Divergent engagements between adeno-associated viruses with their cellular receptor AAVR

Ran Zhang, Guangxue Xu, Lin Cao, Zixian Sun, Yong He, Mengtian Cui, Yuna Sun, Shentao Li, Huapeng Li, Lan Qin, Mingxu Hu, Zhengjia Yuan, Zipei Rao, Wei Ding, Zihe Rao and Zhiyong Lou ()
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Ran Zhang: Tsinghua University
Guangxue Xu: Tsinghua University
Lin Cao: Nankai University
Zixian Sun: Tsinghua University
Yong He: Nankai University
Mengtian Cui: Capital Medical University
Yuna Sun: Chinese Academy of Science
Shentao Li: Capital Medical University
Huapeng Li: PackGene Biotech
Lan Qin: DIAN Diagnostics
Mingxu Hu: Tsinghua University
Zhengjia Yuan: High School Attached to Capital Normal University
Zipei Rao: No. 4 High School
Wei Ding: Capital Medical University
Zihe Rao: Tsinghua University
Zhiyong Lou: Tsinghua University

Nature Communications, 2019, vol. 10, issue 1, 1-11

Abstract: Abstract Adeno-associated virus (AAV) receptor (AAVR) is an essential receptor for the entry of multiple AAV serotypes with divergent rules; however, the mechanism remains unclear. Here, we determine the structures of the AAV1-AAVR and AAV5-AAVR complexes, revealing the molecular details by which PKD1 recognizes AAV5 and PKD2 is solely engaged with AAV1. PKD2 lies on the plateau region of the AAV1 capsid. However, the AAV5-AAVR interface is strikingly different, in which PKD1 is bound at the opposite side of the spike of the AAV5 capsid than the PKD2-interacting region of AAV1. Residues in strands F/G and the CD loop of PKD1 interact directly with AAV5, whereas residues in strands B/C/E and the BC loop of PKD2 make contact with AAV1. These findings further the understanding of the distinct mechanisms by which AAVR recognizes various AAV serotypes and provide an example of a single receptor engaging multiple viral serotypes with divergent rules.

Date: 2019
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DOI: 10.1038/s41467-019-11668-x

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