1887

Abstract

Human lactoferrin (HLf) is an iron-binding protein and a host-defence component at the mucosal surface. Recently, a specific receptor for HLf has been identified on a strain of associated with toxic shock syndrome. We have looked for the occurrence of I-HLf binding among 489 strains of isolated from various clinical sources. HLf binding was common among strains associated with furunculosis (94·3%), toxic shock syndrome (94·3%) endocarditis (83·3%) and septicaemia (82·8%) and other (nasal, vaginal or ocular) infections (96·1%) with a mean binding (in fmol) of 29·1, 21·9, 16·9, 22·2 and 29·2 respectively; the differences between mean HLf binding values of 29·1–29·2, 21·9–22·2 and 16·9 were significant. Furunculosis-associated (low-invasive or localised) isolates were high-to-moderate binders of HLf; 50% gave positive results at a threshold of≫31 fmol of I-HLf bound. In contrast, endocarditis-associated (high-invasive or systemic) isolates demonstrated low binding and did not bind I-HLf at the above threshold level. recognised human or bovine Lf. However, boundI-HLf was more effectively inhibited in a dose-dependent manner by unlabelled bovine Lf than by homologous HLf. Binding of I-HLf to staphylococci was optimal with organisms grown in agar compared with those from broth cultures. The binding capacity of was abolished when strains were grown on carbohydrate- and salt-rich agar media. HLf-binding ability of did not correlate with fibronectin, fibrinogen, immunoglobulin G or laminin binding.

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/content/journal/jmm/10.1099/00222615-34-6-323
1991-06-01
2019-10-22
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http://instance.metastore.ingenta.com/content/journal/jmm/10.1099/00222615-34-6-323
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