Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 6 de 6
Filter
Add more filters










Database
Language
Publication year range
1.
Anim Health Res Rev ; 23(2): 165-193, 2022 12.
Article in English | MEDLINE | ID: mdl-36688278

ABSTRACT

Dietary fiber (DF) is receiving increasing attention, and its importance in pig nutrition is now acknowledged. Although DF for pigs was frowned upon for a long time because of reductions in energy intake and digestibility of other nutrients, it has become clear that feeding DF to pigs can affect their well-being and health. This review aims to summarize the state of knowledge of studies on DF in pigs, with an emphasis on the underlying mode of action, by considering research using DF in sows as well as suckling and weaned piglets, and fattening pigs. These studies indicate that DF can benefit the digestive tracts and the health of pigs, if certain conditions or restrictions are considered, such as concentration in the feed and fermentability. Besides the chemical composition and the impact on energy and nutrient digestibility, it is also necessary to evaluate the possible physical and physiologic effects on intestinal function and intestinal microbiota, to better understand the relation of DF to animal health and welfare. Future research should be designed to provide a better mechanistic understanding of the physiologic effects of DF in pigs.


Subject(s)
Dietary Fiber , Gastrointestinal Microbiome , Swine , Animals , Female , Dietary Fiber/analysis , Gastrointestinal Microbiome/physiology , Animal Feed/analysis , Diet/veterinary
2.
Open Vet J ; 6(3): 242-246, 2016.
Article in English | MEDLINE | ID: mdl-28116248

ABSTRACT

Staphylococcus sciuri is known as an opportunistic pathogen colonizing domesticated animals and has also been associated with wound infections in humans. Particularly over the last decade, oxacillin (methicillin) resistant strains had been emerged, which now increase the medical relevance of this species. This report describes the identification of an oxacillin-resistant S. sciuri isolate from a wound infection of a horse. We determined the absence of coagulase and hyaluronidase activity and analysed the antibiotic resistance profile.

3.
Thromb Haemost ; 111(3): 401-16, 2014 Mar 03.
Article in English | MEDLINE | ID: mdl-24196407

ABSTRACT

Streptococcus pneumoniae is not only a commensal of the nasopharyngeal epithelium, but may also cause life-threatening diseases. Immune-electron microscopy studies revealed that the bacterial glycolytic enzyme, phosphoglycerate kinase (PGK), is localised on the pneumococcal surface of both capsulated and non-capsulated strains and colocalises with plasminogen. Since pneumococci may concentrate host plasminogen (PLG) together with its activators on the bacterial cell surface to facilitate the formation of plasmin, the involvement of PGK in this process was studied. Specific binding of human or murine PLG to strain-independent PGK was documented, and surface plasmon resonance analyses indicated a high affinity interaction with the kringle domains 1-4 of PLG. Crystal structure determination of pneumococcal PGK together with peptide array analysis revealed localisation of PLG-binding site in the N-terminal region and provided structural motifs for the interaction with PLG. Based on structural analysis data, a potential interaction of PGK with tissue plasminogen activator (tPA) was proposed and experimentally confirmed by binding studies, plasmin activity assays and thrombus degradation analyses.


Subject(s)
Bacterial Proteins/metabolism , Phosphoglycerate Kinase/metabolism , Plasminogen/metabolism , Streptococcus pneumoniae/physiology , Tissue Plasminogen Activator/metabolism , Animals , Bacterial Proteins/genetics , Cloning, Molecular , Crystallography, X-Ray , Fibrinolysin/metabolism , Humans , Laryngeal Mucosa/microbiology , Mice , Nasal Mucosa/microbiology , Phosphoglycerate Kinase/genetics , Protein Binding , Protein Conformation , Protein Interaction Domains and Motifs/genetics , Protein Transport , Surface Plasmon Resonance
4.
Vet Microbiol ; 167(3-4): 584-91, 2013 Dec 27.
Article in English | MEDLINE | ID: mdl-24095145

ABSTRACT

Suilysin is a pore-forming cholesterol-dependent cytolysin secreted by Streptococcus suis (S. suis), an important swine and zoonotic pathogen. The role of suilysin in S. suis host-cell interaction is still unclear. We found a higher adherence and invasion rate of an unencapsulated sly-positive strain in comparison to its isogenic sly-negative mutant. Electron microscopy revealed that formation of membrane ruffles accompanying invasion of the sly-positive strain was abolished in the sly-negative mutant. Inhibition experiments showed that the actin cytoskeleton was involved in suilysin-mediated effects. Point-mutation of the domain putatively responsible for macropore-formation resulted in abolished hemolytic and cytolysin activity, but had no effect on S. suis host cell association. Concluding, our results indicate that subcytolytic suilysin promotes S. suis association with epithelial cells.


