Conservation and antigenic cross-reactivity of the transferrin-binding proteins of Haemophilus influenzae, Actinobacillus pleuropneumoniae and Neisseria meningitidis

Article Abstract:

The transferrin-binding proteins (Tbps) of Haemophilus influenzae, Actinobacillus pleuropneumoniae and Neisseria meningitidis have shared epitopes, despite their transferrin species specificity. Screening of the human sera for the presence of cross-reactive antibodies to the Tbps revealed that sera from healthy adults contained antibodies which recognized both Tbp1 and Tbp2 from H. influenzae but not N. meningitidis. Convalescent sera from patients recovering from Haemophilus or meningococcal meningitis contained antibodies which recognized the Tbps2s of both pathogens on Western blots.

Physiological aspects, Neisseria meningitidis, Antigenic determinants, Hemophilus influenzae, Haemophilus influenzae

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Sequence, genetic analysis, and expression of Actinobacillus pleuropneumoniae transferrin receptor genes

Article Abstract:

The transcription of transferrin receptor genes tbpA and tbpB of Actinobacillus pleuropneumoniae, present in an operon, is controlled by one promoter. The structure of Tbp1 protein, encoded by tbpA, is similar to that of Lbp and Tbp1s proteins of Neisseria and the outer membrane (OM) receptors of Escherichia coil. Most of the recombinant Tbp1 formed by tbpA overexpression is present in the inclusion bodies while most of the recombinant Tbp2, encoded by tbpB, is present in the OM region. Both Tbp1 and Tbp2 bind to the C region of porcine transferrin.

Observations, Bacteria, Gene expression, Amino acid sequence, Amino acid sequencing

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The staphylococcus aureus and Staphylococcus epidermidis transferrin-binding proteins are expressed in vivo during infection

Article Abstract:

A cell wall associated protein in Staphylococcus aureus and S. epidermidis preferentially binds transferrin. This protein is expressed by this organisms in vivo during infection as determined from in vivo studies using mice. Further, antibodies against this protein has been identified among dialysis patients. Competitive binding assays have proven the specific binding affinity of this protein to transferrin.

Staphylococcus aureus, Membrane proteins, Staphylococcus

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