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Binding and degradation of lactoferrin by Porphyromonas gingivalis, Prevotella intermedia and Prevotella nigrescens.

Authors
  • de Lillo, A
  • Teanpaisan, R
  • Fierro, J F
  • Douglas, C W
Type
Published Article
Journal
FEMS immunology and medical microbiology
Publication Date
Jun 01, 1996
Volume
14
Issue
2-3
Pages
135–143
Identifiers
PMID: 8809549
Source
Medline
License
Unknown

Abstract

The ability of laboratory and clinical strains of Porphyromonas gingivalis, Prevotella intermedia and Prevotella nigrescens to bind and to degrade lactoferrin (Lf) has been assessed. Lf bound readily to whole cells of each species apparently via high-affinity site and one or more low-affinity sites. P. gingivalis showed a lower affinity for Lf than the other two species (P < 0.001). Virtually all strains of P. gingivalis completely degraded Lf under the conditions employed, whereas P. intermedia and P. nigrescens showed only partial degradation. These data suggest that Lf binds to a high-affinity receptor on all these bacteria and, particularly in the case of P. gingivalis, is then degraded by cell-associated proteases. This property may provide protection to the cell against the effects of Lf in periodontal sites and so is a possible virulence factor in disease. There was no association between the ability to degrade Lf and whether the strains had originated from healthy or diseased oral sites.

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