As antimicrobial resistance continues to evolve, vancomycin-resistant enterococci (VRE) remain a major concern, particularly in healthcare settings. Among the various resistance types, VanB-mediated resistance is one of the most frequently encountered in clinical isolates of Enterococcus faecium and Enterococcus faecalis. Unlike VanA, which confers resistance to both vancomycin and teicoplanin, VanB confers resistance solely to vancomycin, presenting unique challenges and opportunities in diagnostic development.

Rapid and specific identification of VanB resistance mechanisms is essential for appropriate treatment and infection control. While nucleic acid-based techniques are common, monoclonal antibodies (mAbs) offer a compelling complementary approach. SynAbs leverages its deep expertise in small molecule immunogenicity to generate RUO-grade in-vitro diagnostic antibodies against VanB-associated vancomycin derivatives.

VanB-type resistance arises from the vanB operon, which encodes enzymes that remodel bacterial peptidoglycan precursors from D-Ala-D-Ala to D-Ala-D-Lac. This biochemical change results in a reduced binding affinity of vancomycin, though teicoplanin sensitivity is preserved. VanB expression is inducible and varies depending on environmental conditions, making detection particularly challenging.

VanB-modified peptides differ slightly in molecular architecture from VanA-modified ones. These nuanced differences make the development of specific antibodies against VanB-associated modifications extremely difficult. A high degree of molecular fidelity is required to ensure that mAbs bind only to vancomycin B-related epitopes.

Due to the structural similarity between VanA and VanB modified ligands, cross-reactivity is a persistent issue. Developing a monoclonal antibody that recognizes only VanB-modified D-Ala-D-Lac precursors while ignoring VanA-induced forms is a sophisticated immunological challenge that SynAbs is actively addressing.

Vancomycin, being a small glycopeptide, is inherently non-immunogenic. To raise monoclonal antibodies, vancomycin analogs must be conjugated to carrier proteins like KLH or BSA. However, the immunogenicity of VanB-associated structures is further diminished due to their minimal variation from native forms.

We design and synthesize haptens that closely mimic VanB-specific modifications. These are conjugated using controlled chemistries that maximize immunogenic exposure while preserving functional group integrity.

SynAbs advanced hybridoma technology enables high-throughput screening of thousands of antibody-producing clones. Each candidate is evaluated for:

• High specificity for VanB-modified peptides

• Minimal or no binding to VanA forms

• Strong binding affinity to free and conjugated targets

All antibodies developed for VanB detection undergo rigorous validation and are produced under strict quality control to ensure lot-to-lot consistency, reproducibility, and suitability for RUO IVD applications.

Monoclonal antibodies targeting VanB resistance can be incorporated into a wide array of diagnostic formats:

• ELISA: For lab-based screening with high sensitivity and throughput.

• Lateral Flow Devices (LFD): For rapid detection at point-of-care.

• Microfluidics and Biosensors: For integration into digital diagnostics.

These platforms enable fast and accurate VanB resistance surveillance in hospitals, clinics, and community settings.

SynAbs is at the frontier of immunodiagnostics, pushing boundaries in the generation of high-quality monoclonal antibodies for complex small molecule targets like VanB-modified vancomycin. Our collaborative model offers:

• Antibody development

• Comprehensive screening and validation

• RUO and pre-IVD grade antibody supply up to 150 grams

Get in touch to discover how we can help you develop rapid, accurate, and scalable solutions for detecting Vancomycin B resistance.

SynAbs – Where precision meets diagnostic innovation.