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J. Bacteriol. doi:10.1128/JB.00952-06
Copyright (c) 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Localized tufts of fibrils on Staphylococcus epidermidis NCTC 11047 are comprised of the Accumulation Associated Protein (Aap)

Faculty of Life Sciences, 1.800 Stopford Building, The University of Manchester, Oxford Road, M13 9PT, UK; Wirral Hospital NHS Trust, Arrowe Park Hospital, Arrowe Park Road, Upton, Wirral, Merseyside, LH49 5PE, UK; Dept. of Microbiology, Moyne Institute of Preventative Medicine, Trinity College, Dublin 2, Ireland; Institut für Medizinische Mikrobiologie, Virologie und Hygiene, Zentrum für Klinische Pathologie, Universitätsklinikum Hamburg-Eppendorf, Martinistrasse 52, 20246 Hamburg, Germany; Medical Microbiology and Infectious Diseases, The School of Medicine, University of Wales Swansea, Singleton Park, Swansea SA2 8PP, UK; NeuTec Pharma PLC, Clinical Sciences Building 1, Manchester Royal Infirmary, Oxford Road, Manchester, M13 9WL, UK; Faculty of Life Sciences, MIB Building, North Campus, The University of Manchester; Division of Laboratory and Regenerative Medicine, School of Medicine, The University of Manchester, Clinical Sciences Building 1, Manchester Royal Infirmary, Oxford Road, Manchester, M13 9WL, UK

^* To whom correspondence should be addressed. Email: p.handley{at}man.ac.uk.

	Abstract

Staphylococcus epidermidis is both a human skin commensal and an opportunistic pathogen, causing infections linked to implanted medical devices. This paper describes localized tufts of fibrillar appendages on a sub-population (25%) of wild type (WT) S. epidermidis NCTC 11047 cells. The fibrils (122.2 +/- 10.8 nm long) are usually in a lateral position on the cells. Fibrillar (Fib+) and non-fibrillar (Fib-) sub-populations were separated (enriched) by 34 sequential partitions of wild type (WT) cells between a buffer phase and a hexadecane phase. Following enrichment, hydrophobic cells from the hexadecane phase comprised of 70 % Fib+ cells and the less hydrophobic cells from the buffer phase comprised entirely of Fib- cells. The Fib+ and Fib- sub-populations did not revert on subculture (x 34) on solid medium. SDS PAGE of cell surface proteins from WT, Fib+ and Fib- cells revealed two high molecular mass proteins (280 kDa and 230 kDa) on the WT and Fib+ cells that were absent from the Fib- cells. Amino acid sequencing revealed that fragments of both the 280 and 230 kDa proteins had 100 % identity to the accumulation associated protein (Aap). Aap is known to cause biofilm formation if it is truncated by loss of the terminal A domain. Immunogold staining with anti-Aap antibodies labelled tuft fibrils of the WT and Fib+ cells, but not the cell surface of Fib- cells. The tufts labelled with N-terminal directed antibodies (anti-A domain) showing that the fibrillar Aap was not truncated on the cell surface. Thus the presence of full length Aap correlated with the low biofilm forming ability of both WT and Fib+ S. epidermidis NCTC 11047 populations. RT-PCR showed that aap was transcribed in both Fib+ and Fib- cells. We therefore propose that full length Aap is expressed on cells of S. epidermidis NCTC 11047 as tufts of short fibrils and that fibril expression is regulated at a posttranscriptional level.

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