Dynamic force spectroscopy of the Helicobacter pylori BabA-Lewis b binding.
The binding strength of the Helicobacter pylori adhesin-receptor complex BabA-ABO/Lewis b has been analyzed by means of dynamic force spectroscopy. High-resolution measurements of rupture forces were performed in situ on single bacterial cells, expressing the high-affinity binding BabA adhesin, by the use of force measuring optical tweezers. The resulting force spectra revealed the mechanical properties of a single BabA-Leb bond. It was found that the bond is dominated by one single energy barrier and that it is a slip-bond. The bond length and thermal off-rate were assessed to be 0.86+/-0.07 nm and 0.015+/-0.006 s(-1), respectively.
Department of Applied Physics and Electronics, Umeå University, SE-901 87 Umeå, Sweden. oscar.bjornham@tfe.umu.se
Oscar
O
Björnham
Jeanna
J
Bugaytsova
Thomas
T
Borén
Staffan
S
Schedin
D000017:ABO Blood-Group System / Q000378:metabolism; D018829:Adhesins, Bacterial / Q000378:metabolism*; D006001:Glycoconjugates / Q000737:chemistry / Q000378:metabolism; D016480:Helicobacter pylori / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D007983:Lewis Blood Group Antigens / Q000378:metabolism*; D008954:Models, Biological; D052898:Optical Tweezers; D011485:Protein Binding; D013057:Spectrum Analysis
D000017:ABO Blood-Group System; D018829:Adhesins, Bacterial; C400429:BabA protein, Helicobacter pylori; D006001:Glycoconjugates; D007983:Lewis Blood Group Antigens