Isolation and characterization of a Clostridium sp. with cinnamoyl esterase activity and unusual cell envelope ultrastructure

1999 ◽  
Vol 172 (3) ◽  
pp. 139-149 ◽  
Author(s):  
C. S. McSweeney ◽  
Amanda Dulieu ◽  
Richard I. Webb ◽  
Therese Del Dot ◽  
Linda L. Blackall
1994 ◽  
Vol 29 (1) ◽  
pp. 70-78 ◽  
Author(s):  
S. Kokeguchi ◽  
M. Miyamoto ◽  
K. Kato ◽  
I. Tanimoto ◽  
H. Kurihara ◽  
...  

2012 ◽  
Vol 393 (8) ◽  
pp. 749-755
Author(s):  
Kathleen Fischer ◽  
Evgueny Vinogradov ◽  
Buko Lindner ◽  
Holger Heine ◽  
Otto Holst

Abstract The Gram-positive bacterium Lactococcus lactis G121 is a farm isolate that protects mice from ovalbumin-induced asthma. To understand the molecular mechanisms of such allergy-protective properties, the isolation and characterization of cell envelope constituents is crucial. Here, structural analyses of the extracellular teichoic acid (EC TA) from L. lactis G121 are presented. Extraction with 0.9% saline afforded a crude TA fraction. Consecutive size exclusion chromatography on Biogel P60 and P10 matrix was performed to purify the sample. Chemical component analyses, high-resolution electrospray ionization Fourier-transformed ion cyclotron mass spectrometry, and nuclear magnetic resonance spectroscopy were conducted for structural elucidation. The EC TA was a poly(glycosylglycerol phosphate) molecule with a repeating unit of -6)-[β-d-Glcp-(1→3)-][α-d-GlcpNAc-(1→4)-]α-d-GalpNAc-(1→3)-β-d-GlcpNAc-(1→2)-glycerol-(1-P-).


1983 ◽  
Vol 29 (9) ◽  
pp. 1159-1170 ◽  
Author(s):  
R. D. Bryant ◽  
K. M. McGroarty ◽  
J. W. Costerton ◽  
E. J. Laishley

An acidophilic, rod-shaped, sulfur-oxidizing bacterium was isolated from extremely acidic soil adjacent to a sulfur stockpile at Fox Creek, Alta. This isolate was found to grow only autotrophically by oxidizing S° and reduced inorganic sulfur compounds (S2O32− and S4O62−), placing it in the genus Thiobacillus. Aerobic growth was observed over a pH range of 2.0 to 4.5 with optimum growth at 3.5 to 4.0. Analysis of its DNA revealed a mol% G + C content of 61.5. Ultrastructural studies showed that the isolate possessed a tuft of polar flagella. A glycocalyx was observed only after the antiserum stabilization procedure, which showed it extending outwards from the outer membrane of the bacterial cell envelope. Cleavage planes of this cell showed a typical Gram-negative cell wall. The cytoplasm contained two types of inclusion bodies, carboxysomes and a single large membrane-bound sulfur granule. This isolate had morphological and physiological characteristics which were not totally comparable with other known acidiophilic thiobacilli demonstrating this bacterium to be a new Thiobacillus sp. named T.albertis.


2005 ◽  
Vol 187 (6) ◽  
pp. 1892-1900 ◽  
Author(s):  
Anthony R. Flores ◽  
Linda M. Parsons ◽  
Martin S. Pavelka

ABSTRACT Our laboratory previously constructed mutants of Mycobacterium tuberculosis and Mycobacterium smegmatis with deletions in the genes for their major β-lactamases, BlaC and BlaS, respectively, and showed that the mutants have increased susceptibilities to most β-lactam antibiotics, particularly the penicillins. However, there is still a basal level of resistance in the mutants to certain penicillins, and the susceptibilities of the mutants to some cephalosporin-based β-lactams are essentially the same as those of the wild types. We hypothesized that characterizing additional mutants (derived from β-lactamase deletion mutants) that are hypersusceptible to β-lactam antibiotics might reveal novel genes involved with other mechanisms of β-lactam resistance, peptidoglycan assembly, and cell envelope physiology. We report here the isolation and characterization of nine β-lactam antibiotic-hypersusceptible transposon mutants, two of which have insertions in genes known to be involved with peptidoglycan biosynthesis (ponA2 and dapB); the other seven mutants have insertions which affect novel genes. These genes can be classified into three groups: those involved with peptidoglycan biosynthesis, cell division, and other cell envelope processes. Two of the peptidoglycan-biosynthetic genes (ponA2 and pbpX) may encode β-lactam antibiotic-resistant enzymes proposed to be involved with the synthesis of the unusual diaminopimelyl linkages within the mycobacterial peptidoglycan.


2000 ◽  
Vol 31 (2) ◽  
pp. 149-149 ◽  
Author(s):  
T Tozaki ◽  
H Kakoi ◽  
S Mashima ◽  
K Hirota ◽  
T Hasegawa ◽  
...  

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