[Detection of Salmonella Choleraesuis var. Kunzendorf in a fattening pig with septicaemic salmonellosis. A case report].

The present case reports the detection of Salmonella (S.) Choleraesuis var. Kunzendorf and porcine circovirus type 2 in an organic fattening pig suffering from septicaemic salmonellosis and porcine dermatitis and nephropathy syndrome.

Cytokinesis mediated through the recruitment of cortexillins into the cleavage furrow.

The fact that substrate-anchored Dictyostelium cells undergo cytokinesis in the absence of myosin II underscores the importance of other proteins in enabling the cleavage furrow to constrict. Cortexillins, a pair of actin-bundling proteins, are required for normal cleavage. They are targeted to the incipient furrow in wild-type and, more prominently, in myosin II-null cells.

Three-dimensional patterns and redistribution of myosin II and actin in mitotic Dictyostelium cells.

Myosin II is not essential for cytokinesis in cells of Dictyostelium discoideum that are anchored on a substrate (Neujahr, R., C. Heizer, and G.

Microfilament dynamics during cell movement and chemotaxis monitored using a GFP-actin fusion protein.

Background: The microfilament system in the cortex of highly motile cells, such as neutrophils and cells of the eukaryotic microorganism Dictyostelium discoideum, is subject to rapid re-organization, both spontaneously and in response to external signals. In particular, actin polymerization induced by a gradient of chemoattractant leads to local accumulation of filamentous actin and protrusion of a 'leading edge' of the cell in the direction of the gradient. In order to study the dynamics of actin in these processes, actin was tagged at its amino terminus with green fluorescent protein (GFP) and observed with fluorescence microscopy in living cells of D.

Myosin II-independent processes in mitotic cells of Dictyostelium discoideum: redistribution of the nuclei, re-arrangement of the actin system and formation of the cleavage furrow.

Mitosis was studied in multinucleated and mononucleated mutant cells of Dictyostelium discoideum that lack myosin II (Manstein et al. (1989) EMBO J. 8, 923-932).

Chemoattractant-controlled accumulation of coronin at the leading edge of Dictyostelium cells monitored using a green fluorescent protein-coronin fusion protein.

Background: The highly motile cells of Dictyostelium discoideum rapidly remodel their actin filament system when they change their direction of locomotion either spontaneously or in response to chemoattractant. Coronin is a cytoplasmic actin-associated protein that accumulates at the coritcal sites of moving cells and contributes to the dynamics of the actin system. It is a member of the WD-repeat family of proteins and is known to interact with actin-myosin complexes.

A talin homologue of Dictyostelium rapidly assembles at the leading edge of cells in response to chemoattractant.

In an attempt to identify unknown actin-binding proteins in cells of Dictyostelium discoideum that may be involved in the control of cell motility and chemotaxis, monoclonal antibodies were raised against proteins that had been enriched on an F-actin affinity matrix. One antibody recognized a protein distinguished by its strong accumulation at the tips of filopods. These cell-surface extensions containing a core of bundled actin filaments are rapidly protruded and retracted by cells in the growth-phase stage.

Actin-associated proteins in motility and chemotaxis of Dictyostelium cells.

The amoeboid cells of Dictyostelium discoideum are amenable to a combined biochemical, genetic, and cell biological approach that can be focussed to the study of molecular interactions underlying the chemotactic responses of eukaryotic cells. In these responses the actin-based motility system is involved. This system is characterised in Dictyostelium cells by a large number and variety of regulatory proteins.