Morphological Studies on Relaxed and Contracted Forms of Purified Pyocin Particles

Author:

Higerd Thomas B.1,Baechler Charles A.1,Berk Richard S.1

Affiliation:

1. Department of Microbiology, Wayne State University School of Medicine, Detroit, Michigan 48207

Abstract

The bacteriocin from Pseudomonas aeruginosa , pyocin, consists of a contractile sheath and inner core reminiscent of T-even coliphage tails. Contraction of the outer sheath was found to be promoted by 0.5 m magnesium chloride, 1% Formalin, low p H, sonic treatment, and freezing or thawing or both. The contraction caused by 0.5 m magnesium chloride, however, was found to be reversible and occurred upon reduction of the salt concentration from 0.5 to 0.02 m . In addition, direct assay showed that pyocin activity was nearly proportional to the percentage of only uncontracted forms. Initial studies suggested that the adsorption of purified pyocin onto cell wall fragments from the sensitive indicator strain of P. aeruginosa occurs with the relaxed particle only and not with the contracted form. However, after adsorption, contraction occurred. Various morphological structures, such as tail fibers and base-platelike appendages, were also observed. Upon contraction, six tail fibers were observed on many particles, four of which appeared to originate from the sheath and two from the inner core. Polysheaths and polycores several hundred nanometers in length were also occasionally observed.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference25 articles.

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3. The structure of pyocin particles released from Pseudomonas aeruginosa by mitomycin C;Bradley D. E.;Int. Congr. Electron Microscopy,1966

4. The structure and infective process of a contractile Pseudomonas aeruginosa bacteriophage;Bradley D. E.;J. Gen. Virol.,1968

5. A negative staining method for high resolution electron microscopy of viruses;Brenner S.;Biochim. Biophys. Acta,1959

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