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| Title | The prefusion structure of the HERV-K (HML-2) Env spike complex. |
|---|---|
| Journal, issue, pages | Proc Natl Acad Sci U S A, Vol. 122, Issue 28, Page e2505505122, Year 2025 |
| Publish date | Jul 15, 2025 |
 Authors | Ron Shaked / Michael Katz / Hadas Cohen-Dvashi / Ron Diskin /  |
| PubMed Abstract | The human endogenous retrovirus K (HERV-K) is a retrovirus that got assimilated into the human genome in ancient times and has been inherited in our germline ever since. It enters cells using a class- ...The human endogenous retrovirus K (HERV-K) is a retrovirus that got assimilated into the human genome in ancient times and has been inherited in our germline ever since. It enters cells using a class-I spike protein (Env) that mediates receptor recognition and membrane fusion. On top of having a biological role during development, HERV-K is activated in amyotrophic lateral sclerosis, various cancers, and other pathological conditions. Antibodies that target the HERV-K spike complex have therapeutic value, flagging the spike as a novel drug target. Here, we use cryo-EM to determine the trimeric structure of the HERV-K spike. The spike presents a distinct structure, which substantially differs from other class-I fusogens. Nevertheless, some general architectural features suggest a common origin with other retroviruses. The ability to structurally characterize the HERV-K spike may facilitate the development of antibody-based therapies. |
 External links | Proc Natl Acad Sci U S A / PubMed:40632556 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 2.13 Å |
| Structure data | EMDB-49572, PDB-9nnd: |
| Chemicals |  ChemComp-NAG:  ChemComp-HOH: |
| Source |
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 Keywords | VIRAL PROTEIN / HERV-K Endogenous retrovirus K Spike protein Viral glycoprotein / HML-2 |
homo sapiens (human)
