Figure 4: Diversity of post-REG vaccination antibody response against different antigenic sites within RSV G and correlation with nasal and lung viral loads following RSV challenge. | Scientific Reports

Figure 4: Diversity of post-REG vaccination antibody response against different antigenic sites within RSV G and correlation with nasal and lung viral loads following RSV challenge.

From: Preclinical evaluation of bacterially produced RSV-G protein vaccine: Strong protection against RSV challenge in cotton rat model

Figure 4

All individual post-REG vaccination cotton rat sera (groups C and D) were tested for total antibody binding to the biotinylated peptides representing different antigenic sites within the extracellular domain of RSV-G consisting of amino acids 66–90, 90–110, 129–152, 148–178, 169–207, 236–263 and 263–298 of the RSV G protein using real time SPR kinetics (A). Total antibody binding is represented as SPR resonance units. Statistical significance was tested with one-way ANOVA and Bonferroni multiple comparisons tests. ***p < 0.0001, **p < 0.001, *p < 0.05. (B,C) Relationship between the total antibody binding of each individual post- vaccination sera from immunized animals against different antigenic sites within the extracellular domain of RSV-G representing amino acids 66–90, 90–110, 129–152, 148–178, 169–207, 236–263 and 263–298 and either nasal viral loads (B) or lung viral loads (C) in cotton rats at 2 days post-challenge with RSV-A2 with Spearman’s correlations. Total antibody binding is represented as SPR resonance units and lung viral loads are represented as pfu per gram tissue weight.

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