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Journal of Bacteriology, April 2003, p. 2628-2634, Vol. 185, No. 8
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.8.2628-2634.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

The Mechanism of Bacterial Infection by Filamentous Phages Involves Molecular Interactions between TolA and Phage Protein 3 Domains

Fredrik Karlsson, Carl A. K. Borrebaeck,^* Nina Nilsson, and Ann-Christin Malmborg-Hager

Department of Immunotechnology, Lund University, SE-220 07 Lund, Sweden

Received 6 September 2002/ Accepted 17 January 2003

The early events in filamentous bacteriophage infection of gram-negative bacteria are mediated by the gene 3 protein (g3p) of the virus. This protein has a sophisticated domain organization consisting of two N-terminal domains and one C-terminal domain, separated by flexible linkers. The molecular interactions between these domains and the known bacterial coreceptor protein (TolA) were studied using a biosensor technique, and we report here on interactions of the viral coat protein with TolA, as well as on interactions between the TolA molecules. We detected an interaction between the pilus binding second domain (N2) of protein 3 and the bacterial TolA. This novel interaction was found to depend on the periplasmatic domain of TolA (TolAII). Furthermore, extensive interaction was detected between TolA molecules, demonstrating that bacterial TolA has the ability to interact functionally with itself during phage infection. The kinetics of g3p binding to TolA is also different from that of bacteriocins, since both N-terminal domains of g3p were found to interact with TolA. The multiple roles for each of the separate g3p and TolA domains imply a delicate interaction network during the phage infection process and a model for the infection mechanism is hypothesized.

Present address: Affibody AB, SE-161 02 Bromma, Sweden.

Present address: Alligator Bioscience AB, SE-223 70 Lund, Sweden.

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