Essential functional role of the polysaccharide intercellular adhesin of Staphylococcus epidermidis in hemagglutination.
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Essential functional role of the polysaccharide intercellular adhesin of Staphylococcus epidermidis in hemagglutination. / Mack, D; Riedewald, J; Rohde, Holger; Magnus, T; Feucht, H H; Elsner, H A; Laufs, R; Rupp, M E.
In: INFECT IMMUN, Vol. 67, No. 2, 2, 1999, p. 1004-1008.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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TY - JOUR
T1 - Essential functional role of the polysaccharide intercellular adhesin of Staphylococcus epidermidis in hemagglutination.
AU - Mack, D
AU - Riedewald, J
AU - Rohde, Holger
AU - Magnus, T
AU - Feucht, H H
AU - Elsner, H A
AU - Laufs, R
AU - Rupp, M E
PY - 1999
Y1 - 1999
N2 - Hemagglutination of erythrocytes is a common property of Staphylococcus epidermidis strains, which is related to adherence and biofilm formation and may be essential for the pathogenesis of biomaterial-associated infections caused by S. epidermidis. In three independent biofilm-producing, hemagglutination-positive S. epidermidis isolates, interruption of the icaADBC operon essential for polysaccharide intercellular adhesin (PIA) synthesis by Tn917 insertions led to a hemagglutination-negative phenotype. An immunoglobulin G fraction of antiserum to PIA greatly reduced hemagglutination. Purified PIA led to a 64-fold decrease of hemagglutination titers of these strains; however, it did not mediate hemagglutination by itself. These observations define PIA as the hemagglutinin of S. epidermidis or at least as its major functional component.
AB - Hemagglutination of erythrocytes is a common property of Staphylococcus epidermidis strains, which is related to adherence and biofilm formation and may be essential for the pathogenesis of biomaterial-associated infections caused by S. epidermidis. In three independent biofilm-producing, hemagglutination-positive S. epidermidis isolates, interruption of the icaADBC operon essential for polysaccharide intercellular adhesin (PIA) synthesis by Tn917 insertions led to a hemagglutination-negative phenotype. An immunoglobulin G fraction of antiserum to PIA greatly reduced hemagglutination. Purified PIA led to a 64-fold decrease of hemagglutination titers of these strains; however, it did not mediate hemagglutination by itself. These observations define PIA as the hemagglutinin of S. epidermidis or at least as its major functional component.
M3 - SCORING: Zeitschriftenaufsatz
VL - 67
SP - 1004
EP - 1008
JO - INFECT IMMUN
JF - INFECT IMMUN
SN - 0019-9567
IS - 2
M1 - 2
ER -