David Vance

Research Assistant Professor

University at Albany, State University of New York

United States

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David Vance is a Research Assistant Professor at the University at Albany, USA. His research focuses on the structural analysis and immune response to proteins associated with Lyme disease, particularly Borreliella burgdorferi, and includes the study of monoclonal antibodies and single-domain antibodies. Recent articles authored by Dr. Vance explore various B-cell epitopes and their role in vaccine development and toxin inhibition.

Articles (15)

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2025

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2020

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2020

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2020

Collaborators (2)

David Weis

Adjunct Professor

University of Kansas

UNITED STATES

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Nicholas J. Mantis

University at Albany, State University of New York

UNITED STATES

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David Vance

Research Interests

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Articles (15)

A type-specific B-cell epitope at the apex of outer surface protein C (OspC) of the Lyme disease spirochete, Borreliella burgdorferi

Structure of a Human Monoclonal Antibody in Complex with Outer Surface Protein C of the Lyme Disease Spirochete, Borreliella burgdorferi

A Biparatopic Intrabody Renders Vero Cells Impervious to Ricin Intoxication

Single-domain antibodies reveal unique borrelicidal epitopes on the Lyme disease vaccine antigen, outer surface protein A (OspA)

Structure of a transmission blocking antibody in complex with Outer surface protein A from the Lyme disease spirochete, Borreliella burgdorferi

Structural Elucidation of a Protective B Cell Epitope on Outer Surface Protein C (OspC) of the Lyme Disease Spirochete, Borreliella burgdorferi.

Structural Basis of Antibody-Mediated Inhibition of Ricin Toxin Attachment to Host Cells.

Human B Cell Epitope Map of the Lyme Disease Vaccine Antigen, OspA

Serological Analysis Identifies Consequential B Cell Epitopes on the Flexible Linker and C-Terminus of Decorin Binding Protein A (DbpA) from Borrelia burgdorferi

Single-domain antibodies neutralize ricin toxin intracellularly by blocking access to ribosomal P-stalk proteins

Neutralization of typhoid toxin by alpaca-derived, single-domain antibodies targeting the PltB and CdtB subunits

Structural analysis of toxin-neutralizing, single-domain antibodies that bridge ricin's A-B subunit interface.

Slaying SARS-CoV-2 One (Single-domain) Antibody at a Time.

Sites of vulnerability on ricin B chain revealed through epitope mapping of toxin-neutralizing monoclonal antibodies.

Intracellular Neutralization of Ricin Toxin by Single-domain Antibodies Targeting the Active Site.

Collaborators (2)

David Weis

Nicholas J. Mantis

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