title: Expression and distribution of very late antigen-5 in mouse peritoneal macrophages upon ingestion of fibronectin-bound Staphylococcus aureus.
abstract: Many pathogens colonize host tissues by binding to the extracellular matrix via their cell surface adhesion molecules, which are called MSCRAMMs (microbial surface components recognizing adhesive matrix molecules). Staphylococcus aureus expresses several of these adhesion molecules, some of which bind to fibronectin. Of these adhesion molecules, fibronectin-binding proteins play a role in the pathogenicity of S. aureus, although it is not yet clear whether they enhance its virulence. We have previously shown that fibronectin-bound S. aureus is efficiently phagocytosed by thioglycolate-induced mouse peritoneal macrophages. Bacterial ingestion is mediated by Very Late Antigen-5 (VLA-5; alpha5beta1 integrin) and is accompanied by the formation of adhesion complexes. Here we show that the expression of VLA-5 is restricted to thioglycolate-induced inflammatory macrophages and is not found in the resident macrophages. When cells were in suspension, alpha5 integrin was not expressed on the surface of either resident or inflammatory macrophages, whereas in adherent cells, this integrin was distributed on the surface of inflammatory but not resident macrophages. A high level of this integrin was present in the cytoplasmic region only in inflammatory macrophages. In agreement with this, fibronectin-mediated phagocytosis of S. aureus was observed only in the inflammatory macrophages. In inflammatory macrophages ingesting fibronectin-bound S. aureus, alpha5 integrin was concentrated close to the phagocytosed bacteria. This change in distribution was not found in macrophages ingesting untreated bacteria. Together with our previous work, these results indicate that, upon ingestion of fibronectin-bound S. aureus, VLA-5 accumulates in the area of phagocytosis in inflammatory macrophages, where it forms adhesion complexes.
authors.affiliation: Department of Microbiology (II), The Jikei University School of Medicine, Tokyo, Japan. hshinji@jikei.ac.jp
authors.forename: Hitomi
authors.initials: H
authors.lastname: Shinji
authors.forename: Minori
authors.initials: M
authors.lastname: Kamada
authors.forename: Keiko
authors.initials: K
authors.lastname: Seki
authors.forename: Akiko
authors.initials: A
authors.lastname: Tajima
authors.forename: Tadayuki
authors.initials: T
authors.lastname: Iwase
authors.forename: Shogo
authors.initials: S
authors.lastname: Masuda
mesh_terms: D000818:Animals; D000954:Antigens, Surface / Q000032:analysis; D002478:Cells, Cultured; D003593:Cytoplasm / Q000737:chemistry; D005260:Female; D005353:Fibronectins / Q000378:metabolism; D005434:Flow Cytometry; D015870:Gene Expression; D006651:Histocytochemistry; D039081:Integrin alpha5beta1 / Q000096:biosynthesis / Q000378:metabolism*; D017737:Macrophages, Peritoneal / Q000276:immunology*; D051379:Mice; D008856:Microscopy, Fluorescence; D010587:Phagocytosis; D013211:Staphylococcus aureus / Q000276:immunology*
chemical_list: D000954:Antigens, Surface; D005353:Fibronectins; D039081:Integrin alpha5beta1