Grafting Segments From the Extracellular Surface of CCR5 Onto a Bacterirohodopsin Transmembrane Scaffold Confers HIV-1 Coreceptor Activity
N G. Abdulaev, T T. Strassmaier, T Ngo, Ruby I. Chen, H Lueke, K D. Ridge
Components from the extracellular surface of CCR5interact with certain macrophage-tropic strains of hu-man immunodeficiency virus type I (HIV-1) to mediateviral fusion and entry. To mimic these viral interactingsite(s), the amino-terminal and extracellular loop seg-ments of CCR5 were linked in tandem to form concate-nated polypeptides, or grafted onto a seven-trans-membrane bacteriorhodopsin scaffold to generateseveral chimeras. The chimera studies identified spe-cific regions in CCR5 that confer HIV-1 coreceptorfunction, structural rearrangements in the transmem-brane region that may modulate this activity, and a rolefor the extracellular surface in folding and assembly.Methods developed here may be applicable to the dis-section of functional domains from other seven-trans-membrane receptors and form a basis for future struc-tural studies.
, Strassmaier, T.
, Ngo, T.
, Chen, R.
, Lueke, H.
and Ridge, K.
Grafting Segments From the Extracellular Surface of CCR5 Onto a Bacterirohodopsin Transmembrane Scaffold Confers HIV-1 Coreceptor Activity, Structure
(Accessed September 21, 2023)