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Volume 34, Issue 6

Human lactoferrin binding in clinical isolates of Free

Abstract

Summary

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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© J. MED. MICROBIOL. 1991
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1991-06-01
2024-04-18
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Human lactoferrin binding in clinical isolates of Staphylococcus aureus
J. Med. Microbiol. 34, 323 (1991); https://doi.org/10.1099/00222615-34-6-323
/content/journal/jmm/10.1099/00222615-34-6-323
/content/journal/jmm/10.1099/00222615-34-6-323
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