Structural basis of transmembrane coupling of the HIV-1 envelope glycoprotein

Alessandro Piai, Qingshan Fu, Yongfei Cai, Fadi Ghantous, Tianshu Xiao, Md Munan Shaik, Hanqin Peng, Sophia Rits-Volloch, Wen Chen, Michael S. Seaman, Bing Chen () and James J. Chou ()
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Alessandro Piai: Harvard Medical School
Qingshan Fu: Harvard Medical School
Yongfei Cai: Boston Children’s Hospital
Fadi Ghantous: Beth Israel Deaconess Medical Center
Tianshu Xiao: Boston Children’s Hospital
Md Munan Shaik: Boston Children’s Hospital
Hanqin Peng: Boston Children’s Hospital
Sophia Rits-Volloch: Boston Children’s Hospital
Wen Chen: Harvard Medical School
Michael S. Seaman: Beth Israel Deaconess Medical Center
Bing Chen: Boston Children’s Hospital
James J. Chou: Harvard Medical School

Nature Communications, 2020, vol. 11, issue 1, 1-12

Abstract: Abstract The prefusion conformation of HIV-1 envelope protein (Env) is recognized by most broadly neutralizing antibodies (bnAbs). Studies showed that alterations of its membrane-related components, including the transmembrane domain (TMD) and cytoplasmic tail (CT), can reshape the antigenic structure of the Env ectodomain. Using nuclear magnetic resonance (NMR) spectroscopy, we determine the structure of an Env segment encompassing the TMD and a large portion of the CT in bicelles. The structure reveals that the CT folds into amphipathic helices that wrap around the C-terminal end of the TMD, thereby forming a support baseplate for the rest of Env. NMR dynamics measurements provide evidences of dynamic coupling across the TMD between the ectodomain and CT. Pseudovirus-based neutralization assays suggest that CT-TMD interaction preferentially affects antigenic structure near the apex of the Env trimer. These results explain why the CT can modulate the Env antigenic properties and may facilitate HIV-1 Env-based vaccine design.

Date: 2020
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DOI: 10.1038/s41467-020-16165-0

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