scholarly journals Lipid A Structure and Immunoinhibitory Effect of the Marine Bacterium Cobetia pacifica KMM 3879T

2018 ◽  
Vol 2018 (20-21) ◽  
pp. 2707-2716 ◽  
Author(s):  
Flaviana Di Lorenzo ◽  
Angelo Palmigiano ◽  
Sami Albitar-Nehme ◽  
Mateusz Pallach ◽  
Maxim Kokoulin ◽  
...  
Keyword(s):  
Marine Bacterium ◽  
Lipid A ◽  
Lipid A Structure

Mass spectrometry analysis of intact Francisella bacteria identifies lipid A structure remodeling in response to acidic pH stress

Biochimie ◽  
2017 ◽  
Vol 141 ◽  
pp. 16-20 ◽  
Author(s):  
Camille B. Robert ◽  
Michael Thomson ◽  
Alain Vercellone ◽  
Francesca Gardner ◽  
Robert K. Ernst ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Lipid A ◽  
Mass Spectrometry Analysis ◽  
Acidic Ph ◽  
Spectrometry Analysis ◽  
Ph Stress ◽  
Lipid A Structure

Lipopolysaccharide and proteins of the cell envelope of Vibrio marinus, a marine bacterium

1973 ◽  
Vol 19 (10) ◽  
pp. 1211-1217 ◽  
Author(s):  
Carl F. Deneke ◽  
R. R. Colwell
Keyword(s):  
Fatty Acids ◽  
Gel Electrophoresis ◽  
Marine Bacterium ◽  
Lipid A ◽  
Cell Envelope ◽  
Polyacrylamide Gel Electrophoresis ◽  
Amino Sugar ◽  
High Ratio ◽  
Side Chain ◽  
Total Fatty Acids

Lipopolysaccharides isolated from the marine bacterium Vibrio marinus strain PS-207 were found to be similar to the lipopolysaccharides of R mutants of enteric organisms, with respect to extraction characteristics, percentage of lipid A (61%), and sugars of the polysaccharide side chain (glucose and heptose). A high ratio (2:1) of phosphate to amino sugar was found in the lipid A. Hydroxy fatty acids constituted only 14% of the total fatty acids of the lipid A fraction, whereas branched and straight-chain fatty acids were present in greater abundance. The major envelope proteins of V. marinus strain PS-207 fell into three molecular weight classes determined by SDS gel electrophoresis. Numerous protein species were observed in urea – acetic polyacrylamide gel electrophoresis preparations.

scholarly journals Characterization of htrB and msbB Mutants of the Light Organ Symbiont Vibrio fischeri

2007 ◽  
Vol 74 (3) ◽  
pp. 633-644 ◽  
Author(s):  
Dawn M. Adin ◽  
Nancy J. Phillips ◽  
Bradford W. Gibson ◽  
Michael A. Apicella ◽  
Edward G. Ruby ◽  
...  
Keyword(s):  
Lipid A ◽  
Vibrio Fischeri ◽  
Sodium Dodecyl ◽  
Chromosome 1 ◽  
Chromosome 2 ◽  
Euprymna Scolopes ◽  
Host Interactions ◽  
Lipid A Structure ◽  
Bacterial Lipid

ABSTRACT Bacterial lipid A is an important mediator of bacterium-host interactions, and secondary acylations added by HtrB and MsbB can be critical for colonization and virulence in pathogenic infections. In contrast, Vibrio fischeri lipid A stimulates normal developmental processes in this bacterium's mutualistic host, Euprymna scolopes, although the importance of lipid A structure in this symbiosis is unknown. To further examine V. fischeri lipid A and its symbiotic function, we identified two paralogs of htrB (designated htrB1 and htrB2) and an msbB gene in V. fischeri ES114 and demonstrated that these genes encode lipid A secondary acyltransferases. htrB2 and msbB are found on the Vibrio “housekeeping” chromosome 1 and are conserved in other Vibrio species. Mutations in htrB2 and msbB did not impair symbiotic colonization but resulted in phenotypic alterations in culture, including reduced motility and increased luminescence. These mutations also affected sensitivity to sodium dodecyl sulfate, kanamycin, and polymyxin, consistent with changes in membrane permeability. Conversely, htrB1 is located on the smaller, more variable vibrio chromosome 2, and an htrB1 mutant was wild-type-like in culture but appeared attenuated in initiating the symbiosis and was outcompeted 2.7-fold during colonization when mixed with the parent. These data suggest that htrB2 and msbB play conserved general roles in vibrio biology, whereas htrB1 plays a more symbiosis-specific role in V. fischeri.

scholarly journals Hemin-Dependent Modulation of the Lipid A Structure of Porphyromonas gingivalis Lipopolysaccharide

2006 ◽  
Vol 74 (8) ◽  
pp. 4474-4485 ◽  
Author(s):  
Montaser N. Al-Qutub ◽  
Pamela H. Braham ◽  
Lisa M. Karimi-Naser ◽  
Xinyan Liu ◽  
Caroline A. Genco ◽  
...  
Keyword(s):  
Porphyromonas Gingivalis ◽  
Host Response ◽  
Lipid A ◽  
Iron Acquisition ◽  
Extraction Procedure ◽  
Structural Heterogeneity ◽  
Related Factors ◽  
Adult Type ◽  
Structural Content ◽  
Lipid A Structure

ABSTRACT Porphyromonas gingivalis is a periopathogen strongly associated with the development of adult-type periodontitis. Both the virulence characteristics of periopathogens and host-related factors are believed to contribute to periodontitis. P. gingivalis lipopolysaccharide (LPS) displays a significant amount of lipid A structural heterogeneity, containing both penta- and tetra-acylated lipid A structures. However, little is known concerning how the lipid A structural content of P. gingivalis is regulated. Alterations in the lipid A content may facilitate the ability of P. gingivalis to modulate the innate host response to this bacterium. In this report, it is shown that the concentration of hemin in the growth medium significantly modulates the lipopolysaccharide lipid A structural content of P. gingivalis. Hemin is a key microenvironmental component of gingival cervicular fluid which is believed to vary depending upon the state of vascular ulceration. At low hemin concentrations, one major penta-acylated lipid A structure was found, whereas at high concentrations of hemin, multiple tetra- and penta-acylated lipid A structures were observed. Hemin concentrations, not iron acquisition, were responsible for the alterations in the lipid A structural content. The modifications of the lipid A structural content were independent of the LPS extraction procedure and occurred in a variety of laboratory strains as well as a freshly obtained clinical isolate. The known hemin binding proteins Kgp and HmuR contributed to the lipid A modulation sensing mechanism. To the best of our knowledge, this is the first report that hemin, a clinically relevant microenvironmental component for P. gingivalis, can modulate the lipid A structure found in a bacterium. Since tetra- and penta-acylated P. gingivalis lipid A structures have opposing effects on Toll-like receptor 4 activation, the alteration of the lipid A structural content may have significant effects on the host response to this bacterium.

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