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• W1836093301 abstract "Research Article18 April 1995free access Protein H--a bacterial surface protein with affinity for both immunoglobulin and fibronectin type III domains. I.M. Frick I.M. Frick Department of Medical and Physiological Chemistry, Lund University, Sweden. Search for more papers by this author K.L. Crossin K.L. Crossin Department of Medical and Physiological Chemistry, Lund University, Sweden. Search for more papers by this author G.M. Edelman G.M. Edelman Department of Medical and Physiological Chemistry, Lund University, Sweden. Search for more papers by this author L. Björck L. Björck Department of Medical and Physiological Chemistry, Lund University, Sweden. Search for more papers by this author I.M. Frick I.M. Frick Department of Medical and Physiological Chemistry, Lund University, Sweden. Search for more papers by this author K.L. Crossin K.L. Crossin Department of Medical and Physiological Chemistry, Lund University, Sweden. Search for more papers by this author G.M. Edelman G.M. Edelman Department of Medical and Physiological Chemistry, Lund University, Sweden. Search for more papers by this author L. Björck L. Björck Department of Medical and Physiological Chemistry, Lund University, Sweden. Search for more papers by this author Author Information I.M. Frick1, K.L. Crossin1, G.M. Edelman1 and L. Björck1 1Department of Medical and Physiological Chemistry, Lund University, Sweden. The EMBO Journal (1995)14:1674-1679https://doi.org/10.1002/j.1460-2075.1995.tb07156.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Several bacterial species express surface proteins with affinity for the constant region (Fc) of immunoglobulin (Ig) G. The biological consequences of the interaction with IgG are poorly understood but it has been demonstrated that genes encoding different IgG Fc-binding proteins have undergone convergent evolution, suggesting that these surface molecules are connected with essential microbial functions. One of the molecules, protein H, is present in some strains of Streptococcus pyogenes, the most significant streptococcal species in clinical medicine. In contrast to other Ig-binding bacterial proteins tested, protein H was found to interact also with the neural cell adhesion molecule (N-CAM), a eukaryotic cell surface glycoprotein mediating homo- and heterophilic cell-cell interactions. The affinity for the interaction between protein H and N-CAM was 1.6 × 10(8)/M and the binding site on protein H was mapped to the NH2-terminal 80 amino acid residues. N-CAM and IgG are both members of the Ig superfamily and analogous to N-CAM, IgG binds to the NH2-terminal part of protein H. However, the binding sites for the two proteins were found to be separate, an unexpected result which was explained by the observation that the fibronectin type III (FNIII) domains and not the Ig-like domains of N-CAM are responsible for the interaction with protein H. Thus, the binding of N-CAM to protein H was blocked with fibronectin but not with IgG. Moreover, apart from fibronectin itself and N-CAM, fragments of fibronectin and the matrix protein cytotactin/tenascin containing FNIII domains also showed affinity for protein H.(ABSTRACT TRUNCATED AT 250 WORDS) Previous ArticleNext Article Volume 14Issue 81 April 1995In this issue RelatedDetailsLoading ..." @default.
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• W1836093301 title "Protein H--a bacterial surface protein with affinity for both immunoglobulin and fibronectin type III domains." @default.
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