Inhibition of Toxic Shock by Human Monoclonal Antibodies against Staphylococcal Enterotoxin B
Abstract
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.more »
- Authors:
-
- 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)
- Publication Date:
- Research Org.:
- Medical Research Institute of Infectious Diseases, Frederick, MD (United States); Hood College, Frederick, MD (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC); Medical Research and Materiel Command; Joint Science and Technology Office
- OSTI Identifier:
- 1627427
- Grant/Contract Number:
- SC0014664
- Resource Type:
- Accepted Manuscript
- Journal Name:
- PLoS ONE
- Additional Journal Information:
- Journal Volume: 5; Journal Issue: 10; Journal ID: ISSN 1932-6203
- Publisher:
- Public Library of Science
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; enzyme-linked immunoassays; antibodies; T cells; toxins; monoclonal antibodies; staphylococcus aureus; toxic shock syndrome; antibody therapy
Citation Formats
Larkin, Eileen A., Stiles, Bradley G., and Ulrich, Robert G. Inhibition of Toxic Shock by Human Monoclonal Antibodies against Staphylococcal Enterotoxin B. United States: N. p., 2010.
Web. doi:10.1371/journal.pone.0013253.
Larkin, Eileen A., Stiles, Bradley G., & Ulrich, Robert G. Inhibition of Toxic Shock by Human Monoclonal Antibodies against Staphylococcal Enterotoxin B. United States. https://doi.org/10.1371/journal.pone.0013253
Larkin, Eileen A., Stiles, Bradley G., and Ulrich, Robert G. Mon .
"Inhibition of Toxic Shock by Human Monoclonal Antibodies against Staphylococcal Enterotoxin B". United States. https://doi.org/10.1371/journal.pone.0013253. https://www.osti.gov/servlets/purl/1627427.
@article{osti_1627427,
title = {Inhibition of Toxic Shock by Human Monoclonal Antibodies against Staphylococcal Enterotoxin B},
author = {Larkin, Eileen A. and Stiles, Bradley G. and Ulrich, Robert G.},
abstractNote = {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.},
doi = {10.1371/journal.pone.0013253},
journal = {PLoS ONE},
number = 10,
volume = 5,
place = {United States},
year = {Mon Oct 11 00:00:00 EDT 2010},
month = {Mon Oct 11 00:00:00 EDT 2010}
}
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- Toxins, Vol. 11, Issue 3
Evaluation of a novel type of imaging probe based on a recombinant bivalent mini-antibody construct for detection of CD44v6-expressing squamous cell carcinoma
journal, December 2015
- Haylock, Anna-Karin; Spiegelberg, Diana; Mortensen, Anja C.
- International Journal of Oncology, Vol. 48, Issue 2
The staphylococcal enterotoxin (SE) family: SEB and siblings
journal, November 2013
- Krakauer, Teresa; Stiles, Bradley G.
- Virulence, Vol. 4, Issue 8
Staphylococcal Superantigens: Pyrogenic Toxins Induce Toxic Shock
journal, March 2019
- Krakauer, Teresa
- Toxins, Vol. 11, Issue 3
Engineered pH-dependent recycling antibodies enhance elimination of Staphylococcal enterotoxin B superantigen in mice
journal, December 2018
- Kroetsch, Andrew; Qiao, Chunxia; Heavey, Mairead
- mAbs, Vol. 11, Issue 2