Vaccine-elicited receptor-binding site antibodies neutralize two New World hemorrhagic fever arenaviruses
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抄録
While five arenaviruses cause human hemorrhagic fevers in the Western Hemisphere, only Junin virus (JUNV) has a vaccine. The GP1 subunit of their envelope glycoprotein binds transferrin receptor 1 (TfR1) using a surface that substantially varies in sequence among the viruses. As such, receptor-mimicking antibodies described to date are type-specific and lack the usual breadth associated with this mode of neutralization. Here we isolate, from the blood of a recipient of the live attenuated JUNV vaccine, two antibodies that cross-neutralize Machupo virus with varying efficiency. Structures of GP1–Fab complexes explain the basis for efficient cross-neutralization, which involves avoiding receptor mimicry and targeting a conserved epitope within the receptor-binding site (RBS). The viral RBS, despite its extensive sequence diversity, is therefore a target for cross-reactive antibodies with activity against New World arenaviruses of public health concern.
収録刊行物
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- Nature Communications
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Nature Communications 9 1884-, 2018-05-14
Springer Nature
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詳細情報 詳細情報について
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- CRID
- 1050282812779571328
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- NII論文ID
- 120006535081
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- NII書誌ID
- AA12645905
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- ISSN
- 20411723
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- 本文言語コード
- en
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- 資料種別
- journal article
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- データソース種別
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- IRDB
- CiNii Articles