title: Fibronectin attachment protein is necessary for efficient attachment and invasion of epithelial cells by Mycobacterium avium subsp. paratuberculosis.
abstract: Attachment and ingestion of Mycobacterium avium subsp. paratuberculosis by two epithelial cell lines were enhanced by soluble fibronectin (FN). Peptide blocking of the FN attachment protein (FAP-P) inhibited the internalization of M. avium subsp. paratuberculosis. Disruption of FAP-P expression significantly reduced attachment and ingestion of M. avium subsp. paratuberculosis by T-24 and Caco-2 cells. The results indicate that the interaction between FN and FAP-P facilitates attachment and internalization of M. avium subsp. paratuberculosis by epithelial cells.
authors.affiliation: Department of Veterinary Pathobiology, Purdue University, West Lafayette, Indiana 47907, USA.
authors.forename: T E
authors.initials: TE
authors.lastname: Secott
authors.forename: T L
authors.initials: TL
authors.lastname: Lin
authors.forename: C C
authors.initials: CC
authors.lastname: Wu
mesh_terms: D018829:Adhesins, Bacterial / Q000502:physiology*; D000595:Amino Acid Sequence; D001422:Bacterial Adhesion; D018938:Caco-2 Cells; D004847:Epithelial Cells / Q000382:microbiology; D006801:Humans; D008969:Molecular Sequence Data; D016927:Mycobacterium avium subsp. paratuberculosis / Q000472:pathogenicity*
chemical_list: D018829:Adhesins, Bacterial; C117704:FAP-A protein, Mycobacterium avium