Vaccine-elicited receptor-binding site antibodies neutralize two New World hemorrhagic fever arenaviruses

Clark, Lars E.; Mahmutovic, Selma; Raymond, Donald D.; Dilanyan, Taleen; Koma, Takaaki; Manning, John T.; Shankar, Sundaresh; Levis, Silvana C.; Briggiler, Ana M.; Enria, Delia A.; Wucherpfennig, Kai W.; Paessler, Slobodan; Abraham, Jonathan

doi:10.1038/s41467-018-04271-z

Title: Vaccine-elicited receptor-binding site antibodies neutralize two New World hemorrhagic fever arenaviruses

Journal Article · Mon May 14 00:00:00 EDT 2018 · Nature Communications

DOI:https://doi.org/10.1038/s41467-018-04271-z· OSTI ID:1440602

Clark, Lars E. ^[1]; Mahmutovic, Selma ^[1]; Raymond, Donald D. ^[1]; Dilanyan, Taleen ^[1]; Koma, Takaaki ^[2]; Manning, John T. ^[2]; Shankar, Sundaresh ^[1]; Levis, Silvana C. ^[3]; Briggiler, Ana M. ^[3]; Enria, Delia A. ^[3]; Wucherpfennig, Kai W. ^[4]; Paessler, Slobodan ^[2];

^[5]

Harvard Medical School, Boston, MA (United States)
Univ. of Texas Medical Branch, Galveston, TX (United States)
Inst. Nacional de Enfermedades Virales Humanas “Dr. Julio I. Maiztegui”, Buenos Aires (Argentina)
Harvard Medical School, Boston, MA (United States); Dana-Farber Cancer Inst., Boston, MA (United States)
Harvard Medical School, Boston, MA (United States); Brigham and Women's Hospital, Boston, MA (United States)

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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Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States)

Sponsoring Organization:: National Inst. of Health; NIAID

Grant/Contract Number:: AI109740

OSTI ID:: 1440602

Journal Information:: Nature Communications, Vol. 9, Issue 1; ISSN 2041-1723

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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Cited by: 27 works

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