🚨 Preprint alter - bis 🚨 I am thrilled to share our last preprint where we identify and characterize a new coronavirus receptor! 🦠 This work was done in collaboration with the team of Félix Rey @virusfusion007 at the Institut Pasteur. A 🧶 below...

RT @SFV_France: Rafael Sanjuan, Professeur à l’Universitat València @UV_EG, est invité aux #JFV2025 et présentera son travail « Entrée de v…

@mpalomino_seg @UV_EG Thanks a lot Miguel! Hope everything's going well for you! 😃

@gonzamoratorio Thanks a lot Gonzalo! 😃

@SystemsVirology Thanks a lot Kei! 😁

Thanks @sathvikpal and Michael S. Diamond for this nice "News and Views" on our recent study in @NatureMicrobiol !

RT @Rafa_Sanjuan_: Reservad la fecha! El 20-21 de febrero tendrá lugar el III Congreso del Master en Virología de la Universitat de Valenci…

@JBuigues @Rafa_Sanjuan_ Thanks Jaime!! 🙏

@b_steve36b @siamosolocani We did not isolate the viruses. We examined their receptor usage using viral pseudotypes.

I'd like to warmly thank all the collaborators involved, especially in the labs of @Rafa_Sanjuan_ and @virusfusion007, in particular Ignacio Fernández (not on X), co-first author of the study! Hope you'll enjoy the read! 📚

This allowed us to identify critical residues at the interface. Morevover, this revealed that despite variations in RBD sequences and receptor usage , the structural elements involved in receptor recognition are conserved across embecoviruses.

Ignacio Fernández, from Félix Rey's lab, beautifully obtained the X-ray structure of DPEP1 in complex with the PHEV RBD.

DPEP1 was a PHEV-specific receptor and could not bind other betacoronavirus 1 spikes. This could be explained by large sequence variations between the RBD of PHEV and that of other members of the species, including BCoV or OC43.

Here, we show that contrary to other embecoviruses, the entry of PHEV does not require binding to sialic acid. In contrast, we identify dipeptidase 1 (DPEP1) as a functional PHEV receptor triggering PHEV spike-mediated fusion (entry and cell-cell fusion).

Therefore, sialic acid had long been considered as the only embecovirus receptor. However, the recent discovery that TMPRSS2 acts as the protein receptor of HKU1 revealed a more complex scenario. Whether other embecovirus dually depends on a protein and sialic acid is unknown.

The N-terminal domain (NTD) of the embecovirus spike harbors a conserved glycan-binding site that interacts with sialic acid in HKU1, OC43, BCoV, and PHEV and this interaction is necessary for HKU1, OC43 and BCoV entry.

The betacoronavirus 1 species is the main taxon of the Embecovirus subgenus (Betacoronavirus genus), which includes other relevant viruses such as the human common cold virus HKU1 🤒 and murine hepatitis virus (MHV) 🐁.

In this work, we focused on the betacoronavirus 1 species. It includes ten host-specific viruses such as the porcine hemagglutinating encephalomyelitis virus (PHEV) 🐖 and bovine coronavirus (BCoV) 🐄, but also the human seasonal cold virus OC43 🤒.