Modified coiled coil type proteins having improved properties

Abstract

The present application is related to a modified protein comprising a protein having a coiled coil domain and a peptide having the sequence such as shown in SEQ ID NO 1: ZXBBBBZ that is linked to the coiled coil domain wherein: Z is any amino acid or is absent; X is any amino acid; B is an arginine (R) or a lysine (K). Said modified protein is in particular an antigen or a carrier protein, associated to an antigen. This modified protein has an increased affinity for negatively charged polymers such as nucleic acids or heparin, and shows an increased immunogenicity.

Description

[0001] The present invention relates to recombinant antigens containing coiled coil domains or antigens fused to proteins containing coiled coils, wherein said coiled coils are modified. This modification improves the immunogenicity of the antigen. At the same time, it improves their ability to bind negatively charged polymers such as nucleic acids, including DNA and RNA, and to bind heparin. Background technique [0002] A coiled coil is a structural motif in proteins in which α-helices are coiled together like a rope. Coiled-coil domains are abundant in natural proteins (1,2) and are probably the most prevalent means of oligomerizing proteins in nature. A coiled-coil consists of two or more α-helices intertwined into a supercoil, a simple but versatile protein fold (3). A typical coiled-coil primary sequence is repetitive and consists of a seven-residue repeat called a "heptad". [0003] Many coiled-coil proteins are associated with important biological functions. The fo...

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Problems solved by technology

However, binding to RNA or ssDNA was not demonstrated, and Suzuki's data strongly suggest that binding to ssDNA does not occur because only the minor groove is present in the double helix molecule

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