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Enveloped viruses can have severe consequences for human health, causing various diseases such as acquired immunodeficiency syndrome (AIDS), seasonal influenza, COVID-19, and Ebola virus disease. The complex arrangement and pleomorphic architecture of many enveloped viruses pose a challenge for the more widely used structural biology techniques, such as X-ray crystallography. Cryo-electron tomography (cryo-ET), however, is a particularly well-suited tool for overcoming the limitations associated with visualizing the irregular shapes and morphology enveloped viruses possess at macromolecular resolution. The purpose of this review is to explore the latest structural insights that cryo-ET has revealed about enveloped viruses, with particular attention given to their architectures, mechanisms of entry, replication, assembly, maturation and egress during infection. Cryo-ET is unique in its ability to visualize cellular landscapes at 3\u20135 nanometer resolution. Therefore, it is the most suited technique to study asymmetric elements and structural rearrangements of enveloped viruses during infection in their native cellular context.<\/jats:p>","DOI":"10.1042\/bst20210433","type":"journal-article","created":{"date-parts":[[2022,1,25]],"date-time":"2022-01-25T14:55:46Z","timestamp":1643122546000},"page":"95-105","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":7,"title":["Three-dimensional insights into human enveloped viruses <i>in vitro<\/i> and <i>in situ<\/i>"],"prefix":"10.1042","volume":"50","author":[{"given":"Naveen","family":"Vankadari","sequence":"first","affiliation":[{"name":"Monash Biomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Melbourne, VIC, Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Doulin C.","family":"Shepherd","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Pharmacology, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Melbourne, VIC, Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Stephen D.","family":"Carter","sequence":"additional","affiliation":[{"name":"Centre for Virus Research, Medical Research Council-University of Glasgow Centre for Virus Research, Glasgow, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2227-0330","authenticated-orcid":false,"given":"Debnath","family":"Ghosal","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Pharmacology, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Melbourne, VIC, Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","published-online":{"date-parts":[[2022,1,25]]},"reference":[{"key":"2022030117174244000_BST-2021-0433CC1","doi-asserted-by":"publisher","first-page":"2089","DOI":"10.1016\/j.febslet.2007.03.060","article-title":"More than one door: budding of enveloped viruses through cellular membranes","volume":"581","year":"2007","journal-title":"FEBS Lett."},{"key":"2022030117174244000_BST-2021-0433CC2","doi-asserted-by":"publisher","first-page":"519","DOI":"10.1016\/B978-0-12-814515-9.00023-0","article-title":"Virus budding","year":"2021","journal-title":"Encyclopedia Virol."},{"key":"2022030117174244000_BST-2021-0433CC3","doi-asserted-by":"publisher","first-page":"906","DOI":"10.1038\/nsmb.3291","article-title":"Natively glycosylated HIV-1 Env structure reveals new mode for antibody recognition of the CD4-binding site","volume":"23","year":"2016","journal-title":"Nat. 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