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Infection and Immunity, September 2006, p. 5414-5418, Vol. 74, No. 9
0019-9567/06/$08.00+0 doi:10.1128/IAI.00172-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Christina Morris,
and
Jim Hackett*
Department of Biochemistry, Hong Kong University of Science and Technology, Clear Water Bay, Hong Kong, China
Received 1 February 2006/ Returned for modification 19 April 2006/ Accepted 14 June 2006
Salmonella enterica serovar Typhi and some strains (Vi+) of serovar Dublin use type IVB pili to facilitate bacterial self-association, but only when the PilV proteins (potential minor pilus proteins) are not synthesized. Pilus-mediated self-association may be important in the pathogenesis of enteric fever. We have shown previously that the extent of DNA supercoiling controls the rate of Rci-catalyzed inversion of a DNA fragment which includes the C-terminal portions of the PilV proteins. This inversion therefore controls PilV synthesis as a high inversion rate prohibits transcription of pilV-encoding DNA. Here, we describe the manner in which PilV protein expression inhibits bacterial self-association and present data which suggest that incorporation of one or a few PilV protein molecules into a growing pilus, comprised of PilS subunits, causes the pilus to detach at the bacterial membrane. The bacteria are then unable to self-associate. We suggest that this phenomenon may be relevant to the pathogenesis of typhoid fever.
Present address: School of Optometry, University of California, Berkeley, CA 94720-2020.
Contact Christina Morris for strains or biological materials. E-mail: bctina{at}ust.hk.
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