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The Journal of Medical Microbiology, Vol 29, Issue 2 121-130, Copyright © 1989 by Society for General Microbiology

JOURNAL ARTICLE

Identification of the transferrin- and lactoferrin-binding proteins in Haemophilus influenzae

A. B. Schryvers
Department of Microbiology and Infectious Diseases, University of Calgary, Alberta, Canada.

An affinity procedure with purified, biotinylated human transferrin and streptavidin-agarose was used to identify the transferrin-binding proteins in strains of Haemophilus influenzae. Proteins of 58 and 98 Kda were isolated from total membranes prepared from iron-deficient but not iron-sufficient H. influenzae KC548 cells. The 58-Kda protein was capable of binding human transferrin after sodium dodecyl sulphate (SDS)-polyacrylamide gel electrophoresis (PAGE) and electroblotting. Isolation of transferrin-binding proteins from type-b and non-typable H. influenzae strains demonstrated some variability in the size of the higher mol. wt protein (94-106 Kda) and in ease of elution of the smaller protein from the affinity resin. Use of purified, biotinylated human lactoferrin in the affinity isolation procedure with membranes from a strain expressing lactoferrin-binding activity resulted in isolation of proteins of 105 and 106 Kda distinct from the transferrin-binding proteins.


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