Abstract
An in vitro adherence assay was developed to study the adherence of Campylobacter pylori to mammalian cells. Strains of C. pylori were isolated from individuals with gastritis. These strains possessed the fibrillar N-acetylneuraminyllactose(neuraminlactose)-binding hemagglutinin (NLBH) and were found to adhere to monolayers of mouse Y-1 adrenal cells. Adherence was rapid, prevented by pretreatment of the Y-1 cells with Clostridium perfringens neuraminidase, and blocked by the neuraminlactose-containing protein fetuin. Electron microscopy by the immunogold technique and with anti-NLBH antibody showed that NLBH was present at the sites of interaction between C. pylori and the Y-1 cells. These results indicate that the Y-1 monolayer is a valid model for receptor-specific adherence of C. pylori.
MeSH Terms
Adrenal Glands/microbiology,ultrastructure
Animals
Bacterial Adhesion/drug effects
Bacterial Proteins/physiology
Campylobacter/physiology,ultrastructure
Cell Line
Clostridium perfringens/enzymology
Colony Count, Microbial
Culture Techniques
Kinetics
Mice
Neuraminidase/pharmacology
Receptors, Immunologic/physiology
alpha-Fetoproteins/pharmacology
Chemicals
Bacterial Proteins
Receptors, Immunologic
alpha-Fetoproteins
bacterial adhesin receptor
Neuraminidase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Evans D G
Department of Medicine, Baylor College of Medicine, Houston, Texas 77030.
Evans D J
Graham D Y
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