Change search
ReferencesLink to record
Permanent link

Direct link
Isolated hypervariable regions derived from streptococcal M proteins specifically bind human C4b-binding protein: implications for antigenic variation.
Lund University.
Lund University.
Lund University.
Lund University.
Show others and affiliations
2001 (English)In: Journal of Immunology, ISSN 0022-1767, E-ISSN 1550-6606, Vol. 167, no 7, 3870-7 p.Article in journal (Refereed) Published
Abstract [en]

Antigenic variation in microbial surface proteins represents an apparent paradox, because the variable region must retain an important function, while exhibiting extensive immunological variability. We studied this problem for a group of streptococcal M proteins in which the approximately 50-residue hypervariable regions (HVRs) show essentially no residue identity but nevertheless bind the same ligand, the human complement regulator C4b-binding protein (C4BP). Synthetic peptides derived from different HVRs were found to retain the ability to bind C4BP, implying that the HVR corresponds to a distinct ligand-binding domain that can be studied in isolated form. This finding allowed direct characterization of the ligand-binding properties of isolated HVRs and permitted comparisons between different HVRs in the absence of conserved parts of the M proteins. Affinity chromatography of human serum on immobilized peptides showed that they bound C4BP with high specificity and inhibition experiments indicated that different peptides bound to the same site in C4BP. Different C4BP-binding peptides did not exhibit any immunological cross-reactivity, but structural analysis suggested that they have similar folds. These data show that the HVR of streptococcal M protein can exhibit extreme variability in sequence and immunological properties while retaining a highly specific ligand-binding function.

Place, publisher, year, edition, pages
2001. Vol. 167, no 7, 3870-7 p.
National Category
Immunology Bioinformatics and Systems Biology
URN: urn:nbn:se:kth:diva-82634PubMedID: 11564804OAI: diva2:498406
NR 20140805Available from: 2012-02-12 Created: 2012-02-12 Last updated: 2012-02-12Bibliographically approved

Open Access in DiVA

No full text


Search in DiVA

By author/editor
Lindahl, E
By organisation
In the same journal
Journal of Immunology
ImmunologyBioinformatics and Systems Biology

Search outside of DiVA

GoogleGoogle Scholar
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Altmetric score

Total: 16 hits
ReferencesLink to record
Permanent link

Direct link