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Journal of Bacteriology, February 2005, p. 1173-1181, Vol. 187, No. 3
0021-9193/05/$08.00+0     doi:10.1128/JB.187.3.1173-1181.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

NopB, a Type III Secreted Protein of Rhizobium sp. Strain NGR234, Is Associated with Pilus-Like Surface Appendages

LBMPS, Département de Biologie Végétale, Université de Genève, Sciences III, Geneva, Switzerland,¹ Unité de Génétique Microbienne, INRA, Domaine de Vilvert, Jouy en Josas, France,² Department of Biological Sciences, Imperial College at Wye, University of London, Ashford, Kent, United Kingdom³

Received 20 August 2004/ Accepted 22 October 2004

Rhizobium sp. strain NGR234 possesses a functional type three secretion system (TTSS), through which a number of proteins, called nodulation outer proteins (Nops), are delivered to the outside of the cell. A major constraint to the identification of Nops is their low abundance in the supernatants of NGR234 strains grown in culture. To overcome this limitation, a more sensitive proteomics-based strategy was developed. Secreted proteins from wild-type NGR234 were separated by two-dimensional gel electrophoresis, and the gel was compared to similar gels containing the proteins from a TTSS mutant (NGRrhcN). To identify the proteins, spots unique to the NGR234 gels were analyzed by matrix-assisted laser desorption ionization-time of flight mass spectrometry and the data were compared to the sequence of the symbiotic plasmid of NGR234. A nonpolar mutant of one of these proteins was generated called NopB. NopB is required for Nop secretion but inhibits the interaction with Pachyrhizus tuberosus and augments nodulation of Tephrosia vogelii. Flavonoids and a functional TTSS are required for the formation of some surface appendages on NGR234. In situ immunogold labeling and isolation of these pili showed that they contain NopB.

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