AbstractPseudomonas aeruginosa lectin PA-II agglutinates human peripheral lymphocytes and stimulates mitogenesis (predominantly in T cells), like the plant lectins PHA and Con A. Murine splenocytes are also agglutinated and stimulated by PA-II as by Con A. Sialidase treatment of the human and murine cells enhances their agglutination and augments the stimulation of human lymphocytes at low PA-II concentrations. The PA-II agglutinating and mitogenic effects are specifically inhibited by L-fucose. The bacterial source and the specificity of PA-II for L-fucose are both rare features among the hitherto described mitogenic lectins. However, since this lectin also binds mannose, a mannose-bearing receptor might be involved in its mitogenicity
Lectin-like bacteriocins are antibacterial proteins constituted of two structurally similar monocot ...
SummaryThe human pathogenic bacterium Pseudomonas aeruginosa produces a fucose-specific lectin, LecB...
Lectins are glycan-binding proteins with no catalytic activity and ubiquitously expressed in nature....
AbstractPseudomonas aeruginosa lectin PA-II agglutinates human peripheral lymphocytes and stimulates...
Slime glycolipoprotein of Pseudomonasaeruginosa has been found to exert a mitogenic effect on human ...
A unique sialic-acid-binding lectin, AchatininH, isolated from the hemolymph of Achatina fulica snai...
AbstractNumerous bacterial strains produce surface lectins, commonly in the form of fimbriae that ar...
Bacterial biofilms represent a challenge to the healthcare system because of their resilience agains...
Copyright © 2015 Park-media, Ltd. This is an open access article distributed under the Creative Comm...
Pseudomonas aeruginosa is an opportunistic pathogen that causes nosocomial infections most commonly ...
Lectin-like bacteriocins consist of tandem monocot mannose-binding domains and display a genus-speci...
AbstractLipopolysaccharide (LPS) induction of TNF-α release is a central event in the pathophysiolog...
Lectin-like bacteriocins consist of tandem monocot mannose-binding domains and display a genus-speci...
Bacterial lectins are typically multivalent and bind noncovalently to specific carbohydrates on host...
Lipopolysaccharide (LPS, endotoxin), the main surface antigen and virulence factor of Gram-negative ...
Lectin-like bacteriocins are antibacterial proteins constituted of two structurally similar monocot ...
SummaryThe human pathogenic bacterium Pseudomonas aeruginosa produces a fucose-specific lectin, LecB...
Lectins are glycan-binding proteins with no catalytic activity and ubiquitously expressed in nature....
AbstractPseudomonas aeruginosa lectin PA-II agglutinates human peripheral lymphocytes and stimulates...
Slime glycolipoprotein of Pseudomonasaeruginosa has been found to exert a mitogenic effect on human ...
A unique sialic-acid-binding lectin, AchatininH, isolated from the hemolymph of Achatina fulica snai...
AbstractNumerous bacterial strains produce surface lectins, commonly in the form of fimbriae that ar...
Bacterial biofilms represent a challenge to the healthcare system because of their resilience agains...
Copyright © 2015 Park-media, Ltd. This is an open access article distributed under the Creative Comm...
Pseudomonas aeruginosa is an opportunistic pathogen that causes nosocomial infections most commonly ...
Lectin-like bacteriocins consist of tandem monocot mannose-binding domains and display a genus-speci...
AbstractLipopolysaccharide (LPS) induction of TNF-α release is a central event in the pathophysiolog...
Lectin-like bacteriocins consist of tandem monocot mannose-binding domains and display a genus-speci...
Bacterial lectins are typically multivalent and bind noncovalently to specific carbohydrates on host...
Lipopolysaccharide (LPS, endotoxin), the main surface antigen and virulence factor of Gram-negative ...
Lectin-like bacteriocins are antibacterial proteins constituted of two structurally similar monocot ...
SummaryThe human pathogenic bacterium Pseudomonas aeruginosa produces a fucose-specific lectin, LecB...
Lectins are glycan-binding proteins with no catalytic activity and ubiquitously expressed in nature....