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Capsid forming and cystein modified chimaeric MS2-coat protein
| Details |
Inventors: Mastico, Robert Allan; Stockley, Peter George;
Assignee: British Technology Group Ltd. (GB2)
Primary Examiner: Feisee; Lila
Assistant Examiner: Reeves; Julie E.
Attorney, Agent or Firm: Graham & James LLP
A chimaeric protein is provided, capable of forming part of a capsid assembly and comprising the amino acid sequence of the coat protein of phage MS-2, or a conservatively modified variant thereof, or sufficient of said sequence or variant to retain the capability of forming a capsid assembly, which amino acid sequence has been modified by removal of the cysteine residues present externally of the N-terminal protruberant .beta.-hairpin of the coat protein and insertion of a cysteine residue within the region corresponding to the N-terminal protruberant .beta.-hairpin. |
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DETAILED DESCRIPTION We claim: 1.
A modified coat protein capable of forming a capsid which comprises the coat protein of a bacteriophage selected from the group consisting of MS-2, R17 and fr, wherein the coat protein is modified by an insertion of a cysteine residue in the region of corresponding to glycine residue 13 and 14 of N-terminal .
beta.
-hairpin region, and by replacement of each of the cysteine residues located external to the N-terminal .
beta.
-hairpin region by a non-cysteine amino acid residue.
2.
A modified coat protein capable of forming a capsid which comprises the coat protein of a bacteriophage selected from the group consisting of GA, Q.
beta.
and SP, wherein the coat protein is modified by an insertion of a cysteine residue in the region corresponding to glycine residue 13 and 14 of the N-terminal .
beta.
-hairpin region when the bacteriophage is GA, or in the region of amino acid residues corresponding to glycine residue 13 and 14 of GA when the bacteriophage is Q.
beta.
or SP, and, when the coat protein contains cysteine residues external to the N-terminal .
beta.
-hairpin region, the coat protein further modified by removal of each of the external cysteine residues.
3.
The modified coat protein according to claim 1, wherein the bacteriophage is MS-2.
4.
The modified coat protein according to claim 3, wherein the inserted cysteine residue replaces glycine 13 or 14 residue of the N-terminal .
beta.
-hairpin region of the coat protein.
5.
The modified coat protein according to claim 4, wherein each cysteine residue removed is replaced by a serine residue.
6.
The modified coat protein of claim 1 further comprising a foreign molecular species linked to the inserted cysteine residue.
7.
The modified coat protein of claim 6, wherein the foreign molecular species is linked to the inserted cysteine residue via a spacer moiety.
8.
The modified coat protein of claim 7, wherein the spacer moiety is derived from a bifunctional crosslinking reagent selected from the group consisting of m-maleimidobenzoyl-N-hydroxysulfosuccinimide ester, N-succinimidyl-(4-iodoacetyl)aminobenzoate and N-succinimidyl-3-(2-pyridyldithio)propionate
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