Binding inhibition of type 1 fimbriae to human granulocytes: a flow cytometric inhibition assay using trivalent cluster mannosides.

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Binding inhibition of type 1 fimbriae to human granulocytes: a flow cytometric inhibition assay using trivalent cluster mannosides. / Horst, Andrea; Kötter, S; Lindhorst, T K; Ludwig, A; Brandt, E; Wagener, C.

In: MED MICROBIOL IMMUN, Vol. 190, No. 3, 3, 2001, p. 145-149.

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@article{32a76e72bc46490d807e3db5b77921d0,
title = "Binding inhibition of type 1 fimbriae to human granulocytes: a flow cytometric inhibition assay using trivalent cluster mannosides.",
abstract = "The binding of type 1 fimbriae from Escherichia coli to vital human neutrophilic granulocytes was inhibited by synthetic trivalent cluster mannosides. Binding of type 1 fimbriae was measured in a flow cytometric assay. Based on the molarity of mannosyl residues, the clusters exceed the inhibitory potency of methyl alpha-D-mannoside by a factor of more than 1,000 and the inhibitory potency of p-nitrophenyl alpha-D-mannoside by a factor of more than 10. The inhibition studies indicate that the trivalent cluster mannosides are very potent inhibitors of the binding of type 1 fimbriae to human neutrophilic granulocytes. Based on their defined structure, cluster mannosides are well suited for characterizing the molecular interactions of mannose-sensitive fimbriae with their cell membrane receptors.",
author = "Andrea Horst and S K{\"o}tter and Lindhorst, {T K} and A Ludwig and E Brandt and C Wagener",
year = "2001",
language = "Deutsch",
volume = "190",
pages = "145--149",
journal = "MED MICROBIOL IMMUN",
issn = "0300-8584",
publisher = "Springer",
number = "3",

}

RIS

TY - JOUR

T1 - Binding inhibition of type 1 fimbriae to human granulocytes: a flow cytometric inhibition assay using trivalent cluster mannosides.

AU - Horst, Andrea

AU - Kötter, S

AU - Lindhorst, T K

AU - Ludwig, A

AU - Brandt, E

AU - Wagener, C

PY - 2001

Y1 - 2001

N2 - The binding of type 1 fimbriae from Escherichia coli to vital human neutrophilic granulocytes was inhibited by synthetic trivalent cluster mannosides. Binding of type 1 fimbriae was measured in a flow cytometric assay. Based on the molarity of mannosyl residues, the clusters exceed the inhibitory potency of methyl alpha-D-mannoside by a factor of more than 1,000 and the inhibitory potency of p-nitrophenyl alpha-D-mannoside by a factor of more than 10. The inhibition studies indicate that the trivalent cluster mannosides are very potent inhibitors of the binding of type 1 fimbriae to human neutrophilic granulocytes. Based on their defined structure, cluster mannosides are well suited for characterizing the molecular interactions of mannose-sensitive fimbriae with their cell membrane receptors.

AB - The binding of type 1 fimbriae from Escherichia coli to vital human neutrophilic granulocytes was inhibited by synthetic trivalent cluster mannosides. Binding of type 1 fimbriae was measured in a flow cytometric assay. Based on the molarity of mannosyl residues, the clusters exceed the inhibitory potency of methyl alpha-D-mannoside by a factor of more than 1,000 and the inhibitory potency of p-nitrophenyl alpha-D-mannoside by a factor of more than 10. The inhibition studies indicate that the trivalent cluster mannosides are very potent inhibitors of the binding of type 1 fimbriae to human neutrophilic granulocytes. Based on their defined structure, cluster mannosides are well suited for characterizing the molecular interactions of mannose-sensitive fimbriae with their cell membrane receptors.

M3 - SCORING: Zeitschriftenaufsatz

VL - 190

SP - 145

EP - 149

JO - MED MICROBIOL IMMUN

JF - MED MICROBIOL IMMUN

SN - 0300-8584

IS - 3

M1 - 3

ER -