Mechanisms mediating enhanced neutralization efficacy of Staphylococcal enterotoxin B by combinations of monoclonal antibodies

Dutta, Kaushik; Varshney, Avanish K.; Franklin, Matthew C.; Goger, Michael; Wang, Xiaobo; Fries, Bettina C.

doi:10.1074/jbc.m114.630715

Mechanisms mediating enhanced neutralization efficacy of Staphylococcal enterotoxin B by combinations of monoclonal antibodies

Journal Article · Thu Jan 08 00:00:00 EST 2015 · Journal of Biological Chemistry

DOI:https://doi.org/10.1074/jbc.m114.630715· OSTI ID:1347990

Dutta, Kaushik ^[1]; Varshney, Avanish K. ^[2]; Franklin, Matthew C. ^[3]; Goger, Michael ^[3]; Wang, Xiaobo ^[4]; Fries, Bettina C. ^[2]

New York Structural Biology Center, New York, NY (United States); DOE Office of Scientific and Technical Information (OSTI)
Stony Brook Univ., Stony Brook, NY (United States); Albert Einstein College of Medicine, Bronx, NY (United States)
New York Structural Biology Center, New York, NY (United States)
Albert Einstein College of Medicine, Bronx, NY (United States)

Staphylococcal enterotoxin B (SEB) is a superantigen that cross-links the major histocompatibility complex class II and specific V-β chains of the T-cell receptor, thus forming a ternary complex. Developing neutralizing mAb to disrupt the ternary complex and abrogate the resulting toxicity is a major therapeutic challenge because SEB is effective at very low concentrations. We show that combining two SEB-specific mAbs enhances their efficacy, even though one of the two mAbs by itself has no effect on neutralization. Crystallography was employed for fine-mapping conformational epitopes in binary and ternary complexes between SEB and Fab fragments. NMR spectroscopy was used to validate and identify subtle allosteric changes induced by mAbs binding to SEB. The mapping of epitopes established that a combination of different mAbs can enhance efficacy of mAb-mediated protection from SEB induced lethal shock by two different mechanisms: one mAb mixture promoted clearance of the toxin both in vitro and in vivo by FcR-mediated cross-linking and clearance, whereas the other mAb mixture induced subtle allosteric conformational changes in SEB that perturbed formation of the SEB·T-cell receptor·major histocompatibility complex class II trimer. Lastly structural information accurately predicted mAb binding to other superantigens that share conformational epitopes with SEB. Fine mapping of conformational epitopes is a powerful tool to establish the mechanism and optimize the action of synergistic mAb combinations.

View Accepted Manuscript (DOE)

Research Organization:: New York Structural Biology Center, New York, NY (United States)

Sponsoring Organization:: Department of Defense (DoD); National Institutes of Health (NIH); USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)

Grant/Contract Number:: AC02-98CH10886

OSTI ID:: 1347990

Journal Information:: Journal of Biological Chemistry, Journal Name: Journal of Biological Chemistry Journal Issue: 11 Vol. 290; ISSN 0021-9258

Publisher:: American Society for Biochemistry and Molecular BiologyCopyright Statement

Country of Publication:: United States

Language:: English

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59 BASIC BIOLOGICAL SCIENCES
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SEB
Staphylococcal enterotoxin B
X-ray crystallography
bacterial toxin
crystal structure
epitope mapping
monoclonal antibody
nuclear magnetic resonance (NMR)

Mechanisms mediating enhanced neutralization efficacy of Staphylococcal enterotoxin B by combinations of monoclonal antibodies

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