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  • 1
    Electronic Resource
    Electronic Resource
    Recognition by peptide mapping of three different structural groups of outer membrane protein YOP-1 of Yersinia enterocolitica and Yersinia pseudotuberculosis (1991)
    Springer
    Medical microbiology and immunology 180 (1991), S. 205-211 
    Details
    ISSN: 1432-1831
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The structural relation of YOP-1 of “european” and “american” Yersinia enterocolitica serotypes O∶3, O∶9, O∶5, 27, and O∶8 and O∶20, respectively, and Y. pseudotuberculosis serotypes I, II, and III was compared by sodium dodecyl sulfate polyacrylamide gel electrophoresis and peptide mapping using Staphylococcus aureus protease V8. Apparent molecular weights of YOP-1 ranged from 206,000 (O∶3) to approx. 180,000 (O∶8). According to their respective peptide maps YOP-1 of the “european” and “american” Y. enterocolitica serotypes and Y. pseudotuberculosis serotypes could be assigned to three different groups. Evaluation of several isolates of Y. enterocolitica serotypes O∶3, O∶9, and O∶8 by peptide mapping indicated that YOP-1 is conserved within a serotype. However, one serotype O∶8 isolate differed from the consensus peptide pattern of the other serotype O∶8 and O∶20 isolates. The similarity of the peptide patterns of Yersinia serotypes which predominate in certain geographical locations, i. e., “european” and “american” Y. enterocolitica serotypes, suggest common evolution of YOP-1 of these serotypes independent of the evolution of the other serotypes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00215249
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  • 2
    Electronic Resource
    Electronic Resource
    Characterization of different oligomeric species of the Yersinia enterocolitica outer membrane protein YadA (1994)
    Springer
    Medical microbiology and immunology 183 (1994), S. 217-227 
    Details
    ISSN: 1432-1831
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The oligomeric structure of the plasmid-encoded outer membrane protein YadA of Yersinia enterocolitica was studied by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and sucrose gradient sedimentation, respectively. The apparent molecular weight (M r) of the oligomeric 200-kDa YadA species detected by SDS-PAGE varied from 152,000 to 240,000 depending on the respective acrylamide concentration. The atypical electrophoretic behavior of the 200-kDa YadA species results from an exceptionally high relative free mobility as revealed by the Ferguson plot. In contrast, the apparent M r of 53,000 of the YadA monomer was independent of the acrylamide concentration. An additional oligomeric 116-kDa YadA species was detected by SDS-PAGE when membrane preparations of Y. enterocolitica were solubilized in SDS at 37 °C. The gel-purified 116-k Da YadA species was completely converted to the 200-kDa species by heating at 100 °C and to the monomeric form (M r 53,000) by heating in the presence of 10 M urea without reducing agents, respectively. This suggests that the 116-kDa YadA species represents the native oligomeric form of YadA, whereas the 200-kDa species is only generated from native YadA during denaturation in SDS. The significance of the 116-kDa YadA species is also supported by the rather slow sedimentation at about 6 S of detergent-solubilized YadA in sucrose gradients, which probably contains only two or three monomers.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00194174
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  • 3
    Electronic Resource
    Electronic Resource
    Experimental Yersinia enterocolitica infection in rats: analysis of the immune response to plasmid-encoded antigens of arthritis-susceptible Lewis rats and arthritis-resistent Fischer rats (1992)
    Springer
    Medical microbiology and immunology 181 (1992), S. 165-172 
    Details
    ISSN: 1432-1831
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Recently, experimentally Yersinia-induced arthritis in Lewis and SHR rats has been described as a potential animal model for analyzing the pathomechanism of reactive arthritis (Toivanen et al. 1986; Hill and Yu 1987). We could confirm that Lewis but not Fischer rats develop aseptic arthritis about 2 weeks after an intravenous inoculation of Yersinia enterocolitica, serotype 0∶8 (Hill and Yu 1987). Moreover, we compared the antibody response to virulence-associated Yersinia antigens (Yops) of experimentally infected Lewis rats with that of Fischer rats using an enzyme-linked immunosorbent assay (ELISA) and immunoblotting. The ELISA results revealed a more rapid and vigorous specific IgG, IgA and IgM response for Lewis rats than for Fischer rats in the early state of infection. As demonstrated by immunoblotting, the IgG response was directed predominantly against the plasmid-encoded YopM, YopH, YopD and the V-antigen during the acute phase followed by antibodies against YopE and YadA. Although both rat strains seroconverted against this set of antigens, IgG antibodies to YadA were more prevalent and of higher titer in arthritis-susceptible rats compared to arthritis-resistent rats.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00202056
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  • 4
    Electronic Resource
    Electronic Resource
