Measurements of the binding force between the Helicobacter pylori adhesin BabA and the Lewis b blood group antigen using optical tweezers

2005 ◽  
Vol 10 (4) ◽  
pp. 044024 ◽  
Author(s):  
Oscar Björnham ◽  
Erik Fällman ◽  
Ove Axner ◽  
Jörgen Ohlsson ◽  
Ulf J. Nilsson ◽  
...  
2019 ◽  
Vol 27 (3) ◽  
pp. 193-199 ◽  
Author(s):  
Ashraf A. Hassan ◽  
Amany I. Youssef ◽  
Abeer A. Ghazal ◽  
Manal I. Sheta ◽  
Nabil L. Diwedar ◽  
...  

Helicobacter ◽  
2004 ◽  
Vol 9 (4) ◽  
pp. 324-329 ◽  
Author(s):  
Dietrich Rothenbacher ◽  
Maria Weyermann ◽  
Gunter Bode ◽  
Murrat Kulaksiz ◽  
Bernd Stahl ◽  
...  

2006 ◽  
Vol 74 (5) ◽  
pp. 3046-3051 ◽  
Author(s):  
Ewa E. Hennig ◽  
Johnna M. Allen ◽  
Timothy L. Cover

ABSTRACT Helicobacter pylori babA encodes an outer membrane protein that binds to fucosylated Lewis b blood group antigen. We analyzed a panel of 35 H. pylori strains and identified three possible chromosomal loci for babA. There was a significant association between the presence of babA and the presence of cagA (P = 0.0001). Phylogenetic analysis of babA alleles revealed two divergent families of signal sequences. Among 17 strains in which an intact in-frame babA allele was identified, 10 expressed a detectable BabA protein. Expression of a BabA protein and the Lewis b-binding phenotype were not dependent on the chromosomal locus of babA. These data indicate that there is marked heterogeneity among H. pylori strains in babA genetic content and BabA expression.


2009 ◽  
Vol 96 (3) ◽  
pp. 409a ◽  
Author(s):  
Katja Petzold ◽  
Annelie Olofsson ◽  
Anna Arnqvist ◽  
Thomas Boren ◽  
Gerhard Gröbner ◽  
...  

2014 ◽  
Vol 11 (101) ◽  
pp. 20141040 ◽  
Author(s):  
P. Parreira ◽  
Q. Shi ◽  
A. Magalhaes ◽  
C. A. Reis ◽  
J. Bugaytsova ◽  
...  

The strength of binding between the Helicobacter pylori blood group antigen-binding adhesin (BabA) and its cognate glycan receptor, the Lewis b blood group antigen (Le b ), was measured by means of atomic force microscopy. High-resolution measurements of rupture forces between single receptor–ligand pairs were performed between the purified BabA and immobilized Le b structures on self-assembled monolayers. Dynamic force spectroscopy revealed two similar but statistically different bond populations. These findings suggest that the BabA may form different adhesive attachments to the gastric mucosa in ways that enhance the efficiency and stability of bacterial adhesion.


2011 ◽  
Vol 203 (5) ◽  
pp. 726-735 ◽  
Author(s):  
Tomoyuki Ohno ◽  
Anna Vallström ◽  
Massimo Rugge ◽  
Hiroyoshi Ota ◽  
David Y. Graham ◽  
...  

2020 ◽  
Vol 137 ◽  
pp. 103079
Author(s):  
Jing Xue ◽  
Lei Li ◽  
Feifei Li ◽  
Na Li ◽  
Tao Li ◽  
...  

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