Biochemical analysis of lactoferrin receptors in the Neisseriaceae: Identification of a second bacterial lactoferrin receptor protein

Robert A. Bonnah, Rong Hua Yu, Anthony B. Schryvers

Research output: Contribution to journalArticle

42 Scopus citations

Abstract

Bacterial transferrin receptors that have been described in the families Pasteurellaceae and Neisseriaceae are composed of two receptor proteins, transferrin binding proteins 1 and 2 (Tbp1 and Tbp2). In contrast, bacterial lactoferrin receptors have only been described for human pathogens in the family Neisseriaceae, and were believed to consist of a single protein, Lbp1, which is highly homologous to Tbp1. We describe a modified affinity isolation procedure that facilities isolation of a second lactoferrin receptor protein Lbp2 (a presumptive Tbp2 homologue) from Neisseria meningitidis, Moraxella catarrhalis and Moraxella bovis using immobilized lactoferrin. Antiserum specific for either the M. catarrhalis Tbp1+2 molecules, the M. catarrhalis Lbp1 molecule, or for a commercial preparation of human lactoferrin did not react on western blots with the same organisms’ affinity purified Lbp2. In addition, the M. catarrhalis Lbp2 could be isolated in a functional form without contaminating Lbp1 or Tbp1+2. We also demonstrate that the bovine pathogen, M. bovis, produces functional transferrin and lactoferrin receptors specific for the bovine forms of these glycoproteins. A putative IbpB gene, recently speculated to reside immediately upstream of the N. meningitidis Lbp1 structural gene, IbpA, likely encodes the newly isolated Lbp2 protein from this bacterial species.

Original languageEnglish (US)
Pages (from-to)285-297
Number of pages13
JournalMicrobial Pathogenesis
Volume19
Issue number5
DOIs
StatePublished - Jan 1 1995

Keywords

  • Iron acquisition
  • Lactoferrin
  • Moraxella
  • Neisseria
  • Receptor

ASJC Scopus subject areas

  • Microbiology
  • Infectious Diseases

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