Multiple beta 1 chain integrins are receptors for invasin, a protein that promotes bacterial penetration into mammalian cells

Cell. 1990 Mar 9;60(5):861-71. doi: 10.1016/0092-8674(90)90099-z.

Abstract

Mammalian cell receptors that promote entry of intracellular bacteria into nonphagocytic cells have not been identified. We show here that multiple members of the integrin superfamily of cell adhesion receptors bind the Y. pseudotuberculosis invasin protein prior to bacterial penetration into mammalian cells. Affinity chromatography of crude detergent extracts demonstrated that integrins containing the subunit structures alpha 3 beta 1, alpha 5 beta 1, and alpha 6 beta 1 bound to immobilized invasin. Furthermore, phospholipid vesicles containing isolated integrin proteins were able to attach to invasin. Specificity for invasin binding to the identified integrin receptors was also demonstrated, as immunoprobing and phospholipid reconstitution studies showed that the alpha 2 beta 1 integrin, beta 2 chain integrins, and vitronectin receptor (alpha v beta 3) were not involved in cellular attachment to invasin.

Publication types

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

MeSH terms

  • Adhesins, Bacterial*
  • Amino Acid Sequence
  • Bacterial Proteins / metabolism*
  • Blood Platelets / physiology
  • Humans
  • Integrins / genetics
  • Integrins / physiology*
  • Kinetics
  • Liposomes
  • Macromolecular Substances
  • Molecular Sequence Data
  • Phosphatidylcholines
  • Yersinia pseudotuberculosis / physiology*

Substances

  • Adhesins, Bacterial
  • Bacterial Proteins
  • Integrins
  • Liposomes
  • Macromolecular Substances
  • Phosphatidylcholines
  • invasin, Yersinia