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Microbiology 152 (2006), 2875-2883; DOI  10.1099/mic.0.29158-0
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Microbiology 152 (2006), 2875-2883; DOI  10.1099/mic.0.29158-0
© 2006 Society for General Microbiology

A mannose-sensitive haemagglutinin (MSHA)-like pilus promotes attachment of Pseudoalteromonas tunicata cells to the surface of the green alga Ulva australis

Doralyn S. Dalisay1, Jeremy S. Webb2,3,{dagger}, André Scheffel4, Charles Svenson2, Sally James2,3, Carola Holmström2,3, Suhelen Egan2,3 and Staffan Kjelleberg2,3

1 Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA
2 School of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney, NSW 2052, Australia
3 Centre for Marine Biofouling and Bio-innovation, University of New South Wales, Sydney, NSW 2052, Australia
4 Max-Planck-Institute for Marine Microbiology, Celsiusstraße 1 28359, Bremen, Germany

Correspondence
Staffan Kjelleberg
s.kjelleberg{at}unsw.edu.au

This study demonstrates that attachment of the marine bacterium Pseudoalteromonas tunicata to the cellulose-containing surface of the green alga Ulva australis is mediated by a mannose-sensitive haemagglutinin (MSHA-like) pilus. We have identified an MSHA pilus biogenesis gene locus in P. tunicata, termed mshI1I2JKLMNEGFBACDOPQ, which shows significant homology, with respect to its genetic characteristics and organization, to the MSHA pilus biogenesis gene locus of Vibrio cholerae. Electron microscopy studies revealed that P. tunicata wild-type cells express flexible pili peritrichously arranged on the cell surface. A P. tunicata mutant (SM5) with a transposon insertion in the mshJ region displayed a non-piliated phenotype. Using SM5, it has been demonstrated that the MSHA pilus promotes attachment of P. tunicata wild-type cells in polystyrene microtitre plates, as well as to microcrystalline cellulose and to the living surface of U. australis. P. tunicata also demonstrated increased pilus production in response to cellulose and its monomer constituent cellobiose. The MSHA pilus thus functions as a determinant of attachment in P. tunicata, and it is proposed that an understanding of surface sensing mechanisms displayed by P. tunicata will provide insight into specific ecological interactions that occur between this bacterium and higher marine organisms.


Abbreviations: CLSM, confocal laser scanning microscopy; GFP, green fluorescent protein; MSHA, mannose-sensitive haemagglutinin; RFP, red fluorescent protein; TEM, transmission electron microscopy

The GenBank/EMBL/DDBJ accession numbers for the sequences reported in this paper are AY695819 and ZP_01133305–ZP_01133315.

{dagger}Present address: School of Biological Sciences, University of Southampton, Southampton SO16 7PX, UK.




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