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

Cellular & Molecular Biology Letters

Maurizio Viscardi²  Federico Capuano²  Luigi Michele Pavone³  Simona Tafuri³  Giuseppe Iovane⁴  Laura Rinaldi¹  Norma Staiano³  Clementina Auriemma²  Rossella Morte³ 

[1] Dipartimento di Patologia e Sanità Animale, Università degli Studi di Napoli Federico II, Napoli, Italy$$;Istituto Zooprofilattico Sperimentale del Mezzogiorno, Portici (Na), Italy$$;Dipartimento di Strutture, Funzioni e Tecnologie Biologiche, Università degli Studi di Napoli Federico II, Napoli, Italy$$;Istituto Zooprofilattico Sperimentale del Mezzogiorno, Portici (Na), Italy$$Dipartimento di Patologia e Sanità Animale, Università degli Studi di Napoli Federico II, Napoli, Italy$$

关键词: Internalin B;    Integrins;    FAK;    Paxillin;   

DOI  :  10.2478/s11658-010-0019-z

学科分类：分子生物学，细胞生物学和基因

来源: Uniwersytet Wroclawski * Wydzial Biotechnologii / University of Wroclaw, Faculty of Biotechnology

【 摘 要 】

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.

【 授权许可】

Unknown