Lipopolysaccharide of Pseudomonas Aeruginosa With Special Reference to Pyocin R Receptor Activity

Ikeda, Kayoko; Egami, Fujio

doi:10.2323/jgam.19.115

Cited by 30 publications

(26 citation statements)

References 5 publications

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“…The chemical nature of the receptor substance was proved to be a lipopolysaccharide which could reversibly dissociate into smaller subunits (5). These results are similar to the observation that the receptor substance of E. coli T-series phages are lipopolysaccharide in nature (6-9).…”

supporting

confidence: 81%

“…Receptor activity of reassociated lipopolysaccharide free from aminosugar-rich fraction, described in the preceding paper, was low and unstable (5), therefore, 130P fraction and "preparation 1" in the previous papers (4,5) were used. Dependency of the inactivation reaction on the receptor concentration is Table 1.…”

Section: Properties O F Pyocin R Inactivation Reactionmentioning

confidence: 99%

“…In the previous papers, the preparation and chemical properties of Pyocin R receptor substance from P. aeruginosa were described (4,5). The chemical nature of the receptor substance was proved to be a lipopolysaccharide which could reversibly dissociate into smaller subunits (5).…”

mentioning

confidence: 99%

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Interaction Between Pyocin R and Pyocin R Receptor

Ikeda

Nishi

1973

J. Gen. Appl. Microbiol.

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1) Pyocin R-sensitive cells were digested with lysozyme in the presence of EDTA in hypertonic solution. Most of the receptor activity was solubilized, by this procedure, and separated from spheroplast membrane fraction. This suggested the location of receptor on the cell wall.2) Electron microscopic figure revealed the adsorption of pyocin R on the cell surface and its fragment. Pyocin particles were adsorbed on the receptor site with the contracted sheath, at the tip of core.3) Properties of interaction between pyocin R and its receptor were studied. Pyocin R inactivation by its adsorption to the receptor was highly dependent on temperature, and the presence of 0.1-0.2 M NaC1 was necessary for the optimal inactivation. 4) Size of receptor site required for the inactivation of a pyocin particle was estimated.Pyocin R is adsorbed on some strains of Pseudomonas aeruginosa and kills the bacterium by a single-hit killing process (1).About the action mechanism of pyocin R, KAZIRO and TANAKA reported that the pyocin R infection caused the complete stop of macromolecule synthesis and the degradation of ribosomes (2, 3).At the infection of bacteriocin such as colicin, the first step is considered to be the adsorption of the particle to the specific receptor site on the cell surface, but there has been no direct information about the chemical nature of the receptor and the interaction between the bacteriocin and the receptor.In the previous papers, the preparation and chemical properties of Pyocin

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supporting

confidence: 81%

Section: Properties O F Pyocin R Inactivation Reactionmentioning

confidence: 99%

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Interaction Between Pyocin R and Pyocin R Receptor

Ikeda

Nishi

1973

J. Gen. Appl. Microbiol.

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“…2 and 3, respectively) of the LPS molecules in the low-molecular-weight population and 30 to 50% in the high-molecular-weight fractions (36,48). It (47), antibiotic susceptibility (la, 4, 18), LPS aggregate structure (47), bacteriophage recognition (25,27), immunochemical characterization (8,9,49), virulence (11,50), protection against the bactericidal action of serum (21,41), polyclonal B cell aativation, and macrophage cytotoxicity (43). The low level of LPS on P. aeruginosa that contains a long 0 polymer, however, may be sufficient to form a uniform cover over the cell, since the surface is inaccessible to rough-core-specific monoclonal antibodies (52).…”

Section: Discussionmentioning

confidence: 99%

Heterogeneity of lipopolysaccharides from Pseudomonas aeruginosa: analysis of lipopolysaccharide chain length

et al. 1988

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Lipopolysaccharide (LPS) from smooth strains of Pseudomonas aeruginosa 503, PAZ1, PA01715, PA01716, and Z61 was fractionated by gel filtration chromatography. LPS samples from the first four strains, all PAO1 derivatives, separated into three major size populations, whereas LPS from strain Z61, a Pac K799/WT mutant strain, separated into two size populations. When column fractions were applied to sodium dodecyl sulfate-polyacrylamide gels in their order of elution, molecules of decreasing size were resolved, and the ladder of molecules with different-length 0 antigens formed a diagonal across the gel. The LPS from the PAO1 derivatives contained two distinct sets of bands, distinguished on the gels as two sets of diagonals. The set of bands with the faster mobility, the B bands, was found in column fractions comprising the three major amino sugar-containing peaks. In the sample from strain 503, a fourth minor peak which contained B bands was resolved. The slower-moving set of bands, the A bands, were recovered in a minor peak. LPS from strain Z61 contained only one set of bands, with the higher-molecular-weight molecules eluting from the column in a volume similar to that of the B bands of the PAO1 strains. Analysis of the fractions of LPS from all strains indicated that less than 8% of the LPS molecules had a long, attached 0 antigen. Analysis of the peak that contained mainly A bands indicated a lack of reactive amino sugar and phosphate, although heptose and 2-keto-3-deoxyoctulosonic acid were detected. Reaction of isolated fractions with monoclonal antibody specific for the PA01 0-antigen side chain indicated that only the B bands from the PAO1 strains were antigenically reactive. The bands from strain Z61 showed no reactivity. The data suggest that the A and B bands from the PAO1 strains are antigenically distinct. We propose that PAO1 strains synthesize two types of molecules that are antigenically different.Lipopolysaccharide (LPS), a major component of the outer membranes of gram-negative bacteria, is important in the structure (33, 37) and function (33,36) of this membrane. Structural microheterogeneity in several regions of LPS molecules from members of the family Enterobacteriaceae (2,14,22,37,38,48,51) and Pseudomonas aeruginosa strains (33, 57) has been demonstrated. Of the several methods used to separate the subclasses of LPS from individual strains, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) (20,24,45,48) and gel filtration (9, 26, 30, 32, 34, 48) are the best. Either of these two methods by themselves, however, may be insufficient to completely characterize the high-and low-molecular-weight fractions of LPS. Peterson and McGroarty (48) demonstrated that the SDS-PAGE of the column fractions of samples from Salmonella typhimurium, Salmonella minnesota, and Escherichia coli was instrumental in characterizing the various-sized fractions. Analysis of the isolated fractions allowed for the estimation of the average number of 0-antigen repeat units per LPS from each of the si...

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“…Because the preparations used in Sidberry and Sadoffs studies were equivalent to our crude lysates, some of the inhibition by R2 and R3 pyocines that they observed with a few gonococcal strains may have been due to the presence of material other than the R-type pyocines. The receptor site for the R-type pyocines is in the lipopolysaccharide (LPS) (LPS) of Pseudomonas (Ikeda and Egami, 1973;Govan, 1974a;Koval and Meadow, 1977) and a similar location has been suggested for Neisseria (Sidberry and Sadoff, 1977). Table VIII is based on Kageyama's (1975) proposed pyocine receptor sites for his groups R1-R5 in the LPS of Pseudomonas.…”

Section: Discussionmentioning

confidence: 80%