The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Relationship between antibacterial activity and porin binding of lactoferrin in Escherichia coli and Salmonella typhimurium.

The effect of lactoferrin ( Lf) on bacterial growth was tested by measuring conductance changes in the cultivation media by using a Malthus-AT system and was compared with the magnitude of 125I-labeled Lf binding in 15 clinical isolates of Escherichia coli. The binding property was inversely related to the change in bacterial metabolic rate (r = 0.91) and was directly related to the degree of bacteriostasis (r = 0.79). The magnitude of Lf-bacterium interaction showed no correlation with the MIC of Lf. In certain strains, Lf at supraoptimal levels reduced the bacteriostatic effect. Thus, the Lf concentration in the growth media was critical for the antibacterial effect. The cell envelopes of Salmonella typhimurium 395MS with smooth lipopolysaccharide (LPS) and its five isogenic rough mutants revealed 38-kDa porin proteins as peroxidase-labeled- Lf-reactive components in sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blot (ligand blot) analysis. However, in the whole cell binding assay, parent strain 395MS demonstrated a very low interaction with 125I- Lf. On the other hand, Lf interaction gradually increased in correspondence with the decrease in LPS polysaccharide moiety in the isogenic rough mutants. Conductance measurement studies revealed that the low-level- Lf-binding (low- Lf-binding) strain 395MS with smooth LPS was relatively insusceptible to Lf, while the high- Lf-binding mutant Rd was more susceptible to Lf. These data suggested a correlation between Lf binding to porins and the Lf-mediated antimicrobial effect. The polysaccharide moiety of LPS shielded porins from the Lf interaction and concomitantly decreased the antibacterial effect.[1]


  1. Relationship between antibacterial activity and porin binding of lactoferrin in Escherichia coli and Salmonella typhimurium. Naidu, S.S., Svensson, U., Kishore, A.R., Naidu, A.S. Antimicrob. Agents Chemother. (1993) [Pubmed]
WikiGenes - Universities