Ab-CoV

Ab-CoV catalogs experimental interaction profiles and structural annotations of coronavirus-neutralizing antibodies to support analysis of antibody binding, neutralization potency, epitope–paratope relationships, and the effects of point mutations on stability and affinity.

Key Features:

• Extensive experimental dataset: Contains interaction profiles for 1,780 neutralizing antibodies with over 3,200 datapoints including IC50, EC50, and KD measurements.
• Structural mutation effects: For entries with known three-dimensional structures, provides predicted changes in stability and affinity resulting from point mutations at interface residues.
• Epitope and paratope annotations: Includes detailed epitope and paratope information for antibody–antigen interactions.
• Viral protein structural features: Documents structural characteristics of viral proteins relevant to antibody binding.
• Comparative antibody analysis: Reports sequentially similar therapeutic antibodies to enable comparative studies.
• Structural representation: Includes Collier de Perles plots as a graphical representation of protein interface features.

Scientific Applications:

• Antibody design and engineering: Supports rational modification and optimization of antibodies by providing binding metrics, epitope–paratope data, and predicted mutation effects.
• Vaccine development: Informs identification of antigenic sites and epitope targets relevant for eliciting neutralizing responses.
• Drug discovery: Facilitates selection and comparison of antibody candidates based on measured affinities and neutralization potencies.
• Structural biology research: Enables analysis of protein–protein interfaces, structural determinants of binding, and mutation-induced stability or affinity changes.

Methodology:

Curated experimental interaction profiles; prediction of stability and affinity changes for point mutations at interface residues; generation of Collier de Perles plots for structural representation.