Sequence and structural relationships of leucocins A-, B- and C-TA33a from Leuconostoc mesenteroides TA33a

Article Abstract:

Strain TA33a of Leuconostoc mesenteroides contains three leucocins designated as Leucocin A-TA33a, B-TA33a and C-TA33a. Leucocin B-TA33a has 31 amino acid residues and is homologous to mesenterocin 52B. Leucocin C-TA33a contains 36 amino acid residues and belongs to the class II bacteriocin superfamily. Leucocin A-TA33a is the same as leucocin A-UAL 187. These leucocins exhibit structural transitions adopting a beta structure when placed in an environment that mimics biological membranes based on circular dichroism spectra and gel electrophoresis.

Bacterial toxins

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Attacin - an insect immune protein - binds LPS and triggers the specific inhibition of bacterial outer-membrane protein synthesis

Article Abstract:

Experiments were performed showing that lipopolysaccharide (LPS) on the cell surface acts as the receptor for attacin, a 20 kDa antibacterial protein from the immune haemolymph of Hyalophora cecropia. Results also showed that attacin does not produce any inhibitory effect on cell growth when reacted with purified LPS. Moreover, it was also observed that attacin need not enter the inner membrane of the cytoplasm to interfere with the synthesis of the outer membrane protein of the cell.

Endotoxins, Cell membranes, Plasma membranes, Immune response

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Enterobacterial lipocalins precede Vibrio homologue

Article Abstract:

Lipocalins belong to a family of proteins formerly identified only with eukaryotic organisms. Recent studies have identified a number of lipocalins among bacteria. These lipocalins have been found to be closely homologous to either apolipoprotein D or Lazarillo. The claims of Barker and Manning as to having discovered the first bacterial lipocalin in Vibrio is erroneous as a lipocalin had been identified in Escherichia coli two years prior to their report.

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