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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Regions in beta-chemokine receptors CCR5 and CCR2b that determine HIV-1 cofactor specificity.

Macrophage-tropic (M-tropic) HIV-1 strains use the beta-chemokine receptor CCR5, but not CCR2b, as a cofactor for membrane fusion and infection, while the dual-tropic strain 89.6 uses both. CCR5/2b chimeras and mutants were used to map regions of CCR5 important for cofactor function and specificity. M-tropic strains required either the amino-terminal domain or the first extracellular loop of CCR5. A CCR2b chimera containing the first 20 N-terminal residues of CCR5 supported M-tropic envelope protein fusion. Amino-terminal truncations of CCR5/CCR2b chimeras indicated that residues 2-5 are important for M-tropic viruses, while 89.6 is dependent on residues 6-9. The identification of multiple functionally important regions in CCR5, coupled with differences in how CCR5 is used by M- and dual-tropic viruses, suggests that interactions between HIV-1 and entry cofactors are conformationally complex.[1]

References

  1. Regions in beta-chemokine receptors CCR5 and CCR2b that determine HIV-1 cofactor specificity. Rucker, J., Samson, M., Doranz, B.J., Libert, F., Berson, J.F., Yi, Y., Smyth, R.J., Collman, R.G., Broder, C.C., Vassart, G., Doms, R.W., Parmentier, M. Cell (1996) [Pubmed]
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