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The IgD C(H)1 region contains the binding site for the human respiratory pathogen Moraxella catarrhalis IgD-binding protein MID.

Författare

Summary, in English

The Moraxella catarrhalis IgD-binding protein (MID) has a unique specificity for human IgD, and the sequence with maximal IgD binding is located within the amino acids MID962-1200. In the present paper, we examined the MID binding site on IgD using a series of recombinant Ig. Full-length IgD, IgD F(ab')(2), and an IgD F(ab') C290R mutant lacking the inter-heavy-chain cysteine 290 were manufactured. Furthermore, a series of IgD/IgG chimeras were constructed. ELISA, dot blot and flow cytometry were used to study the binding of purified Ig to native MID, recombinant MID912-1200 or to Moraxella with or without MID. MID962-1200 bound both the IgD F(ab')(2) and F(ab') C290R, indicating that the binding occurred independently of antibody structure. When amino acids 157-224 of the IgD C(H)1 region were substituted with IgG sequences, binding by M. catarrhalis or recombinant MID962-1200 was abolished. Subsequent smaller substitutions of IgD C(H)1 157-224 with IgG sequences led us to conclude that IgD C(H)1 amino acids 198-206 were crucial for the interaction between MID and IgD.

Avdelning/ar

Publiceringsår

2006

Språk

Engelska

Sidor

2525-2534

Publikation/Tidskrift/Serie

European Journal of Immunology

Volym

9

Issue

Sep;36

Dokumenttyp

Artikel i tidskrift

Förlag

John Wiley & Sons Inc.

Ämne

  • Immunology in the medical area

Nyckelord

  • Moraxella catarrhalis
  • immunoglobulin D
  • binding

Status

Published

Forskningsgrupp

  • Clinical Microbiology, Malmö
  • Islet cell physiology

ISBN/ISSN/Övrigt

  • ISSN: 1521-4141