ArticleJournal of virology2010
Andes virus recognition of human and Syrian hamster beta3 integrins is determined by an L33P substitution in the PSI domain.
Article in Journal of virology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 49 citations in OpenAlex.
- Andes virus from the 2026Emerging microbes & infections · 2026Article
- Article
- Viruses Binding to Host Receptors Interacts with Autophagy.International journal of molecular sciences · 2023Review
- Binding of the Andes Virus Nucleocapsid Protein to RhoGDI Induces the Release and Activation of the Permeability Factor RhoA.Journal of virology · 2021Article
- Recent Advances in Bunyavirus Glycoprotein Research: Precursor Processing, Receptor Binding and Structure.Viruses · 2021Review
- Article
- Novel Pure αVβ3 Integrin Antagonists That Do Not Induce Receptor Extension, Prime the Receptor, or Enhance Angiogenesis at Low Concentrations.ACS pharmacology & translational science · 2019Article
- Unique Interferon Pathway Regulation by the Andes Virus Nucleocapsid Protein Is Conferred by Phosphorylation of Serine 386.Journal of virology · 2019Article
- A Single-Nucleotide Polymorphism of αViruses · 2019Article
- Hantavirus entry: Perspectives and recent advances.Advances in virus research · 2019Article
- Early Host Interactions That Drive the Dysregulated Response in Sepsis.Frontiers in immunology · 2019Review
- Two recombinant human monoclonal antibodies that protect against lethal Andes hantavirus infection in vivo.Science translational medicine · 2018Article
- Beyond the Matrix: The Many Non-ECM Ligands for Integrins.International journal of molecular sciences · 2018Review
- The Andes Virus Nucleocapsid Protein Directs Basal Endothelial Cell Permeability by Activating RhoA.mBio · 2016Article
- Early Bunyavirus-Host Cell Interactions.Viruses · 2016Review
- Endocytic Pathways Used by Andes Virus to Enter Primary Human Lung Endothelial Cells.PloS one · 2016Article
- Virus interactions with endothelial cell receptors: implications for viral pathogenesis.Current opinion in virology · 2014Review
- Review
- Hantavirus Gn and Gc envelope glycoproteins: key structural units for virus cell entry and virus assembly.Viruses · 2014Review
- Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Andes virus (ANDV) causes a fatal hantavirus pulmonary syndrome (HPS) in humans and Syrian hamsters. Human alpha(v)beta(3) integrins are receptors for several pathogenic hantaviruses, and the function of alpha(v)beta(3) integrins on endothelial cells suggests a role for alpha(v)beta(3) in hantavirus directed vascular permeability. We determined here that ANDV infection of human endothelial cells or Syrian hamster-derived BHK-21 cells was selectively inhibited by the high-affinity alpha(v)beta(3) integrin ligand vitronectin and by antibodies to alpha(v)beta(3) integrins. Further, antibodies to the beta(3) integrin PSI domain, as well as PSI domain polypeptides derived from human and Syrian hamster beta(3) subunits, but not murine or bovine beta(3), inhibited ANDV infection of both BHK-21 and human endothelial cells. These findings suggest that ANDV interacts with beta(3) subunits through PSI domain residues conserved in both Syrian hamster and human beta(3) integrins. Sequencing the Syrian hamster beta(3) integrin PSI domain revealed eight differences between Syrian hamster and human beta(3) integrins. Analysis of residues within the PSI domains of human, Syrian hamster, murine, and bovine beta(3) integrins identified unique proline substitutions at residues 32 and 33 of murine and bovine PSI domains that could determine ANDV recognition. Mutagenizing the human beta(3) PSI domain to contain the L33P substitution present in bovine beta(3) integrin abolished the ability of the PSI domain to inhibit ANDV infectivity. Conversely, mutagenizing either the bovine PSI domain, P33L, or the murine PSI domain, S32P, to the residue present human beta(3) permitted PSI mutants to inhibit ANDV infection. Similarly, CHO cells transfected with the full-length bovine beta(3) integrin containing the P33L mutation permitted infection by ANDV. These findings indicate that human and Syrian hamster alpha(v)beta(3) integrins are key receptors for ANDV and that specific residues within the beta(3) integrin PSI domain are required for ANDV infection. Since L33P is a naturally occurring human beta(3) polymorphism, these findings further suggest the importance of specific beta(3) integrin residues in hantavirus infection. These findings rationalize determining the role of beta(3) integrins in hantavirus pathogenesis in the Syrian hamster model.
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