SurfaceListeria monocytogenescarbohydrate-binding components revealed by agglutination with neoglycoproteins
Autor: | J.M. Senet, O. Loiseau, C. Mahaza, B. Carbonnelle, Raymond Robert, Jane Cottin |
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Rok vydání: | 1990 |
Předmět: |
Protease
medicine.medical_treatment Proteolytic enzymes Lectin Carbohydrate Biology medicine.disease_cause Microbiology Direct agglutination chemistry.chemical_compound Agglutination (biology) chemistry Listeria monocytogenes Biochemistry Glucosamine Genetics medicine biology.protein Molecular Biology |
Zdroj: | FEMS Microbiology Letters. 68:301-306 |
ISSN: | 1574-6968 0378-1097 |
DOI: | 10.1111/j.1574-6968.1990.tb13955.x |
Popis: | 1. Summary Carbohydrate-binding components were shown to be present at the surface of Listeria monocytogenes by means of a panel of neoglycoproteins using direct agglutination. These lectin-like components bind on neoglycoproteins bearing d -glucosamine, l -fucosylamine, or para-amino-phenyl-α- d -mannopyrannoside residues. The interactions were inhibited by the carbohydrate moieties specific to the neoglycoproteins. The protein nature of the lectin-like components of L. monocytogenes was ascertained by the loss of carbohydratebinding capacity following protease treatment. |
Databáze: | OpenAIRE |
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