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Miguel Hernandez Gonzalez

@miguel-virus-cells.bsky.social
33 followers 20 following 1 posts

Cell Biology. Membranes. Viruses. Cryo-ET.

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Reposted by Miguel Hernandez Gonzalez
Jeff Lengyel & TEM Team at Thermo Fisher Scientific @jefflengyeltemteam.bsky.social · 16/09/2026
Our team is highlighting this publication from @drmichaelway.bsky.social and team @crick.ac.uk - beautiful #cryoET subtomogram averaging looking at the poxvirus portal complex with Krios Cryo-TEM. Full paper: ter.li/gaqwi4gi
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Reposted by Miguel Hernandez Gonzalez
Nature @nature.com · 04/08/2026
Nature research paper: In situ structure of the poxvirus portal complex go.nature.com/4fD69xR
go.nature.com
In situ structure of the poxvirus portal complex - Nature
Cryo-electron tomography uncovers the structure of a conserved hexameric ‘portal complex’ that spans the core wall in vaccinia virus, and shows how it is associated with viral functions such as assembly, mRNA release and genome uncoating.
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Reposted by Miguel Hernandez Gonzalez
Michael Way @drmichaelway.bsky.social · 30/07/2026
How do poxviruses initiate infection after getting into the cytoplasm? With Tom Calcraft, @miguel-virus-cells.bsky.social & Peter Rosenthal, @crick.ac.uk we solved the structure of the vaccinia virus portal that mediates viral assembly and early mRNA and subsequent genome release. rdcu.be/fwGTn
rdcu.be
In situ structure of the poxvirus portal complex
Nature - Cryo-electron tomography uncovers the structure of a conserved hexameric ‘portal complex’ that spans the core wall in vaccinia virus, and shows how it is associated with viral...
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Miguel Hernandez Gonzalez @miguel-virus-cells.bsky.social · 29/07/2026
Great to see this finally published! We describe channels at the poxvirus core wall involved in nucleic acid release. www.nature.com/articles/s41...
nature.com
In situ structure of the poxvirus portal complex - Nature
Cryo-electron tomography uncovers the structure of a conserved hexameric ‘portal complex’ that spans the core wall in vaccinia virus, and shows how it is associated with viral functions such as a...
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Reposted by Miguel Hernandez Gonzalez
The Francis Crick Institute @crick.ac.uk · 29/07/2026
Scientists at the Crick have identified three crucial proteins that make up the ‘portal complex’ in the vaccinia poxvirus. The finding could lead to new ways of treating other poxviruses like mpox which have similar portal complexes. bit.ly/45vMhbi
bit.ly
Tuning into the channel helping poxviruses replicate
Uncovering the structure of the poxvirus ‘portal complex’, a channel used by the virus to release its genetic material into infected cells, could help develop new antiviral treatments.
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Reposted by Miguel Hernandez Gonzalez
Michael Way @drmichaelway.bsky.social · 20/08/2025
💥 Another Cryo-ET study from the Way lab by ‪@miguel-virus-cells.bsky.social‬ in collaboration with Rosenthal lab @crick.ac.uk‬ examining Vaccinia virus egress 😀👇 www.biorxiv.org/content/10.1...
biorxiv.org
In situ cryo-electron tomography of vaccinia virus exit from infected cells
Poxvirus-infected cells release newly assembled virions via Golgi-mediated envelopment and subsequent exocytosis at the plasma membrane, prior to cell lysis. Here, we used cryo-electron tomography and...
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Reposted by Miguel Hernandez Gonzalez
Ilaria Dalla Rosa @ilariadallarosa.bsky.social · 26/06/2025
Thrilled to share that my first paper in the lab of @drmichaelway.bsky.social is now published in @narjournal.bsky.social! We showed that Topoisomerase 2α and 2β have opposing roles in vaccinia virus replication, one promoting and the other restricting it 👇🏼 doi.org/10.1093/nar/...
doi.org
Nonredundant roles of topoisomerase 2α and 2β in the cytosolic replication of vaccinia virus
Abstract. Vaccinia virus is a large enveloped DNA virus, which, like all poxviruses, replicates in the cytoplasm of infected cells. Vaccinia was historical
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