    Induction of Staphylococcus epidermidis biofilm formation via proteolytic processing of the accumulation-associated protein by staphylococcal and host proteases (2005)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 55 (2005), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Because of its biofilm forming potential Staphylococcus epidermidis has evolved as a leading cause of device-related infections. The polysaccharide intercellular adhesin (PIA) is significantly involved in biofilm accumulation. However, infections because of PIA-negative strains are not uncommon, suggesting the existence of PIA-independent biofilm accumulation mechanisms. Here we found that biofilm formation in the clinically significant S. epidermidis 5179 depended on the expression of a truncated 140 kDa isoform of the 220 kDa accumulation-associated protein Aap. As expression of the truncated Aap isoform leads to biofilm formation in aap-negative S. epidermidis 1585, this domain mediates intercellular adhesion in a polysaccharide-independent manner. In contrast, expression of full-length Aap did not lead to a biofilm-positive phenotype. Obviously, to gain adhesive function, full-length Aap has to be proteolytically processed through staphylococcal proteases as demonstrated by inhibition of biofilm formation by α2-macroglobulin. Importantly, also exogenously added granulocyte proteases activated Aap, thereby inducing biofilm formation in S. epidermidis 5179 and four additional, independent clinical S. epidermidis strains. It is therefore reasonable to assume that in vivo effector mechanisms of the innate immunity can directly induce protein-dependent S. epidermidis cell aggregation and biofilm formation, thereby enabling the pathogen to evade clearance by phagocytes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.2005.04515.x
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  • 5
    Electronic Resource
    Electronic Resource
    Molecular basis of intercellular adhesion in the biofilm-forming Staphylococcus epidermidis (1996)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 20 (1996), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The Staphylococcus epidermidis genes icaABC are involved in the synthesis of the polysaccharide intercellular adhesin (PIA), which is located mainly on the cell surface, as shown by immunofluorescence studies with PIA-specific antiserum. PIA was shown to be a linear β-1,6-linked glucosaminoglycan composed of at least 130 2-deoxy-2-amino-D-glucopyrano-syl residues of which 80–85% are N-acetylated, the rest being non-N-acetylated and positively charged. A transposon insertion in the icaABC gene cluster (ica, intercellular adhesion) led to the loss of several traits, such as the ability to form a biofilm on a polystyrene surface, cell aggregation, and PIA production. The mutant could be complemented by transformation with the IcaABC-carrying plasmid pCN27. Transfer of pCN27 into the heterologous host Staphylococcus carnosus led to the formation of large cell aggregates, the formation of a biofilm on a glass surface, and PIA expression. The nucleotide sequence of icaABC suggests that the three genes are organized in an operon and that they are co-transcribed from the mapped ica A promoter. Ica A contains four potential transmembrane helices, indicative of a membrane location. The deduced Ica A sequence shows similarity to those of polysaccharide-polymerizing enzymes, the most pronounced being with a Rhizobium meliloti N-acetylglucosaminyltransferase involved in lipo-chitin biosynthesis (22.5% overall identity and 37.4% overall similarity). This similarity suggests that Ica A has N-acetylglucosaminyltransferase activity in the formation
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1996.tb02548.x
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  • 6
    Electronic Resource
    Electronic Resource
    Gastric tonometry accurately predicts mortality in experimental peritonitis in both laparoscopic and conventional surgery (1999)
    Springer
    Langenbeck's archives of surgery 384 (1999), S. 76-83 
    Details
    ISSN: 1435-2451
    Keywords: Key words Peritonitis ; Sepsis ; Tonometry ; Pneumoperitoneum ; Laparoscopic surgery ; Conventional surgery ; Mortality
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Objectives: Tonometry is widely used in the diagnosis of sepsis and splanchnic ischemia. This study was devised to analyze the predictive value of gastric tonometry for outcome of experimental viscus perforation-induced peritonitis. The impact of conventional and laparoscopic intervention on tonometric measurements was the main scope. Methods: This randomized controlled intervention trial was performed in a University experimental laboratory, using 24 female Duroc pigs. Pigs were subjected to gastric perforation followed by a 12 h interval of peritonitis, and then to either laparoscopic or conventional surgical repair of the defect with peritoneal lavage. Gastric tonometry and cardiocirculatory monitoring were performed. Results: Septic shock associated with peritonitis and subsequent lethal outcome was accurately predicted with gastric tonometry. Changes of gastric mucosal pH correlated significantly with decreases of MAP (r 2 = 0.880; P 〈 0.001) and SVR (r 2 = 0.678; P 〈 0.001), increase of QT (r 2 = 0.486; P = 0.013), and mortality (r = 0.752; P 〈 0.001). Mortality was significantly higher in laparoscopically treated animals compared to those subjected to the open procedure (78% vs 22%; P 〈 0.045). Conclusions: Gastric tonometry accurately predicted mortality in experimental peritonitis. The decline of gastric mucosal pH in the laparoscopic group was more than double that of to conventionally treated animals. This finding not only reflected the increase of systemic CO2 due to higher absorption during CO2-pneumoperitoneum, but probably also indicated a more severe form of splanchnic ischemia during laparoscopic surgery. Even though tonometry can be used to accurately predict mortality and separate the high risk group, extreme caution should be applied under conditions associated with severe peritonitis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004230050178
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