期刊
NATURE COMMUNICATIONS
卷 9, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-018-04271-z
关键词
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资金
- National Institutes of Health [T32 AI007061]
- Office of the Director, National Institutes of Health, of the National Institutes of Health [DP5OD023084]
- National Institutes of Health Centers of Excellence for Translational Research (CETR) [AI109740]
- Harvard Medical School Office for Diversity Inclusion and Community Partnership (DICP) Faculty Fellowship
- Brigham and Women's Hospital Young Investigator in Medicine Award
- Burroughs Wellcome Fund Postdoctoral Enrichment Program Award
- Burroughs Wellcome Fund Career Award for Medical Scientists
- William Randolph Hearst Foundation
- Japan Society for the Promotion of Science (JSPS)
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.
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