@article{mbs:/content/journal/jmm/10.1099/00222615-34-6-323, author = "Naidu, A. S. and Miedzobrodzki, J. and Musser, J. M. and Rosdahl, V. T. and HedstrÖm, S-Å. and Forsgren, A.", title = "Human lactoferrin binding in clinical isolates of Staphylococcus aureus", journal= "Journal of Medical Microbiology", year = "1991", volume = "34", number = "6", pages = "323-328", doi = "https://doi.org/10.1099/00222615-34-6-323", url = "https://www.microbiologyresearch.org/content/journal/jmm/10.1099/00222615-34-6-323", publisher = "Microbiology Society", issn = "1473-5644", type = "Journal Article", 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 Staphylococcus aureus associated with toxic shock syndrome. We have looked for the occurrence of 125I-HLf binding among 489 strains of S. aureus isolated from various clinical sources. HLf binding was common among S. aureus 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 125I-HLf bound. In contrast, endocarditis-associated (high-invasive or systemic) isolates demonstrated low binding and did not bind 125I-HLf at the above threshold level. S. aureus recognised human or bovine Lf. However, bound125I-HLf was more effectively inhibited in a dose-dependent manner by unlabelled bovine Lf than by homologous HLf. Binding of 125I-HLf to staphylococci was optimal with organisms grown in agar compared with those from broth cultures. The binding capacity of S. aureus was abolished when strains were grown on carbohydrate- and salt-rich agar media. HLf-binding ability of S. aureus did not correlate with fibronectin, fibrinogen, immunoglobulin G or laminin binding.", }