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. 2022 Nov 25;10:1053139. doi: 10.3389/fcell.2022.1053139

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Copyright © 2022 Turner and Mathias.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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For infection in fibroblasts, the glycoprotein trimer consisting of gH, gL and gO binds to PDGFRα. Fusion between the envelope and cell membrane is mediated by gB and the tegumented nucleocapsid is released into the cytoplasm. For infection of epithelial, endothelial, myeloid, and likely many other cell types, the glycoprotein pentamer consisting of gH, gL, UL128, UL130 and UL131A binds to either OR14I1 or NRP2 on the cell surface and induces endocytosis of the virion. Pentamer mediated entry is dependent on acidification of the endosome as well as gO. The fusion step is mediated by gB to release the tegumented capsid into the cytoplasm, and tegument proteins dissociate and begin to reprogram the host cell. The capsid traffics to the nucleus for genome deposition. PDGFRα, platelet derived growth factor receptor alpha; NRP2, neuropilin; gB, envelope glycoprotein B.