Subversion of antimicrobial calprotectin (S100A8/S100A9 complex) in the cytoplasm of TR146 epithelial cells after invasion by Listeria monocytogenes

Author(s)

Zaia, A. A. ^{[1, 2, 3]} ; Sappington, K. J. ^{[1, 2]} ; Nisapakultorn, K. ^{[1, 2]} ; Chazin, W. J. ^[4] ; Dietrich, E. A. ^{[1, 2]} ; Ross, K. F. ^{[1, 2]} ; Herzberg, M. C. ^{[1, 2]}

Affiliation

^[1] Univ Minnesota, Sch Dent, Dept Diagnost & Biol Sci, Minneapolis, MN 55455 - USA

^[2] Minneapolis VA Med Ctr, Mucosal & Vaccine Res Ctr, Minneapolis, MN - USA

^[3] Univ Estadual Campinas, Sch Dent, Dept Restorat Sci, Campinas - Brazil

^[4] Vanderbilt Univ, Dept Biochem, Struct Biol Ctr, Nashville, TN 37232 - USA

• Document type: Journal article
• Source: MUCOSAL IMMUNOLOGY; v. 2, n. 1, p. 43-53, JAN 2009.
• Web of Science Citations: 29

Abstract

Expressed by squamous mucosal keratinocytes, calprotectin is a complex of two EF-hand calcium-binding proteins of the S100 subfamily (S100A8 and S100A9) with significant antimicrobial activity. Calprotectin-expressing cells resist invasion by Porphyromonas gingivalis, Listeria monocytogenes, and Salmonella enterica serovar Typhimurium ( S. typhimurium). To understand the interactions between calprotectin and invasive bacteria, we studied the distribution of calprotectin in the cytoplasm of TR146 epithelial cells. In response to L. monocytogenes, calprotectin mobilized from a diffuse cytoplasmic distribution to a filamentous pattern and colocalized with the microtubule network. Listeria more frequently invaded cells with mobilized calprotectin. Calprotectin mobilization was listeriolysin O-dependent and required calcium ( extracellular and intracellular) and an intact microtubule network. In the presence of preformed microtubules in vitro, the anti-Listeria activity of calprotectin was abrogated. To facilitate intraepithelial survival, therefore, Listeria mobilizes calprotectin to colocalize with cytoplasmic microtubules, subverting anti-Listeria activity and autonomous cellular immunity. (AU)