4.7 Article

Nontypeable Haemophilus influenzae Adhesin Protein E: Characterization and Biological Activity

Journal

JOURNAL OF INFECTIOUS DISEASES
Volume 199, Issue 4, Pages 522-531

Publisher

OXFORD UNIV PRESS INC
DOI: 10.1086/596211

Keywords

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Funding

  1. Alfred Osterlund
  2. Anna and Edwin Berger
  3. Crafoord
  4. Marianne and Marcus Wallenberg
  5. Greta and Johan Kock Foundations
  6. Swedish Medical Research Council
  7. Swedish Society of Medicine
  8. Cancer Foundation, Malmo University Hospital

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The adhesin protein E (PE) of the human respiratory pathogen nontypeable Haemophilus influenzae (NTHi) exists in all clinical isolates. In the present study, NTHi adherence to epithelial cells of various origins was further analyzed. The number of intraepithelial PE-deficient NTHi was decreased compared with PE-expressing NTHi. Interestingly, PE-expressing NTHi or Escherichia coli transformants, in addition to soluble recombinant PE22-160 without a lipid moiety, induced a proinflammatory cell response. The adhesive PE domain was defined within PE84-108, and preincubation of epithelial cells with this peptide blocked adhesion of several clinical NTHi isolates. Mice immunized with PE84-108 cleared NTHi up to 8-fold more efficiently on pulmonary challenge than did mice immunized with a control peptide. Finally, anti-PE mouse antibodies from vaccinated mice prevented NTHi adhesion. Our data suggest that the ubiquitous adhesin PE plays an important role in the pathogenesis of NTHi infection.

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