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J Gen Virol 37 (1977), 337-347; DOI 10.1099/0022-1317-37-2-337
© 1977 Society for General Microbiology
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Adsorption of a Phage Tail-Like Bacteriocin to Isolated Lipopolysaccharide of Rhizobium

Herbert Pfister* and Günter Lodderstaedt

Institut für Mikrobiologie und Biochemie, Lehrstuhl für Mikrobiologie, Universität Erlangen-Nürnberg, 852 Erlangen, Friedrichstrasse. 33, Germany

Purified lipopolysaccharide (LPS) from the bacteriocin sensitive strain Rhizobium lupini 16-2 was shown to neutralize the killing activity of the bacteriocin. In the electron microscopical preparation the phage tail-like bacteriocin appears to be adsorbed to the LPS; the tail sheath is contracted and the fibres are oriented towards the LPS ribbon. In contrast, no interaction was observed between the bacteriocin and the LPS of two resistant strains of Rhizobium (16-2/I1 and 16-3). The inactivation of the bacteriocin by LPS depends on salt concentration, pH, and temperature. The receptor activity of LPS was destroyed by mild acid hydrolysis and by treatment with deoxycholate, which indicates that the micellar structure of the LPS is necessary for bacteriocin adsorption. The chemical composition of the 16-2 LPS was compared to that of the LPS of two resistant strains. In the case of 16-2/I1 LPS minor modifications suffice to confer resistance against the bacteriocin.

* Present address: Institut für Virologie, Zentrum für Hygiene, Herrmann-Herder-Str. 11, 78 Freiburg, Germany.

Received 19 April 1977; accepted 13 June 1977.




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Copyright © 1977 by the Society for General Microbiology.