ArticleNature structural & molecular biology2024
Receptor-recognition and antiviral mechanisms of retrovirus-derived human proteins.
Article in Nature structural & molecular biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 15 citations in OpenAlex.
- Beyond Genetic Conservation: The Baton Pass Model of Essential Biological Functions.Biomolecules · 2026Review
- Amino acid and viral binding by the high-affinity Cationic Amino acid Transporter 1 (CAT1) from Mus musculus.Nature communications · 2026Article
- The double-positive cells in the tumor microenvironment.Journal of translational internal medicine · 2026Article
- Preparation of Plasma Membrane Vesicles, Lysosomes, Proteoliposomes and Alternative Sample Types for SSM-Based Electrophysiology.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Structural insights into cationic amino acid transport and viral receptor engagement by CAT1.Nature communications · 2025Article
- Variations in blood levels of the anti-fusogenic endogenous retroviral protein suppressyn are associated with fetal growth outcome in preeclampsia.Scientific reports · 2025Article
- Evolution of antiviral host defenses against a backdrop of endogenous retroelements.Science (New York, N.Y.) · 2025Review
- Genetic Diversity in theBiomolecules · 2025Article
- The prefusion structure of the HERV-K (HML-2) Env spike complex.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural basis of excitatory amino acid transporter 3 substrate recognition.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Receptor usage of Syncytin-1: ASCT2, but not ASCT1, is a functional receptor and effector of cell fusion in the human placenta.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Structural basis of the excitatory amino acid transporter 3 substrate recognition.bioRxiv : the preprint server for biology · 2024Article
- Human endogenous retroviruses and exogenous viral infections.Frontiers in cellular and infection microbiology · 2024Review
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human syncytin-1 and suppressyn are cellular proteins of retroviral origin involved in cell-cell fusion events to establish the maternal-fetal interface in the placenta. In cell culture, they restrict infections from members of the largest interference group of vertebrate retroviruses, and are regarded as host immunity factors expressed during development. At the core of the syncytin-1 and suppressyn functions are poorly understood mechanisms to recognize a common cellular receptor, the membrane transporter ASCT2. Here, we present cryo-electron microscopy structures of human ASCT2 in complexes with the receptor-binding domains of syncytin-1 and suppressyn. Despite their evolutionary divergence, the two placental proteins occupy similar positions in ASCT2, and are stabilized by the formation of a hybrid β-sheet or 'clamp' with the receptor. Structural predictions of the receptor-binding domains of extant retroviruses indicate overlapping binding interfaces and clamping sites with ASCT2, revealing a competition mechanism between the placental proteins and the retroviruses. Our work uncovers a common ASCT2 recognition mechanism by a large group of endogenous and disease-causing retroviruses, and provides high-resolution views on how placental human proteins exert morphological and immunological functions.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.