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-Structure paper
タイトル | The prefusion structure of the HERV-K (HML-2) Env spike complex. |
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ジャーナル・号・ページ | Proc Natl Acad Sci U S A, Vol. 122, Issue 28, Page e2505505122, Year 2025 |
掲載日 | 2025年7月15日 |
![]() | Ron Shaked / Michael Katz / Hadas Cohen-Dvashi / Ron Diskin / ![]() |
PubMed 要旨 | 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. |
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手法 | EM (単粒子) |
解像度 | 2.13 Å |
構造データ | EMDB-49572, PDB-9nnd: |
化合物 | ![]() ChemComp-NAG: ![]() ChemComp-HOH: |
由来 |
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![]() | VIRAL PROTEIN / HERV-K Endogenous retrovirus K Spike protein Viral glycoprotein / HML-2 |