J Med Microbiol Email Content Delivery
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Senior, B. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Senior, B. W.
Agricola
Right arrow Articles by Senior, B. W.

The Journal of Medical Microbiology, Vol 16, Issue 3 323-331, Copyright © 1983 by Society for General Microbiology


JOURNAL ARTICLE

The purification, structure and synthesis of proticine 3

B. W. Senior

The ability of Proteus mirabilis to produce the bacteriocin, proticine 3, is found almost exclusively in strains that cause severe infections of the upper urinary tract. Proticine 3 was purified from lysates of mitomycin C-induced cultures. Biological activity was associated with structures resembling bacteriophage tails which, when first produced, were in the form of "nails" with one pointed end and a base plate with appendages at the other end. This form was unstable and changed to a "rocket" form in which the outer sheath contracted and thickened to reveal a protruding, hollow core that often became detached from the sheath. Purified proticine 3 comprises two major and nine minor proteins. Fluorography showed that during production of the proticine, a 58,000 mol. wt protein was synthesized late in the induction process and became the most intensely labelled protein in the culture. Synthesis of this protein coincided with the appearance and increase in titre of biologically-active proticine within the cell and with the appearance of "nail" forms. The protein is believed to be shed when an active "nail" is converted to an inactive "rocket" and to be either the component of proticine 3 associated with its lethal activity, or the protein required for the correct assembly of the constituent components into a biologically-active particle. The role of proticine 3 as a virulence factor is discussed.


This article has been cited by other articles:


Home page
ScienceHome page
K. A. Gibbs, M. L. Urbanowski, and E. P. Greenberg
Genetic Determinants of Self Identity and Social Recognition in Bacteria
Science, July 11, 2008; 321(5886): 256 - 259.
[Abstract] [Full Text] [PDF]


Home page
Appl. Environ. Microbiol.Home page
A. Jabrane, A. Sabri, P. Compere, P. Jacques, I. Vandenberghe, J. Van Beeumen, and P. Thonart
Characterization of Serracin P, a Phage-Tail-Like Bacteriocin, and Its Activity against Erwinia amylovora, the Fire Blight Pathogen
Appl. Envir. Microbiol., November 1, 2002; 68(11): 5704 - 5710.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
INT J SYST EVOL MICROBIOL J MED MICROBIOL MICROBIOLOGY J GEN VIROL ALL SGM JOURNALS
Copyright © 1983 Society for General Microbiology.