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Article

Single Amino Acid Substitutions Surrounding the Icosahedral Fivefold Symmetry Axis Are Critical for Alternative Receptor Usage of Foot-and-Mouth Disease Virus

State Key Laboratory of Veterinary Etiological Biology, OIE/China National Foot-and-Mouth Disease Reference Laboratory, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou 730046, China
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Received: 1 September 2020 / Revised: 28 September 2020 / Accepted: 6 October 2020 / Published: 9 October 2020
(This article belongs to the Section Animal Viruses)
The integrins function as the primary receptor molecules for the pathogenic infection of foot-and-mouth disease virus (FMDV) in vivo, while the acquisition of a high affinity for heparan sulfate (HS) of some FMDV variants could be privileged to facilitate viral infection and expanded cell tropism in vitro. Here, we noted that a BHK-adapted Cathay topotype derivative (O/HN/CHA/93tc) but not its genetically engineered virus (rHN), was able to infect HS-positive CHO-K1 cells and mutant pgsD-677 cells. There were one or three residue changes in the capsid proteins of O/HN/CHA/93tc and rHN, as compared with that of their tissue-originated isolate (O/HN/CHA/93wt). The phenotypic properties of a set of site-directed mutants of rHN revealed that E83K of VP1 surrounding the fivefold symmetry axis was necessary for the integrin-independent infection of O/HN/CHA/93tc. L80 in VP2 was essential for the occurrence of E83K in VP1 during the adaptation of O/HN/CHA/93wt to BHK-21 cells. L80M in VP2 and D138G in VP1 of rHN was deleterious, which could be compensated by K83R of VP1 for restoring an efficient infection of integrin-negative CHO cell lines. These might have important implications for understanding the molecular and evolutionary mechanisms of the recognition and binding of FMDV with alternative cellular receptors. View Full-Text
Keywords: foot-and-mouth disease virus; alternative cellular receptors; site-directed mutations; phenotypic properties; integrin-independent endocytic pathway foot-and-mouth disease virus; alternative cellular receptors; site-directed mutations; phenotypic properties; integrin-independent endocytic pathway
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MDPI and ACS Style

Gong, X.-H.; Bai, X.-W.; Li, P.-H.; Bao, H.-F.; Zhang, M.; Chen, Y.-L.; Sun, P.; Yuan, H.; Huang, L.; Ma, X.-Q.; Fu, Y.-F.; Cao, Y.-M.; Li, K.; Zhang, J.; Li, Z.-Y.; Li, D.; Lu, Z.-J.; Liu, Z.-X. Single Amino Acid Substitutions Surrounding the Icosahedral Fivefold Symmetry Axis Are Critical for Alternative Receptor Usage of Foot-and-Mouth Disease Virus. Viruses 2020, 12, 1147. https://0-doi-org.brum.beds.ac.uk/10.3390/v12101147

AMA Style

Gong X-H, Bai X-W, Li P-H, Bao H-F, Zhang M, Chen Y-L, Sun P, Yuan H, Huang L, Ma X-Q, Fu Y-F, Cao Y-M, Li K, Zhang J, Li Z-Y, Li D, Lu Z-J, Liu Z-X. Single Amino Acid Substitutions Surrounding the Icosahedral Fivefold Symmetry Axis Are Critical for Alternative Receptor Usage of Foot-and-Mouth Disease Virus. Viruses. 2020; 12(10):1147. https://0-doi-org.brum.beds.ac.uk/10.3390/v12101147

Chicago/Turabian Style

Gong, Xiao-Hua, Xing-Wen Bai, Ping-Hua Li, Hui-Fang Bao, Meng Zhang, Ying-Li Chen, Pu Sun, Hong Yuan, Lei Huang, Xue-Qing Ma, Yuan-Fang Fu, Yi-Mei Cao, Kun Li, Jing Zhang, Zhi-Yong Li, Dong Li, Zeng-Jun Lu, and Zai-Xin Liu. 2020. "Single Amino Acid Substitutions Surrounding the Icosahedral Fivefold Symmetry Axis Are Critical for Alternative Receptor Usage of Foot-and-Mouth Disease Virus" Viruses 12, no. 10: 1147. https://0-doi-org.brum.beds.ac.uk/10.3390/v12101147

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