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Robert G. Ulrich

Researcher at United States Army Medical Research Institute of Infectious Diseases

Publications -  52
Citations -  1493

Robert G. Ulrich is an academic researcher from United States Army Medical Research Institute of Infectious Diseases. The author has contributed to research in topics: Antigen & Vaccination. The author has an hindex of 24, co-authored 52 publications receiving 1403 citations. Previous affiliations of Robert G. Ulrich include National Institutes of Health.

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Development of engineered vaccines effective against structurally related bacterial superantigens

TL;DR: It is concluded that an optimal combination of these genetically attenuated superantigen vaccines may protect against all structurally related superantigens.
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Superantigen vaccines: a comparative study of genetically attenuated receptor-binding mutants of staphylococcal enterotoxin A.

TL;DR: These results, combined with an understanding of the molecular nature of superantigen and receptor interactions, indicate that targeting MHC class II binding by site-directed mutagenesis will produce the most effective vaccine.
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Generation of protective immunity by inactivated recombinant staphylococcal enterotoxin B vaccine in nonhuman primates and identification of correlates of immunity

TL;DR: It is suggested that the attenuated SEB is fully protective against aerosolized toxin when administered to unprimed subjects and various biomarkers that showed substantial promise as correlates of immunity and surrogate endpoints for assessing in vivo biological responses in primates, and possibly in humans, to vaccines against SEs.
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Mucosal Vaccination with Recombinantly Attenuated Staphylococcal Enterotoxin B and Protection in a Murine Model

TL;DR: Mice vaccinated mucosally were protected against a 50% lethal dose of wild-type SEB given i.p. or mucosal, thus demonstrating that nasal or oral administration of this SEBv elicits systemic and mucosal antibodies to SEB that protect against SEB-induced lethal shock.
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Staphylococcal enterotoxins A and B share a common structural motif for binding class II major histocompatibility complex molecules.

TL;DR: An examination of the experimental data with the homology model clarifies how T-cell responses to enterotoxin A, and most bacterial superantigens, are likely to be mediated by variations of a structurally conserved HLA-DRα binding motif.