Stress proteins in Listeria monocytogenes.

The proteins induced by the different stress conditions in Listeria monocytogenes were analyzed by two-dimensional (2-D) electrophoresis with the aid of a computerized 2-D gel analysis system. The stress conditions imposed were pH 4, pH 10, 0.015% sodium, dodecyl sulfate (SDS), 0.

A chemically defined minimal medium for the optimal culture of Listeria.

Unlike most other bacteria, many Listeria strains do not grow well in the minimal media described so far in the literature. Among the minimal media tested, a chemically defined medium modified from that of Premaratne and co-workers was found to support the best growth of Listeria spp. The promoting effect was due to the incorporation of several indispensable vitamins and growth factors.

Analysis by two-dimensional electrophoresis of proteins secreted by sheep ovarian follicles: effects of the FecB gene, follicle size and atresia.

Proteins secreted by sheep ovarian follicles at different stages of maturation (small healthy, large healthy or large atretic) and originating from ewes with different ovulation rates (homozygous carriers or noncarriers of the FecB gene) were analysed by two-dimensional electrophoresis (PAGE) followed by computerized image analysis. Follicles were incubated intact for 1 h to assess steroidogenesis, and then incubated for 24 h in the presence of [35S]methionine. Secreted proteins were then resolved by iso-electric focusing followed by migration on 10% acrylamide slab gels and fluorography.

Analysis of heat and cold shock proteins in Listeria by two-dimensional electrophoresis.

The proteins induced by heat and cold shock in Listeria monocytogenes (pathogenic for humans) and L. innocua (nonpathogenic) strains were analyzed by two-dimensional (2-D) electrophoresis with the help of a computerized 2-D gel analysis system. Heat (49 degrees C) and cold (4 degrees C) shock repressed roughly half the number of proteins synthesized at normal temperature (25 degrees C) and decreased the level of numerous other proteins.

Identification and classification of Listeria by two-dimensional protein mapping.

The cellular proteins of 29 Listeria strains belonging to different species and serotypes were analysed by two-dimensional (2-D) electrophoresis with the help of a computerized 2-D gel analysis system. The protein patterns were similar among strains within a Listeria species, but were different from one species to another. The comparative analysis of these protein maps enabled us to find specific proteins and to determine the genetic relatedness among Listeria spp.