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Osbourn, J.K. et al.

Osbourn, Earnshaw, Johnson, Parmentier, Timmermans, McCafferty,

Directed selection of MIP-1 alpha neutralizing CCR5 antibodies from a phage display human antibody library.

The seven trans-membrane chemokine receptor CCR-5 is a coreceptor for macrophage tropic HIV-1 strains. CCR-5 responds to a number of chemokines, including macrophage inflammatory protein (MIP)-1 alpha. We describe the use of MIP-1 alpha in a biotin tyramine- mediated proximity selection to guide the selection of CCR-5-specific phage antibodies from a large phage display human library. Proximity based selections resulted in a population of antibodies recognizing CCR-5 on primary CD4+ lymphocytes, none of which blocked MIP-1 alpha binding to cells. The selected population of phage antibodies were subsequently used as guide molecules for a second phase of selection that was carried out in the absence of MIP-1 alpha. This generated a panel of CCR-5-binding antibodies, of which around 20% inhibited MIP-1 alpha binding to CD4+. The single chain Fvs (scFv) generated by this step-back selection procedure also inhibited MIP-1 alpha-mediated calcium signaling.[1]

References

Directed selection of MIP-1 alpha neutralizing CCR5 antibodies from a phage display human antibody library. Osbourn, J.K., Earnshaw, J.C., Johnson, K.S., Parmentier, M., Timmermans, V., McCafferty, J. Nat. Biotechnol. (1998) [Pubmed]

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