Biomedical subjects

F Ascencio

Publications and source records attributed to F Ascencio.

42 records · Page 3Linked to original sources

PubMed1992

Lactoferrin binding properties of Vibrio cholerae.

The lactoferrin binding properties of Vibrio cholerae, a non-invasive pathogen were investigated. Screening of fifty V. cholerae strains of different serogroups and serotypes, showed that 10% of the V. cholerae strains bound to 125I-labelled lactoferrin, and 40% of the 125I-labelled lactoferrin bound to V. cholerae strain 623 could be displaced by unlabelled lactoferrin. Other iron-binding glycoproteins and ferroproteins like ferritin, transferrin, haemoglobin, and myoglobin inhibited the binding of 125I-lactoferrin to a lesser degree. Monosaccharides (GalNac, Man, Gal, and Fuc), and other glycoproteins such as fetuin and orosomucoid also inhibited the binding to a lesser extent. V. cholerae 623 showed a cell surface associated-proteolytic activity which cleaved off the cell-bound 125I-labelled lactoferrin. The generation of cryptotopes on the V. cholerae cell surface by proteolytic digestion favoured the binding of ferritin, transferrin, haemoglobin, and haemin, as well as Congo red, to cells of V. cholerae 623.

Animals↗

PubMed1991

New lectins and other putative adhesins in Aeromonas hydrophila.

The ability of strains of Aeromonas hydrophila to bind 125I-labelled collagen types I and IV, fibronectin, laminin, lactoferrin, and immobilized mucins and orosomucoid on latex beads was found to be a property common to all the isolated strains. The binding was specific, was inhibited by homologous unlabelled glycoproteins, and was protease sensitive. The nature of the binding is discussed.

Aeromonas↗

PubMed1991

Effect of Aeromonas proteases on the binding of Aeromonas hydrophila strains to connective tissue proteins.

125I-labelled connective tissue protein binding to cells of Aeromonas hydrophila, A. caviae, and A. sobria strains isolated from diseased fish, was correlated with the Aeromonas protease degradation of 125I-labelled collagen types I and IV, fibronectin and laminin, immobilized on tissue culture microtitre plates. An inverse relation between 125I-labelled connective tissue protein binding to cells of Aeromonas strains and proteolytic degradation of immobilized connective tissue proteins by Aeromonas proteases was established. Inhibition of the Aeromonas proteolytic activity by protease inhibitors enhances the 125I-labelled connective tissue protein binding to cells of Aeromonas hydrophila strains. Culture conditions were found to influence both expression of proteolytic activity and binding properties.

Aeromonas↗

PubMed1991

Comparative study of extracellular matrix protein binding to Aeromonas hydrophila isolated from diseased fish and human infection.

Binding of 125I-labelled types I and IV collagen, fibronectin and laminin to Aeromonas cells is a common characteristic among Aeromonas strains isolated from diseased fish and human infections. The proportion of Aeromonas strains which bind to the various proteins were significantly greater for A. hydrophila than for A. sobria or A. caviae. The binding property was specific since it was inhibited by unlabelled homologous proteins. Bacterial cells incubated with proteolytic enzymes lose the ability of binding to 125I-labelled collagen type I and IV, fibronectin, laminin and vitronectin. A bacterial cell surface protein extract, containing active receptors competes with intact cells for 125I-extracellular matrix protein binding. Culture conditions greatly influence the expression of A. hydrophila cell surface binding structures for extracellular matrix proteins. The presence of calcium ions in the growth medium seems to be an important enhancer of the expression of extracellular matrix protein cell surface receptors.

Aeromonas↗

PubMed1990

Type I and IV collagen and fibrinogen binding to Aeromonas species isolated from various infections.

Collagen binding is a common property of strains of Aeromonas species. However, agglutination of latex beads coated with types I and IV collagen and fibrinogen with Aeromonas cells varied among strains of Aeromonas species and their source of isolation. Culture media and growth conditions greatly influenced expression of Aeromonas cell surface receptors to bind collagen (types I and IV) and fibrinogen immobilized on the latex particles as suggested by the particle agglutination assay (PAA). Aeromonas cells aggregated with the differentially coated latex beads in a specified manner. Furthermore, the PAA method was found to be rapid, easy to perform and sensitive for routine screening of a large number of strains for serum and connective-tissue protein cell surface receptors.

Aeromonas↗

PubMed1990

Particle agglutination assays to identify fibronectin and collagen cell surface receptors and lectins in Aeromonas and Vibrio species.

A rapid particle agglutination assay (PAA) utilizing latex beads coated with connective tissue and serum proteins was evaluated for its ability to identify fibronectin, collagen (types I and IV), fibrinogen, and transferrin cell surface receptors on Vibrio and Aeromonas strains isolated from diseased fish, human infections, and the environment. Similar tests were performed to screen for cell surface lectins. Vibrio as well as Aeromonas strains were found to bind connective tissue proteins (collagen types I, II, and IV and fibronectin), serum proteins (i.e., fibrinogen), and glycoproteins (bovine submaxillary mucin, hog gastric mucin, orosomucoid, and fetuin) immobilized on the latex particles. The specificity of the agglutination reaction was studied by particle agglutination inhibition assays performed by preincubating bacterial suspensions in solutions containing either gelatin (for the various connective tissue protein PAA reagents) or sialic acid-rich glycoproteins (for the various glycoprotein PAA reagents). Expression of cell surface receptors for connective tissue proteins was found to depend on culture methods.

Aeromonas↗