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
- Klinisk mikrobiologi, Malmö
- Islet cell physiology
Publiceringsår
2006
Språk
Engelska
Sidor
2525-2534
Publikation/Tidskrift/Serie
European Journal of Immunology
Volym
9
Issue
Sep;36
Länkar
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