Medica 2026
Nov 16-19, 2026 - Düsseldorf, Germany

AMR Recombinant Protein Solutions for Diagnostics and Drug Discovery

Antimicrobial resistance (AMR) has emerged as one of the most critical global health challenges, threatening the effectiveness of antibiotics and complicating the treatment of infectious diseases. The rapid evolution and dissemination of resistance determinants—particularly β-lactamases and last-line resistance mechanisms—have significantly reduced the clinical utility of many antimicrobial agents, including carbapenems and colistin.

To address these challenges, the Coherent AMR Solution Portfolio offers a comprehensive suite of recombinant antimicrobial resistance proteins. This platform is designed to support diagnostic development, therapeutic research, and mechanistic studies by providing highly characterized, reproducible, and application-ready protein reagents.

What Is the Coherent AMR Solution Portfolio?

The Coherent AMR Solution Portfolio is an integrated collection of recombinant proteins representing the most significant antimicrobial resistance determinants found in clinically relevant bacterial pathogens. These proteins include multiple classes of β-lactamases, as well as non-enzymatic resistance factors and bacterial toxins.

Unlike traditional pathogen-derived materials, these recombinant proteins are produced under controlled conditions, ensuring:

The portfolio encompasses key resistance mechanisms, including:

By consolidating these critical targets into a single, coherent platform, this portfolio enables streamlined workflows and facilitates the development of multiplex assays and comprehensive resistance studies.

Key Structural and Functional Features of AMR Proteins

Antimicrobial resistance proteins exhibit diverse structural and mechanistic properties that underpin their ability to neutralize antibiotic activity.

Enzymatic Hydrolysis of Antibiotics

A large proportion of AMR proteins are β-lactamases that catalyze the hydrolysis of β-lactam antibiotics. These enzymes:

This enzymatic activity is central to resistance in many Gram-negative pathogens.

Fig. 1 β-Lactamase-Mediated Hydrolysis Mechanism
Schematic showing five stages of β-lactamase-mediated antibiotic hydrolysis: substrate binding, nucleophilic attack by the active-site serine, formation of an acyl–enzyme intermediate, hydrolysis by water, and release of the inactive ring-opened β-lactam product.Fig. 1 β-Lactamase-Mediated Hydrolysis Mechanism

Metal-Dependent Catalytic Mechanisms

Metallo-β-lactamases, such as NDM, VIM, and IMP, rely on zinc ions for catalytic activity. These enzymes:

Their unique catalytic mechanism makes them critical targets for next-generation inhibitor development.

Structural Diversity Across Enzyme Classes

AMR proteins are categorized into multiple structural classes:

This diversity necessitates a comprehensive panel approach for accurate detection and effective inhibitor screening.

Membrane Modification and Antibiotic Resistance

MCR-1 represents a distinct resistance mechanism involving lipid A modification in the bacterial outer membrane. This modification:

Superantigen Activity and Immune Modulation

TSST-1 is a potent superantigen that:

Fig. 2 TSST-1-Mediated T Cell Activation
Diagram illustrating TSST-1 superantigen activity in six steps, including secretion by *Staphylococcus aureus*, binding to MHC II and TCR Vβ, cross-linking of antigen-presenting cells and T cells, polyclonal T cell activation, and cytokine storm induction.Fig. 2 TSST-1 (Toxic Shock Syndrome Toxin-1)-Mediated T Cell Activation

Product Categories of the Coherent AMR Solution Portfolio

To enhance usability and facilitate targeted applications, the portfolio is organized into several specialized panels.

Carbapenem Resistance

Carbapenem resistance is a major concern in clinical microbiology due to its association with multidrug-resistant organisms.

Included proteins:

Cat_NProduct NameExpression System
DAG-WT7478Recombinant Klebsiella pneumoniae carbapenemase (KPC)E. coli
DAG-WT7479Recombinant New Delhi Metallo-beta-lactamase (NDM)E. coli
DAG-WT7480Recombinant Verona Integron-encoded Metallo-β-lactamase (VIM)E. coli
DAG-WT7481Recombinant Metallo-β-Lactamase (IMP)E. coli
DAG-WT7482Recombinant Oxacillinase-23 (OXA-23)E. coli
DAG-WT7483Recombinant Oxacillinase-48 (OXA-48)E. coli
DAG-WT7484Recombinant Oxacillinase-163 (OXA-163)E. coli

Features:

ESBL (Extended-Spectrum β-Lactamase)

ESBL enzymes are widely distributed and contribute significantly to antibiotic resistance.

