Table 1.
Characterization of human MAbs and Fabs for Venezuelan equine encephalitis virus (VEEV).
Figure 1.
Representative ELISA cross-reactivity patterns for Venezuelan equine encephalitis virus (VEEV) E2-specific human (h) Fabs and MAbs.
A. Anti-hE2a1 MAb. B. Anti-hE2a2 Fab. C. Anti-hE2b Fab. D. Anti-hE2c MAb. E. Anti-hE2d Fab. Four varieties of VEEV subtype 1, TC-83 (1AB, –•–), P676 (1C, –▪–), 3880 (1D, –▴–), and Mena II (1E, –○–); and five other subtypes, EVE (2, –♦–), MUC (3, –□–), PIX (4, –▵–), CAB (5, --○--), and AG80-663 (6, –◊–) were included in the panel of ELISA antigens.
Table 2.
Amino acid sequences of both heavy and light chain complementary determining region 3 of human MAbs and Fabs for Venezuelan equine encephalitis virus.
Figure 2.
Representative ELISA cross-reactivity patterns for Venezuelan equine encephalitis virus (VEEV) E1-specific human (h) Fabs.
A. Anti-hE1a. B. Anti-hE1b. C. Anti-hE1c. Four varieties of VEEV subtype 1, TC-83 (1AB, –•–), P676 (1C, –▪–), 3880 (1D, –▴–), and Mena II (1E, –○–); and five other subtypes, EVE (2, –♦–), MUC (3, –□–), PIX (4, –▵–), CAB (5, --○--), and AG80-663 (6, –◊–) were included in the panel of ELISA antigens.
Table 3.
ELISA-based competition of human Fabs with MAb F5 nIgG for binding to Venezuelan equine encephalitis virus TC-83.
Table 4.
Murine and human MAb competition with MAb-hydrogen peroxidase (HRP) conjugates binding to Venezuelan equine encephalitis virus TC-83.
Table 5.
Neutralization of five murine MAb neutralization-escape variants of Venezuelan equine encephalitis virus (VEEV) TC-83 by human MAb F5 nIgG.
Table 6.
Comparison of the neutralization activity of humanized murine MAb Hy4 IgG and fully human MAb F5 nIgG for parental Venezuelan equine encephalitis virus (VEEV) TC-83 and F5 nIgG neutralization-escape variant viruses vF5 nIgG-3 and vF5 nIgG-5.
Table 7.
Sequence comparisons between Venezuelan equine encephalitis virus TC-83 (VE/IC-92) and two F5 nIgG neutralization-escape variant viruses vF5 nIgG-3 and vF5 nIgG-5.
Figure 3.
A. A top view of the E2 density of one spike looking down the 3‐fold axis (shown as the large purple spot corresponding to three merged carbohydrate moieties at position 46). B. A side view of one E2 molecule with the approximate location of Venezuelan equine encephalitis virus (VEEV) E2 peptide 13 (amino acids 241–265) shown in black. A and B: The markers on the E2 glycoprotein that correspond to carbohydrate moieties at positions 46, 160, 196, 200, 216, 262, and 318 are shown in purple, red, blue, orange, green, pink, and light blue, respectively. Position 216 (green) was also identified with a cryoEM map of a Fab‐Ross River virus complex. Approximate locations of the VEEV murine MAb anti‐mE2c binding site and critical neutralization site are shown by a dotted circle; the proposed binding site of the VEEV human MAb anti‐hE2c is shown in cyan.