Publications by authors named "Ainhoa Moliner-Morro"

G3BP is the central node within stress-induced protein-RNA interaction networks known as stress granules (SGs). The SG-associated proteins Caprin-1 and USP10 bind mutually exclusively to the NTF2 domain of G3BP1, promoting and inhibiting SG formation, respectively. Herein, we present the crystal structure of G3BP1-NTF2 in complex with a Caprin-1-derived short linear motif (SLiM).

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Background: Licensed vaccines against SARS-CoV-2 effectively protect against severe disease, but display incomplete protection against virus transmission. Mucosal vaccines providing immune responses in the upper airways are one strategy to protect against transmission.

Methods: We administered Spike HexaPro trimer formulated in a cationic liposomal adjuvant as a parenteral (subcutaneous - s.

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Antibodies are natural antivirals generated by the vertebrate immune system in response to viral infection or vaccination. Unsurprisingly, they are also key molecules in the virologist's molecular toolbox. With new developments in methods for protein engineering, protein functionalization and application, smaller antibody-derived fragments are moving in focus.

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Article Synopsis
  • Antibodies targeting the SARS-CoV-2 spike protein have potential for treatment, but new variants can evade these defenses, highlighting the need for unique therapies.
  • A novel nanobody was isolated that binds to two receptor-binding domains (RBDs) from different spike trimers of SARS-CoV-2, effectively preventing the virus from attaching to human cells.
  • This nanobody demonstrates strong neutralization of multiple SARS-CoV-2 variants and shows promise as a therapeutic option in mouse models, presenting a new approach to fighting viral infections.
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Article Synopsis
  • Viral proteins use short peptide motifs to interact with host factors, but these interactions are often missed in large-scale studies.
  • A new approach to discover viral peptides covering 23 coronavirus strains revealed 269 peptide-based interactions, particularly highlighting a significant interaction between SARS-CoV-2's nucleocapsid protein and human G3BP1/2 proteins.
  • Disrupting this interaction with a peptide-based inhibitor reduced SARS-CoV-2 infection, indicating a potential avenue for developing specific antiviral therapies.
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Multivalent antibody constructs have a broad range of clinical and biotechnological applications. Nanobodies are especially useful as components for multivalent constructs as they allow increased valency while maintaining a small molecule size. We here describe a novel, rapid method for the generation of bi- and multivalent nanobody constructs with oriented assembly by Cu-free strain promoted azide-alkyne click chemistry (SPAAC).

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SARS-CoV-2 enters host cells through an interaction between the spike glycoprotein and the angiotensin converting enzyme 2 (ACE2) receptor. Directly preventing this interaction presents an attractive possibility for suppressing SARS-CoV-2 replication. Here, we report the isolation and characterization of an alpaca-derived single domain antibody fragment, Ty1, that specifically targets the receptor binding domain (RBD) of the SARS-CoV-2 spike, directly preventing ACE2 engagement.

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Infection by Chikungunya virus (CHIKV) of the Old World alphaviruses (family Togaviridae) in humans can cause arthritis and arthralgia. The virus encodes four non-structural proteins (nsP) (nsP1, nsp2, nsP3 and nsP4) that act as subunits of the virus replicase. These proteins also interact with numerous host proteins and some crucial interactions are mediated by the unstructured C-terminal hypervariable domain (HVD) of nsP3.

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