pH-dependent binding of Helicobacter pylori to pig gastric mucins.
A microtiter-based assay was developed to study the binding of Helicobacter pylori to pig gastric mucins purified by density-gradient centrifugation in CsCl/4 M guanidinium chloride. Binding of H. pylori was observed over the 'mucin' band as well as with 'low-density' components in the gradients, and binding to the latter was more pronounced when incubations were performed at 37 degrees C as compared to 20 degrees C. At a lower pH, binding of H. pylori (strain SVA 40) to the 'high-density' mucins from pig antrum was increased but binding to the 'low-density' ones was decreased. Binding of the P466 strain (Le(b)-specific) was mainly associated with the 'mucin' band, whereas the MO19 strain reacted preferentially with the 'low-density' components. In summary, H. pylori may bind to gastric mucins and the binding is influenced by temperature, pH and the repertoire of bacterial adhesins.
Nordman
H
H
Mucosal Biology Group, CMB, Lund University, Sweden.
Borén
T
T
Davies
J R
JR
Engstrand
L
L
Carlstedt
I
I
D000328:Adult; D000818:Animals; D001422:Bacterial Adhesion; D002499:Centrifugation, Density Gradient; D004195:Disease Models, Animal; D005753:Gastric Mucosa / Q000378:metabolism / Q000382:microbiology*; D016481:Helicobacter Infections / Q000382:microbiology; D016480:Helicobacter pylori / Q000302:isolation & purification / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008297:Male; D009077:Mucins / Q000378:metabolism*; D010437:Peptic Ulcer / Q000382:microbiology; D013552:Swine
D009077:Mucins