Figure 1. Recombinant mouse immunoglobulin G2a (IgG2a) monoclonal antibody rMAb 3F6 neutralizes staphylococcal protein A (SpA), promotes opsonophagocytic.

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Figure 1. Recombinant mouse immunoglobulin G2a (IgG2a) monoclonal antibody rMAb 3F6 neutralizes staphylococcal protein A (SpA), promotes opsonophagocytic killing of Staphylococcus aureus, and protects mice against S. aureus bloodstream infection. A, Dissociation constants (K<sub>d</sub>) were derived for rMAb 3F6 and mouse hybridoma monoclonal antibody (hMAb) 3F6 binding to SpA<sub>KKAA</sub>. Antibodies (0.15 mg/mL) were serially diluted across enzyme-linked immunosorbent assay plates coated with SpA<sub>KKAA</sub> (1 μg/mL) to calculate the dissociation constants using GraphPad Prism software. B, rMAb 3F6 and hMAb 3F6 prevent SpA binding to human IgG. Values were normalized to SpA interaction with human IgG in the absence of antibody (n = 3). C, rMAb 3F6 and hMAb 3F6 promote opsonophagocytic killing of methicillin-resistant S. aureus (MRSA) isolate MW2 in mouse and human blood (n = 3). D, Intraperitoneal administration of rMAb 3F6 and hMAb 3F6 antibodies (5 mg/kg body weight) into mice reduces replication of intravenously injected MRSA in the renal tissues of BALB/c mice. Error bars ± standard error of the means were calculated from multiple independent repetitions of the experiments. *P < .05. Abbreviations: A<sub>450</sub>, absorbance at 450 nm; CD, cytochalasin D; CFU, colony-forming units; hMAb, mouse hybridoma monoclonal antibody; IgG2a, immunoglobulin G2a; ns, not significant; PBS, phosphate-buffered saline; rMAb, mouse recombinant monoclonal antibody; SpA, staphylococcal protein A. From: Staphylococcus aureus Decolonization of Mice With Monoclonal Antibody Neutralizing Protein A J Infect Dis. Published online December 15, 2018. doi:10.1093/infdis/jiy597 J Infect Dis | © The Author(s) 2018. Published by Oxford University Press for the Infectious Diseases Society of America. All rights reserved. For permissions, e-mail: journals.permissions@oup.com.This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model)

Figure 2. Administration of mouse recombinant monoclonal antibody (rMAb) 3F6 promotes Staphylococcus aureus decolonization in mice. A, Enzyme-linked immunosorbent assay examining rMAb 3F6 and mouse hybridoma monoclonal antibody (hMAb) 3F6 affinity for the mouse neonatal Fc receptor. Dissociation constants (K<sub>d</sub>) were calculated using GraphPad Prism software. B, Plasma concentration-time profile of rMAb 3F6 following intraperitoneal administration into C57BL/6 mice (n = 5). C, Intraperitoneal administration of rMAb 3F6 prior to nasal inoculation with S. aureus WU1 promotes progressive decolonization of staphylococci from the nasopharynx of C57BL/6 mice (n = 10). The median and standard deviation for each group of animals on a given day are indicated by the horizontal lines and error bars. D, Administration of rMAb 3F6 prior to colonization promotes enhanced antistaphylococcal serum immunoglobulin G responses. Sera of animals shown in (C) were tested for antibodies against the indicated S. aureus antigens. Error bars ± standard error of the mean were calculated from multiple independent repetitions of the experiments. *P < .05. Abbreviations: A<sub>450</sub>, absorbance at 450 nm; CFU, colony-forming units; hMAb, mouse hybridoma monoclonal antibody; IgG, immunoglobulin G; IgG2a, immunoglobulin G2a; mFcRn, mouse neonatal Fc receptor; PBS, phosphate-buffered saline; rMAb, mouse recombinant monoclonal antibody; SpA, staphylococcal protein A. From: Staphylococcus aureus Decolonization of Mice With Monoclonal Antibody Neutralizing Protein A J Infect Dis. Published online December 15, 2018. doi:10.1093/infdis/jiy597 J Infect Dis | © The Author(s) 2018. Published by Oxford University Press for the Infectious Diseases Society of America. All rights reserved. For permissions, e-mail: journals.permissions@oup.com.This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model)