title: The terminal A domain of the fibrillar accumulation-associated protein (Aap) of Staphylococcus epidermidis mediates adhesion to human corneocytes.
abstract: The opportunistic pathogen Staphylococcus epidermidis colonizes indwelling medical devices by biofilm formation but is primarily a skin resident. In many S. epidermidis strains biofilm formation is mediated by a cell wall-anchored protein, the accumulation-associated protein (Aap). Here, we investigate the role of Aap in skin adhesion. Aap is an LPXTG protein with a domain architecture including a terminal A domain and a B-repeat region. S. epidermidis NCTC 11047 expresses Aap as localized, lateral tufts of fibrils on one subpopulation of cells (Fib(+)), whereas a second subpopulation does not express these fibrils of Aap (Fib(-)). Flow cytometry showed that 72% of NCTC 11047 cells expressed Aap and that 28% of cells did not. Aap is involved in the adhesion of Fib(+) cells to squamous epithelial cells from the hand (corneocytes), as the recombinant A-domain protein partially blocked binding to corneocytes. To confirm the role of the Aap A domain in corneocyte attachment, Aap was expressed on the surface of Lactococcus lactis MG1363 as sparsely distributed, peritrichous fibrils. The expression of Aap increased corneocyte adhesion 20-fold compared to L. lactis carrying Aap without an A domain. S. epidermidis isolates from catheters, artificial joints, skin, and the nose also used the A domain of Aap to adhere to corneocytes, emphasizing the role of Aap in skin adhesion. In addition, L. lactis expressing Aap with different numbers of B repeats revealed a positive correlation between the number of B repeats and adhesion to corneocytes, suggesting an additional function for the B region in enhancing A-domain-dependent attachment to skin. Therefore, in addition to its established role in biofilm formation, Aap can also promote adhesion to corneocytes and is likely to be an important adhesin in S. epidermidis skin colonization.
authors.affiliation: Faculty of Life Sciences, D1401 Michael Smith Building, the University of Manchester, Oxford Road, Manchester M13 9PT, United Kingdom.
authors.forename: Robin L
authors.initials: RL
authors.lastname: Macintosh
authors.forename: Jane L
authors.initials: JL
authors.lastname: Brittan
authors.forename: Ritwika
authors.initials: R
authors.lastname: Bhattacharya
authors.forename: Howard F
authors.initials: HF
authors.lastname: Jenkinson
authors.forename: Jeremy
authors.initials: J
authors.lastname: Derrick
authors.forename: Mathew
authors.initials: M
authors.lastname: Upton
authors.forename: Pauline S
authors.initials: PS
authors.lastname: Handley
mesh_terms: D001422:Bacterial Adhesion / Q000235:genetics / Q000502:physiology*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D015153:Blotting, Western; D002478:Cells, Cultured; D000078404:Epidermal Cells; D004817:Epidermis / Q000382:microbiology* / Q000648:ultrastructure; D005434:Flow Cytometry; D006801:Humans; D013294:Lactococcus lactis / Q000235:genetics / Q000378:metabolism / Q000502:physiology* / Q000648:ultrastructure; D046529:Microscopy, Electron, Transmission; D013212:Staphylococcus epidermidis / Q000235:genetics / Q000378:metabolism* / Q000502:physiology* / Q000648:ultrastructure
chemical_list: D001426:Bacterial Proteins