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Characterisation of a recombinant human granulocyte-colony stimulating factor fused to the major outer membrane protein of Neisseria meningitidis. We have constructed a fusion protein between the major outer membrane protein (P40) of Neisseria meningitidis and the recombinant human granulocyte-colony stimulating factor (G-CSF) by insertion of a polylinker coding sequence between the N-terminal amino-acid residues of G-CSF. The G-CSF-P40 fusion protein stimulated cell-surface receptor-mediated chemotaxis and superoxide production by human neutrophils in response to G-CSF. The G-CSF-P40 fusion protein was purified from Escherichia coli by a combination of sucrose gradient centrifugation and preparative gel electrophoresis. The ratio of G-CSF to P40 in this preparation was 3:1. Both G-CSF and P40 were monomeric in solution by gel filtration and dynamic light scattering. The fusion protein had the same N-terminal amino-acid composition as P40 (one N-terminal proline and three serine residues), and the amino-acid sequence of the first 23 N-terminal residues of G-CSF was preserved in the fusion protein. In addition, the G-CSF-P40 fusion protein retained the ability of G-CSF to stimulate production of superoxide.

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