Inhibition of Toxic Shock by Human Monoclonal Antibodies against Staphylococcal Enterotoxin B

Larkin, Eileen A.; Stiles, Bradley G.; Ulrich, Robert G.

doi:10.1371/journal.pone.0013253

Title: Inhibition of Toxic Shock by Human Monoclonal Antibodies against Staphylococcal Enterotoxin B

Journal Article · Mon Oct 11 00:00:00 EDT 2010 · PLoS ONE

DOI:https://doi.org/10.1371/journal.pone.0013253· OSTI ID:1627427

Larkin, Eileen A. ^[1]; Stiles, Bradley G. ^[2]; Ulrich, Robert G. ^[1]

Medical Research Institute of Infectious Diseases, Frederick, MD (United States); Hood College, Frederick, MD (United States)
Medical Research Institute of Infectious Diseases, Frederick, MD (United States); Wilson College, Chambersburg, PA (United States)

Staphylococcus aureus is implicated in many opportunistic bacterial infections around the world. Rising antibiotic resistance and few alternative methods of treatment are just two looming problems associated with clinical management of S. aureus. Among numerous virulence factors produced by S. aureus, staphylococcal enterotoxin (SE) B is a secreted protein that binds T-cell receptor and major histocompatibility complex class II, potentially causing toxic shock mediated by pathological activation of T cells. Recombinant monoclonal antibodies that target SEB and block receptor interactions can be of therapeutic value. The inhibitory and biophysical properties of ten human monoclonal antibodies, isolated from a recombinant library by panning against SEB vaccine (STEBVax), were examined as bivalent Fabs and native full-length IgG (Mab). The best performing Fabs had binding affinities equal to polyclonal IgG, low nanomolar IC50s against SEB in cell culture assays, and protected mice from SEB-induced toxic shock. The orthologous staphylococcal proteins, SEC1 and SEC2, as well as streptococcal pyrogenic exotoxin C were recognized by several Fabs. Four Fabs against SEB, with the lowest IC50s, were converted into native full-length Mabs. Although SEB-binding kinetics were identical between each Fab and respective Mab, a 250-fold greater inhibition of SEB-induced T-cell activation was observed with two Mabs. Results suggest that these human monoclonal antibodies possess high affinity, target specificity, and toxin neutralization qualities essential for any therapeutic agent.

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Research Organization:: Medical Research Institute of Infectious Diseases, Frederick, MD (United States); Hood College, Frederick, MD (United States)

Sponsoring Organization:: USDOE Office of Science (SC); Medical Research and Materiel Command; Joint Science and Technology Office

Grant/Contract Number:: SC0014664

OSTI ID:: 1627427

Journal Information:: PLoS ONE, Vol. 5, Issue 10; ISSN 1932-6203

Publisher:: Public Library of ScienceCopyright Statement

Country of Publication:: United States

Language:: English

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