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

Lars E. Clark, Selma Mahmutovic, Donald D. Raymond, Taleen Dilanyan, Takaaki Koma, John T. Manning, Sundaresh Shankar, Silvana C. Levis, Ana M. Briggiler, Delia A. Enria, Kai W. Wucherpfennig, Slobodan Paessler and Jonathan Abraham ()
Additional contact information
Lars E. Clark: Harvard Medical School
Selma Mahmutovic: Harvard Medical School
Donald D. Raymond: Harvard Medical School
Taleen Dilanyan: Harvard Medical School
Takaaki Koma: University of Texas Medical Branch at Galveston
John T. Manning: University of Texas Medical Branch at Galveston
Sundaresh Shankar: Harvard Medical School
Silvana C. Levis: Instituto Nacional de Enfermedades Virales Humanas “Dr. Julio I. Maiztegui”, Monteagudo 251 Pergamino
Ana M. Briggiler: Instituto Nacional de Enfermedades Virales Humanas “Dr. Julio I. Maiztegui”, Monteagudo 251 Pergamino
Delia A. Enria: Instituto Nacional de Enfermedades Virales Humanas “Dr. Julio I. Maiztegui”, Monteagudo 251 Pergamino
Kai W. Wucherpfennig: Harvard Medical School
Slobodan Paessler: University of Texas Medical Branch at Galveston
Jonathan Abraham: Harvard Medical School

Nature Communications, 2018, vol. 9, issue 1, 1-12

Abstract: Abstract 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.

Date: 2018
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-018-04271-z Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-04271-z

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-018-04271-z

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().