A functional water channel protein in the pathogenic bacterium Brucella abortus

Article Abstract:

Research has been conducted on bacterial aquaporins which belong to the major intrinsic protein superfamily of membrane proteins. The authors describe the cloning of aquaporin gene from Brucella abortus and its characterization, and report that the functional studies of this gene may help to determine the role of aquaporin proteins in bacterial physiology.

Science & research, Spain, Analysis, Microbiology, Cloning, Water chemistry, Bacterial proteins, Brucella

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Functional characterization of a microbial aquaglyceroporin

Article Abstract:

A microbial aquaglyceroporin from Lactococcus lactis has been functionally characterized. Aquaglyceroporins are one class of major intrinsic proteins (MIPs), which make up a widespread membrane channel family required for osmotic cell equilibrium. Bacterial MIP genes are in archaea and in eubacteria, both Gram-positive and Gram-negative. The MIP is permeable to glycerol and to water.

Eukaryotic cells, Cells (Biology), Eukaryotes, Escherichia coli, Bacteria, Water, Cellular control mechanisms, Cell regulation, Archaeabacteria, Glycerol, Archaea, Lactococcus

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Insertion of fluorescent fatty acid probes into the outer membranes of the pathogenic spirochaetes Treponema pallidum and Borrelia burgdorferi

Article Abstract:

The outer membranes (OMs) of the pathogenic spirochaetes Borrelia burgdorferi and Treponema pallidum have been studied using insertion of fluorescent fatty acid (FA) probes. Support was found for the prediction that lack of lipopolysaccharide makes T. pallidum and B. burgdorferi OMs decidedly more permeable to lipophilic compounds than their Gram-negative bacterial counterparts. It seems the two spirochaetes may obtain long-chain FAs, nutrients they cannot synthesize, through direct OM permeation.

United States, Usage, Lyme disease, Gram-negative bacteria, Flow cytometry, Syphilis, Treponematoses, Molecular probes, Fatty acid metabolism

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