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Construction of Recombinant Chimeric Human Lactoferrin/Bovine Transferrins

  • Henry Wong
  • Anthony B. Schryvers
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 443)

Abstract

One of the contributing factors to bacterial pathogenesis is the ability to acquire iron (Fe) in the extremely Fe scarce environment of the host. The families Neisseriaceae and Pasteurellaceae, which include a number of human and veterinary pathogens, express outer membrane receptors that specifically bind and remove Fe from the hosts’ Fe binding proteins, transferrin (Tf) and lactoferrin (Lf)5. The bacterial Lf receptor was initially identified by affinity methods with immobilized human Lf (hLf) as the affinity matrix, using high salt and pH conditions to minimize nonspecific interactions11. These studies identified a single Fe-repressible outer membrane protein, lactoferrin binding protein (Lbp), in constrast to the two transferrin binding proteins, transferrin binding protein A (TbpA) and transferrin binding protein B (TbpB), that were isolated with a Tf affinity column11. Lbp shared several properties with TbpA and once the gene encoding Lbp was cloned9 it was apparent that the predicted protein sequence was homologous to TbpA.

Keywords

Hybrid Gene Neisseria Meningitidis Moraxella Catarrhalis Unique Restriction Site Baculovirus Expression Vector System 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1998

Authors and Affiliations

  • Henry Wong
    • 1
  • Anthony B. Schryvers
    • 1
  1. 1.Department of Microbiology and Infectious Diseases Faculty of MedicineUniversity of CalgaryCalgaryCanada

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