microorganism that successfully inhabits the human stomach, colonizing it by producing several virulence factors responsible for preventing host self-defense mechanisms. The adherence mechanism to gastric mucosal tissue is one of the most important processes for effective colonization in the stomach. The blood group antigen-binding adhesion (BabA) and sialic acid-binding adherence (SabA) are two H. pylori outer membrane proteins able to interact with antigens in the gastroduodenal tract. H. pylori possesses several mechanisms to control the regulation of both BabA and SabA in either the transcriptional or translational level. BabA is believed to be the most important protein in the early infection phase due to its ability to interact with various Lewis antigens, whereas SabA interaction with sialylated Lewis antigens may prove important for the adherence process in the inflamed gastric mucosal tissue in the ongoing-infection phase. The adherence mechanisms of BabA and SabA allow H. pylori to anchor in the gastric mucosa and begin the colonization process.





1996 ◽  
Vol 34 (9) ◽  
pp. 2196-2200 ◽  
Author(s):  
I M Simoons-Smit ◽  
B J Appelmelk ◽  
T Verboom ◽  
R Negrini ◽  
J L Penner ◽  
...  


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