Open Access

Integrin receptors play a role in the internalin B-dependent entry of Listeria monocytogenes into host cells

  • Clementina Auriemma1,
  • Maurizio Viscardi1,
  • Simona Tafuri2,
  • Luigi Michele Pavone2,
  • Federico Capuano1,
  • Laura Rinaldi3,
  • Rossella Della Morte2,
  • Giuseppe Iovane1, 3 and
  • Norma Staiano2Email author
Cellular & Molecular Biology LettersAn International Journal201015:19

DOI: 10.2478/s11658-010-0019-z

Received: 30 December 2009

Accepted: 28 May 2010

Published: 4 June 2010

Abstract

Listeria monocytogenes enters non-phagocytic cells by binding its surface proteins inlA (internalin) and inlB to the host’s E-cadherin and Met, respectively. The two internalins play either separate or cooperative roles in the colonization of infected tissues. Here, we studied bacterial uptake into HeLa cells using an L. monocytogenes mutant strain (ΔinlA) carrying a deletion in the gene coding for inlA. The ΔinlA mutant strain showed the capability to invade HeLa cells. The monoclonal anti-β3- and anti-β1-integrin subunit antibodies prevented bacterial uptake into the cells, while the anti-β2- and anti-β4-integrin subunit antibodies failed to affect L. monocytogenes entry into HeLa cells. Three structurally distinct disintegrins (kistrin, echistatin and flavoridin) also inhibited bacterial uptake, showing different potencies correlated to their selective affinity for the β3- and β1-integrin subunits. In addition to inducing Met phosphorylation, infection of cells by the L. monocytogenes ΔinlA mutant strain promoted the tyrosine phosphorylation of the focal adhesion-associated proteins FAK and paxillin. Our findings provide the first evidence that β3- and β1-integrin receptors play a role in the inlB-dependent internalization of L. monocytogenes into host cells.

Key words

Listeria monocytogenes Internalin B Integrins FAK Paxillin

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