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Structure paper

TitleReceptor-recognition and antiviral mechanisms of retrovirus-derived human proteins.
Journal, issue, pagesNat Struct Mol Biol, Vol. 31, Issue 9, Page 1368-1376, Year 2024
Publish dateApr 26, 2024
AuthorsShashank Khare / Miryam I Villalba / Juan C Canul-Tec / Arantza Balsebre Cajiao / Anand Kumar / Marija Backovic / Felix A Rey / Els Pardon / Jan Steyaert / Camilo Perez / Nicolas Reyes /
PubMed AbstractHuman 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 ...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.
External linksNat Struct Mol Biol / PubMed:38671230
MethodsEM (single particle)
Resolution2.31 - 3.5 Å
Structure data

17189

8oud

EMDB-17189, PDB-8oud:
Structure of the human neutral amino acid transporter ASCT2 in complex with nanobody 469
Method: EM (single particle) / Resolution: 2.31 Å

17192

8ouh

EMDB-17192, PDB-8ouh:
Complex of human ASCT2 with Syncytin-1
Method: EM (single particle) / Resolution: 2.62 Å

17193

8oui

EMDB-17193, PDB-8oui:
Complex of ASCT2 with Suppressyn
Method: EM (single particle) / Resolution: 3.39 Å

17194

8ouj

EMDB-17194, PDB-8ouj:
Heterotrimeric Complex of Human ASCT2 with Syncytin-1
Method: EM (single particle) / Resolution: 3.5 Å

Chemicals

ChemComp-NA:
Unknown entry

ChemComp-ALA:
ALANINE

ChemComp-Y01:
CHOLESTEROL HEMISUCCINATE

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • lama glama (llama)
KeywordsMEMBRANE PROTEIN / Neutral aminoacid transmembrane transporter activity / ASCT2 / Complex / Nanobody / PROTEIN TRANSPORT / Small neutral amino acid transporter / Syncytin-1 / Receptor binding domain / Small neural amino acid transporter / Suppressyn

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