1. Volume 18, Issue 6, Pages 705-713 (December 2015)
Molecular Basis for Antibody-Mediated Neutralization of New World Hemorrhagic Fever Mammarenaviruses 
Selma Mahmutovic, Lars Clark, Silvana C. Levis, Ana M. Briggiler, Delia A. Enria, Stephen C. Harrison, Jonathan Abraham 
Cell Host & Microbe 
Volume 18, Issue 6, Pages (December 2015)
DOI: /j.chom
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2. Cell Host & Microbe 2015 18, 705-713DOI: (10.1016/j.chom.2015.11.005)
Copyright © 2015 Elsevier Inc. Terms and Conditions

3. Figure 1 Structure of a JUNV GP1-Neutralizing Antibody Complex
Ribbon diagram of JUNV GP1 (pink) bound to the GD01 Fab (heavy chain in cyan, light chain in dark blue). VH, VL, CH1, and CL denote the antibody variable heavy, variable light, constant heavy 1, and constant light chain domains, respectively. The antibody CDR loops (CDR L1, CDR L3, CDR H1, CDR H2, and CDR H3) that contact GP1 are labeled. GP1 glycans are shown as sticks. GP1 disulfides are shown in yellow.
Cell Host & Microbe  , DOI: ( /j.chom )
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4. Figure 2 Details of JUNV GP1-GD01 Interface
The GD01 variable heavy (VH) and variable light (VL) interacting segments are shown along with JUNV GP1 in ribbon diagram with a semi-transparent surface representation. The color scheme is as in Figure 1. Top left: CDR H3 includes a cluster of three tyrosines that fit into a shallow groove on the concave face of GP1. Bottom left: CDRs H1 and H2 form a network of polar contacts with GP1 loop 7 and the C-terminal end of loop 3. Top right: CDR L1 contacts the conserved GP1 Asn178 glycan. Bottom right: CDR L3 provides additional contacts to GP1 loop 3. The asterisk indicates a potential glycan for which we could not observe density.
Cell Host & Microbe  , DOI: ( /j.chom )
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5. Figure 3 Overlap of GP1 Receptor and GD01 Footprints
(A) Left panel: overlay of ribbon diagrams of JUNV GP1 (pink) and MACV GP1 (gray, from PDB: 3KAS). N-linked glycans are shown as sticks (gray for MACV, green for JUNV), and disulfides are shown in yellow. Right panel: Superposition of JUNV GP1 onto the MACV GP1:TfR1 structure (PDB: 3KAS). MACV GP1 is omitted for clarity.
(B) Left panel: surface representation of JUNV GP1 (pink) with the antibody VH and VL chain footprints colored in light and dark blue, respectively. An overlapping contact is shown in gray. Right panel: surface representation of JUNV GP1 with predicted TfR1 footprint shown in green.
(C) Left panel: GD01 CDRs L1 and L3 and CDRs H1, H2, and H3 form two ridges (shown in red) that the antibody presents to GP1. Tyr98 from the antibody heavy chain is shown as sticks. Right panel: TfR1 also presents two ridges to GP1 (shown in red) formed by the helix αII-2, the βII-2 strand, and loop βII-6-βII-7a in its apical domain. Tyr211 in the βII-2 strand of the receptor is shown as sticks.
Cell Host & Microbe  , DOI: ( /j.chom )
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6. Figure 4 The GP1 Tyr211-TfR1 Pocket as an Antibody Target
(A) Left panel: ribbon diagram of JUNV GP1 with GD01 CDR H3 residues 97–100a shown as sticks. Residues labeled with an asterisk are mutated in the JUNV GP1mut construct. The refined 2Fo-Fc electron density at 1 σ for antibody segment is shown. Right panel: ribbon diagram of MACV GP1 with TfR1 βII-2 strand residues 209–212 shown as sticks (from PDB: 3KAS). The refined 2Fo-Fc electron density at 1 σ for receptor segment is shown.
(B) ELISA of AHF survivor IgG binding to plates coated with JUNV GP1 or JUNV GP1mut. LUJV GP1 coated wells were included as a control. The pre-determined neutralization titer of each survivor is shown between parentheses. Error bars indicate SD.
(C) Competition ELISA: GD01 or 17b competitor IgG was added at increasing concentrations to plates coated with JUNV GP1, and the indicated AHF survivor IgG were added at fixed concentrations. Survivor IgG that bound to the plate was detected using a secondary anti-human HRP-conjugated antibody. Error bars indicate SD.
Cell Host & Microbe  , DOI: ( /j.chom )
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