Subject(s)
Hemolysin Proteins/pharmacology , Host-Pathogen Interactions/drug effects , Streptococcal Infections/microbiology , Streptococcus suis/drug effects , Streptococcus suis/physiology , Swine Diseases/microbiology , Animals , Cell Line , Epithelial Cells/microbiology , Hemolysin Proteins/toxicity , Humans , Mutation , Streptococcus suis/genetics , Streptococcus suis/ultrastructure , Swine
5.
Vet Microbiol ; 162(1): 270-7, 2013 Feb 22.
Article in English | MEDLINE | ID: mdl-22939986

ABSTRACT

Although Streptococcus (S.) canis is known to cause severe infections in dogs and cats and harbors a clear zoonotic potential, knowledge about physiology and pathogenesis is mostly elusive. The arginine deiminase system (ADS) has been described in certain streptococcal species and its role in the establishment of infection has been suggested. In this study we focused on the identification and characterization of the ADS in S. canis. Using genome sequencing and subsequent in silico analysis we identified the ADS of S. canis as a gene cluster composed of seven genes. RT-PCR analysis revealed that the ADS of S. canis is transcribed in four transcriptional units, comprising three monocistronical mRNAs and one operon structure. As a secondary metabolic pathway, the ADS of S. canis is strictly regulated by carbon catabolite repression (CCR) and arginine as demonstrated on transcriptional, translational, and enzymatical level, respectively. Furthermore, growth kinetics with a chemically defined medium clearly showed that arginine, the substrate of the ADS, is essential for the biological fitness of S. canis. Using Immuno-electron microscopy analysis, we observed a surface-exposed localization of the ADS enzymes arginine deiminase (ArcA), ornithine carbamoyltransferase (ArcB), and carbamate kinase (ArcC), respectively, which might suggest the contribution of the ADS to the development of streptococcal infections.


Subject(s)
Hydrolases/genetics , Hydrolases/metabolism , Streptococcus/enzymology , Arginine/metabolism , Base Sequence , Hydrolases/chemistry , Multigene Family , Operon , Ornithine Carbamoyltransferase/metabolism , Phosphotransferases (Carboxyl Group Acceptor)/metabolism , Streptococcal Infections/enzymology , Streptococcal Infections/microbiology , Streptococcus/genetics , Streptococcus/metabolism
6.
Microbiology (Reading) ; 157(Pt 6): 1823-1833, 2011 Jun.
Article in English | MEDLINE | ID: mdl-21349980

ABSTRACT

Streptococcus suis is one of the most important pathogens in pigs and is also an emerging zoonotic agent. After crossing the epithelial barrier, S. suis causes bacteraemia, resulting in meningitis, endocarditis and bronchopneumonia. Since the host environment seems to be an important regulatory component for virulence, we related expression of virulence determinants of S. suis to glucose availability during growth and to the sugar metabolism regulator catabolite control protein A (CcpA). We found that expression of the virulence-associated genes arcB, representing arcABC operon expression, cps2A, representing capsular locus expression, as well as sly, ofs, sao and epf, differed significantly between exponential and early stationary growth of a highly virulent serotype 2 strain. Deletion of ccpA altered the expression of the surface-associated virulence factors arcB, sao and eno, as well as the two currently proven virulence factors in pigs, ofs and cps2A, in early exponential growth. Global expression analysis using a cDNA expression array revealed 259 differentially expressed genes in early exponential growth, of which 141 were more highly expressed in the CcpA mutant strain 10ΔccpA and 118 were expressed to a lower extent. Interestingly, among the latter genes, 18 could be related to capsule and cell wall synthesis. Correspondingly, electron microscopy characterization of strain 10ΔccpA revealed a markedly reduced thickness of the capsule. This phenotype correlated with enhanced binding to porcine plasma proteins and a reduced resistance to killing by porcine neutrophils. Taken together, our data demonstrate that CcpA has a significant effect on the capsule synthesis and virulence properties of S. suis.


Subject(s)
Bacterial Capsules/biosynthesis , Bacterial Proteins/metabolism , Gene Expression Regulation, Bacterial , Glucose/metabolism , Repressor Proteins/metabolism , Streptococcus suis/pathogenicity , Virulence Factors/metabolism , Animals , Bacterial Proteins/genetics , DNA, Complementary/genetics , DNA, Complementary/metabolism , Gene Expression Profiling , Mutation , Oligonucleotide Array Sequence Analysis , Repressor Proteins/genetics , Streptococcus suis/genetics , Streptococcus suis/growth & development , Streptococcus suis/metabolism , Swine , Virulence , Virulence Factors/genetics
SELECTION OF CITATIONS
SEARCH DETAIL