Transmembrane topology of the two FhuB domains representing the hydrophobic components of bacterial ABC transporters involved in the uptake of siderophores, haem and vitamin B

Article Abstract:

Ferric hydroxamate transport throughout the Escherichia coli outer membrane is energy dependent. A topology model of the involvement of an integral cytoplasmic membrane protein in bacterial iron uptake is presented. The amino acid sequences of the equivalent siderophore-transport related PBT proteins from both Gram-positive and negative bacterial, showed a distinct polypeptide class which may have similar transmembrane organization. The model protein FhuB differs significantly in some areas from topology models of most other PBT-related hydrophobic proteins.

Escherichia coli, Membrane proteins

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Phenotypic variation in Actinobacillus actinomycetemcomitans during laboratory growth: implications for virulence

Article Abstract:

A study was conducted to analyze the alteration of specific virulence traits related to phenotypic changes seen when a low-passage disease-associated and well maintained parent strain of Actinobacillus actinomycetemcomitans was compared against a laboratory-growth spontaneous variant/mutant. Results indicated that clinical isolates of A actinomycetemomitans undergo virulence-reducing phenotypic alterations during in vitro passage.

Phenotype, Phenotypes, Virulence (Microbiology)

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