Nicholas John Mantis

The paper shows that OspA antibodies rapidly stop B. burgdorferi motility, using single-cell fluorescence microscopy.

This paper identifies a conserved epitope on OspA that is broadly protective against multiple Borrelia genospecies, suggesting a basis for a universal Lyme disease vaccine.

This study shows that an Fc-silent variant of the monoclonal antibody LA-2 provides equivalent passive protection against Borrelia burgdorferi in mice, suggesting its protective mechanism is independent of complement.

This study shows that OspA antibodies inhibit B. burgdorferi transmigration in vitro, with some antibodies causing bacterial aggregation and others blocking movement without agglutination.

This study uses a CRISPRi screen to identify genes in Salmonella Typhimurium that affect multicellular aggregate formation in response to Sal4 IgA, revealing a role for Type 1 Fimbriae in evading antibody-mediated agglutination.

This study identifies distinct antibody profiles in mice vaccinated with potent and subpotent whole cell pertussis vaccines, suggesting a potential serologic surrogate for the intracerebral mouse potency test.

This study evaluates the interchangeability of dried blood spots and oral fluids for SARS-CoV-2 antibody detection across laboratories using microsphere immunoassays.

This study demonstrates that mRNA-LNPs can deliver pathogen-specific monoclonal IgG into breast milk, enabling transfer of functional antibodies to suckling mice.

The paper evaluates IgG reactivity to OspC-derived peptides in Lyme disease serum samples, identifying C10 as the most reactive epitope and highlighting complexities in B cell responses.

This study identifies a type-specific B cell epitope on OspC type A of Borreliella burgdorferi and shows its role in antibody-mediated motility inhibition.

This study evaluates the use of dried blood spots (DBS) to quantify SARS-CoV-2 neutralizing antibodies using multiple assays, finding that DBS eluates can reliably measure neutralizing titers.

The paper describes a biparatopic intrabody that protects Vero cells from ricin toxin by targeting two distinct epitopes on the toxin's enzymatic subunit, offering enhanced resistance compared to individual VHHs.

This study determines the structure of a human monoclonal antibody in complex with OspC from Borreliella burgdorferi, revealing its epitope and interaction mechanism.

The paper identifies unique borreliacidal epitopes on OspA using VHHs and evaluates their reactivity across OspA serotypes.