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Grafting Segments From the Extracellular Surface of CCR5 Onto a Bacterirohodopsin Transmembrane Scaffold Confers HIV-1 Coreceptor Activity

Published

Author(s)

N G. Abdulaev, T T. Strassmaier, T Ngo, Ruby I. Chen, H Lueke, K D. Ridge

Abstract

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.
Citation
Structure
Volume
10
Issue
No. 4

Keywords

bacterirohodopsin, extracellular surface, grafting segments

Citation

Abdulaev, N. , Strassmaier, T. , Ngo, T. , Chen, R. , Lueke, H. and Ridge, K. (2002), Grafting Segments From the Extracellular Surface of CCR5 Onto a Bacterirohodopsin Transmembrane Scaffold Confers HIV-1 Coreceptor Activity, Structure (Accessed April 23, 2024)
Created March 31, 2002, Updated October 12, 2021