scholarly journals Bacterial Cell Wall-Induced Arthritis: Chemical Composition and Tissue Distribution of Four Lactobacillus Strains

2000 ◽  
Vol 68 (6) ◽  
pp. 3535-3540 ◽  
Author(s):  
Egle Šimelyte ◽  
Marja Rimpiläinen ◽  
Leena Lehtonen ◽  
Xiang Zhang ◽  
Paavo Toivanen

ABSTRACT To study what determines the arthritogenicity of bacterial cell walls, cell wall-induced arthritis in the rat was applied, using four strains of Lactobacillus. Three of the strains used proved to induce chronic arthritis in the rat; all were Lactobacillus casei. The cell wall of Lactobacillus fermentum did not induce chronic arthritis. All arthritogenic bacterial cell walls had the same peptidoglycan structure, whereas that of L. fermentum was different. Likewise, all arthritogenic cell walls were resistant to lysozyme degradation, whereas the L. fermentum cell wall was lysozyme sensitive. Muramic acid was observed in the liver, spleen, and lymph nodes in considerably larger amounts after injection of an arthritogenicL. casei cell wall than following injection of a nonarthritogenic L. fermentum cell wall. The L. casei cell wall also persisted in the tissues longer than theL. fermentum cell wall. The present results, taken together with those published previously, underline the possibility that the chemical structure of peptidoglycan is important in determining the arthritogenicity of the bacterial cell wall.

1967 ◽  
Vol 167 (1009) ◽  
pp. 446-447 ◽  

Although we have heard a lot about the mode of binding of low molecular weight, soluble, lysozyme substrates, we have heard little about the mode of action of lysozyme on its natural insoluble substrate, the bacterial cell wall; so I want to bring a biological flavour into this discussion. Lysozyme was the name given by Fleming (1922) to the powerful bacteriolytic agent found in various cells and secretions; it was particularly active against a new bacterial species which he named Micrococcus lysodeikticus . The walls of this species still provide us with one of the best substrates for the study of lysozyme action. Salton showed that there is a considerable spectrum of activity of lysozyme in solubilizing walls of other species of bacteria. For example, walls of M. lysodeikticus are attacked rapidly by a concentration of enzyme of 1 μg/ml., Bacillus megaterium walls need 50 μg/ml., while walls of B. cereus are hardly changed visibly by 50 μg/ml. Consideration of the structure of the basal mucopeptide unit of bacterial cell walls, illustrated by Dr Perkins, shows that there are many ways in which structural differences could be introduced. Knowledge of the effects of some of these differences on lysozyme sensitivity may help in elucidating the mode of action of lysozyme on the complete bacterial cell wall.


1969 ◽  
Vol 47 (1) ◽  
pp. 71-74 ◽  
Author(s):  
Carolyn L. Marshall ◽  
A. J. Wicken ◽  
A. D. Brown

The outer layer of the cell envelope of Halobacterium halobium was isolated after suspending the envelope in either 1 M NaCl or 0.02 M MgCl2. Chemical analysis of the isolated, solubilized outer layer showed it to consist of protein or glycoprotein with about 3% RNA. No free or bound lipid was detected. No cytochromes were present in the outer layer. Components commonly associated with bacterial cell walls were absent.Chemical composition together with the marked instability of the outer layer in a slight ion deficit are not consistent with a function of this layer as a "cell wall" of the organism.


1997 ◽  
Vol 5 (8) ◽  
pp. 8-9
Author(s):  
Lee van Hook

A scanning acoustic microscope (SAM) - a nanomicrophone using a piezoelectric crystal, may be used to examine bacterial colonies, not just materials specimens to detect phonons and listen to propagating microfractures.Since bacterial cell walls are rigid structures, they undergo mechanical distortions when channels open and dose. This causes them to squeak and pop, each channel having its own sound. Channels and receptor molecules are all of different sizes and shapes, and therefore deform the cell wall in unique ways. This means that each channel makes a unique (if faint) sound when it passes a molecule through itself and this activity can be delected, Transport rates of uptake and excretion for the various compounds car then be calculated trom the intensity of the sounds.


1985 ◽  
Vol 5 (4) ◽  
pp. 163-167 ◽  
Author(s):  
T. J. A. Lehman ◽  
J. B. Allen ◽  
P. H. Plotz ◽  
R. L. Wilder

1967 ◽  
Vol 167 (1009) ◽  
pp. 443-445 ◽  

The elegant work that has been presented this afternoon has been concerned with the structure of lysozyme in relation to its action on model substrates of small molecular weight, or its inhibition by equally small molecules. The ‘natural’ substrate is presumably the mucopeptide of bacterial cell wall, which is a large, highly complex and insoluble molecule. A portion of a possible structure of a mucopeptide (Tipper & Strominger 1965) in this case from Staphylococcus aureus , is given in figure 51. Evidently in order to facilitate hydrolysis of the glycosidic links on C-1 of muramic acid (and, in the absence of O-acetyl groups, the enzyme is very good at this) lysozyme molecules must be able to approach closely to the relevant part of the polysaccharide backbone. One of the factors that appears to influence this approach of enzyme and substrate is the presence of positive charges on the mucopeptide. Isolated cell walls of Corynebacterium tritici were completely resistant to lysozyme, but could be made sensitive by the action of formamide at 150 °C for 15 min (Perkins 1965). It was found that this procedure did not remove more than 10% of the non-mucopeptide carbohydrate present, but it did formylate the free amino groups of diaminobutyric acid that occurred in the untreated wall. Acetylation by a mild procedure, followed by treatment with alkali to remove any O-acetyl groups, also caused the walls to become susceptible to dissolution by lysozyme.


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