Viral Entry and Membrane Fusion

A special issue of Viruses (ISSN 1999-4915). This special issue belongs to the section "General Virology".

Deadline for manuscript submissions: 16 February 2027 | Viewed by 893

Editor


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Guest Editor
Núcleo Multidisciplinar de Pesquisa em Biologia—NUMPEX-BIO, Campus Duque de Caxias Professor Geraldo Cidade, Universidade Federal do Rio de Janeiro, Rio de Janeiro 25240-005, Brazil
Interests: viral entry; membrane fusion; virus–host interactions; receptor binding and endocytosis; fusion proteins; ultrastructural and imaging approaches; antiviral and virucidal strategies; emerging and re-emerging viruses

Special Issue Information

Dear Colleagues,

Viral entry and membrane fusion are critical steps in the viral life cycle and key determinants of host range, tissue tropism, and pathogenicity. These processes involve highly coordinated interactions between viral surface proteins and host cell receptors, often coupled to endocytic pathways, membrane remodeling, and conformational changes triggered by pH or proteolytic activation. Advances in structural biology, single-particle imaging, molecular virology, and biophysics have significantly expanded our understanding of viral fusion mechanisms across enveloped and non-enveloped viruses. This Special Issue aims to highlight recent discoveries, innovative methodologies, and therapeutic strategies targeting viral entry and membrane fusion, fostering integrative insights into virus–host interactions and antiviral intervention.

This Special Issue will highlight recent advances in the molecular, cellular, and structural understanding of viral entry and membrane fusion, including receptor interactions, endocytic pathways, and fusion protein activation. It will also cover innovative methodologies and antiviral strategies targeting early stages of infection across diverse viral families.

Dr. Fabiana Carneiro
Guest Editor

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Keywords

  • viral entry
  • membrane fusion
  • virus–host interactions
  • endocytosis
  • antiviral strategies

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Published Papers (1 paper)

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Research

16 pages, 8781 KB  
Article
Specific Determinants of the Transmembrane Region of the Andes Virus Gc Glycoprotein Drive the Transition from Membrane Hemifusion to Pore Formation
by Chantal L. Márquez, Fernando Villalón-Letelier, Gianina Arata-Salas and Nicole D. Tischler
Viruses 2026, 18(6), 633; https://doi.org/10.3390/v18060633 - 31 May 2026
Viewed by 575
Abstract
Andes virus (ANDV), a highly pathogenic orthohantavirus, enters host cells through low pH–triggered membrane fusion mediated by the Gc glycoprotein, a class II fusion protein containing a single C-terminal transmembrane domain (TMD). While the ectodomain has been extensively characterized, the role of the [...] Read more.
Andes virus (ANDV), a highly pathogenic orthohantavirus, enters host cells through low pH–triggered membrane fusion mediated by the Gc glycoprotein, a class II fusion protein containing a single C-terminal transmembrane domain (TMD). While the ectodomain has been extensively characterized, the role of the TMD in late-stage fusion remains unclear. Here, we investigated the minimal functional length and sequence requirements of the ANDV Gc TMD using site-directed mutagenesis. C-terminal deletion mutants and serine-to-alanine substitutions were evaluated for protein expression, virus-like particle production, cell–cell fusion, pseudotyped vector entry, and hemifusion activity. Deletion of the Gc cytoplasmic tail (CT) or a single C-terminal TMD residue was tolerated, whereas deletion of two or more residues impaired particle production and fusion, indicating that at least 21 of the 22 TMD residues are required for efficient membrane fusion and viral entry. Hemifusion assays showed that deletion of two or three residues, or substitution of the strictly conserved S1121, allowed lipid mixing but blocked progression to full fusion, while deletion of four residues also abolished hemifusion. In contrast, mutation of the less conserved S1126 had minimal effect. These results identify a precise TMD length and a conserved polar TMD residue as critical determinants of fusion pore formation in ANDV. Full article
(This article belongs to the Special Issue Viral Entry and Membrane Fusion)
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