Receptor-mediated adherence of Campylobacter pylori to mouse Y-1 adrenal cell monolayers

Infect Immun. 1989 Aug;57(8):2272-8. doi: 10.1128/iai.57.8.2272-2278.1989.

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.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adrenal Glands / microbiology*
  • Adrenal Glands / ultrastructure
  • Animals
  • Bacterial Adhesion* / drug effects
  • Bacterial Proteins / physiology*
  • Campylobacter / physiology*
  • Campylobacter / ultrastructure
  • Cell Line
  • Clostridium perfringens / enzymology
  • Colony Count, Microbial
  • Culture Techniques
  • Kinetics
  • Mice
  • Neuraminidase / pharmacology
  • Receptors, Immunologic / physiology*
  • alpha-Fetoproteins / pharmacology

Substances

  • Bacterial Proteins
  • Receptors, Immunologic
  • alpha-Fetoproteins
  • bacterial adhesin receptor
  • Neuraminidase