scholarly journals Priming Activity for Chemiluminescence Reaction of PMN in the Culture Supernatant of Streptococcal Preparation (OK-432)-Stimulated Spleen Cells

1988 ◽  
Vol 32 (6) ◽  
pp. 621-633 ◽  
Author(s):  
Yoko Fukase ◽  
Shigeru Fukase ◽  
Fujiro Sendo
1999 ◽  
Vol 65 (3) ◽  
pp. 1071-1077 ◽  
Author(s):  
Dominique Granato ◽  
Fabienne Perotti ◽  
Isabelle Masserey ◽  
Martine Rouvet ◽  
Mireille Golliard ◽  
...  

ABSTRACT The influence of pH on the adhesion of twoLactobacillus strains to Caco-2 human intestinal cells was investigated. One strain, Lactobacillus johnsonii La1, was adherent at any pH between 4 and 7. The other one, L. acidophilus La10, did not attach to this cell line under the same experimental conditions. On the basis of these results, we used the monoclonal antibody technique as a tool to determine differences on the surface of these bacteria and to identify a factor for adhesion. Mice were immunized with live La1, and the hybridomas produced by fusion of spleen cells with ONS1 cells were screened for the production of antibodies specific for L. johnsonii La1. A set of these monoclonal antibodies was directed against a nonproteinaceous component of the L. johnsonii La1 surface. It was identified as lipoteichoic acid (LTA). This molecule was isolated, chemically characterized, and tested in adhesion experiments in the same system. The adhesion of L. johnsonii La1 to Caco-2 cells was inhibited in a concentration-dependent way by purified LTA as well as by L. johnsonii La1 culture supernatant that contained LTA. These results showed that the mechanism of adhesion of L. johnsonii La1 to human Caco-2 cells involves LTA.


1989 ◽  
Vol 21 (2) ◽  
pp. 127-130 ◽  
Author(s):  
Hiroyasu Fukui ◽  
Yasuo Koishihara ◽  
Masahiro Nagamuta ◽  
Yohichi Mizutani ◽  
Atsushi Uchida

Author(s):  
Xiaorong Zhu ◽  
Richard McVeigh ◽  
Bijan K. Ghosh

A mutant of Bacillus licheniformis 749/C, NM 105 exhibits some notable properties, e.g., arrest of alkaline phosphatase secretion and overexpression and hypersecretion of RS protein. Although RS is known to be widely distributed in many microbes, it is rarely found, with a few exceptions, in laboratory cultures of microorganisms. RS protein is a structural protein and has the unusual properties to form aggregate. This characteristic may have been responsible for the self assembly of RS into regular tetragonal structures. Another uncommon characteristic of RS is that enhanced synthesis and secretion which occurs when the cells cease to grow. Assembled RS protein with a tetragonal structure is not seen inside cells at any stage of cell growth including cells in the stationary phase of growth. Gel electrophoresis of the culture supernatant shows a very large amount of RS protein in the stationary culture of the B. licheniformis. It seems, Therefore, that the RS protein is cotranslationally secreted and self assembled on the envelope surface.


Pneumologie ◽  
2016 ◽  
Vol 70 (07) ◽  
Author(s):  
G Jatzlauk ◽  
S Bartel ◽  
S Reuter ◽  
S Krauss-Etschmann
Keyword(s):  

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