Included proteins:

Cat_NProduct NameExpression System
DAG-WT7485Recombinant Cefotaximase-M (CTX-M)E. coli
DAG-WT7486Recombinant Temoniera β-Lactamase (TEM)E. coli
DAG-WT7487Recombinant Sulfhydryl Variable β-Lactamase-1 (SHV-1)E. coli

Applications:

AmpC Resistance

AmpC enzymes confer resistance to cephalosporins and are often underdiagnosed.

Included proteins:

Cat_NProduct NameExpression System
DAG-WT7488Recombinant Class C β-Lactamase (AmpC)E. coli
DAG-WT7489Recombinant CMY-type β-lactamase (CMY-2)E. coli

Applications:

Colistin Resistance Marker

Included protein:

Cat_NProduct NameExpression System
DAG-WT7490Recombinant Mobilized Colistin Resistance Protein-1 (MCR-1)E. coli

Significance:

Bacterial Toxin

Included protein:

Cat_NProduct NameExpression System
DAG-WT6239Recombinant S. aureus Toxic Shock Syndrome Toxin-1 (TSST-1) [His]E. coli

Applications:

Applications of the Coherent AMR Solution Portfolio

The portfolio supports a wide spectrum of applications across multiple disciplines.

Diagnostic Assay Development

Recombinant AMR proteins are essential for developing:

They serve as:

Antibody Development

These proteins are widely used as immunogens for:

Drug Discovery and Inhibitor Screening

AMR proteins play a critical role in:

Structural Biology and Mechanistic Studies

Applications include:

AMR Surveillance and Public Health Research

Standardized proteins support:

Immunological and Toxicological Studies

TSST-1 enables:

Advantages of the Coherent AMR Solution Portfolio

Comprehensive Coverage

This portfolio includes all major classes of AMR determinants, enabling:

High Purity and Reproducibility

Recombinant production ensures:

Application-Oriented Design

Products are tailored for:

Scalable Supply

Production pipelines support both research and commercial-scale needs.

Alignment with Global Health Needs

Targets included in this portfolio are directly associated with:

Frequently Asked Questions (FAQ)

Antibody FAQs

Still have questions?

Contact Us

They are used in diagnostics, antibody development, drug discovery, and resistance mechanism studies.

No. These recombinant proteins are non-infectious and safe to handle under standard laboratory conditions.

The portfolio includes carbapenemases, ESBLs, AmpC enzymes, colistin resistance, and bacterial toxins.

Yes. Many of these proteins are enzymatically active and suitable for inhibitor screening and kinetic analysis.

Yes. Custom protein expression, purification, and assay development services are available upon request.

Explore Related Services & Products

The Coherent AMR Solution Portfolio represents a unified and strategically designed platform to address the escalating global challenge of antimicrobial resistance. By integrating key resistance determinants into a single, application-focused offering, this portfolio empowers researchers and developers to accelerate innovation in diagnostics, therapeutics, and surveillance.

With its combination of scientific rigor, comprehensive coverage, and application versatility, this portfolio provides essential tools for advancing the understanding of resistance mechanisms and supporting the global effort to combat drug-resistant infections.

References

  1. Bush, K., & Bradford, P. A. (2020). Epidemiology of β-lactamase-producing pathogens. Clinical Microbiology Reviews, 33(2), e00047-19.
  2. Nordmann, P., Naas, T., & Poirel, L. (2011). Global spread of carbapenemase-producing Enterobacteriaceae. Emerging Infectious Diseases, 17(10), 1791–1798.
  3. Wang, R., van Dorp, L., Shaw, L. P., et al. (2018). The global distribution and spread of the mobilized colistin resistance gene mcr-1. Nature Communications, 9, 1179.
  4. Queenan, A. M., & Bush, K. (2007). Carbapenemases: the versatile β-lactamases. Clinical Microbiology Reviews, 20(3), 440–458.
  5. Liu, Y.-Y., Wang, Y., Walsh, T. R., et al. (2016). Emergence of plasmid-mediated colistin resistance mechanism MCR-1. The Lancet Infectious Diseases, 16(2), 161–168.
  6. Spaulding, A. R., Salgado-Pabón, W., Kohler, P. L., et al. (2013). Staphylococcal and streptococcal superantigen exotoxins. Clinical Microbiology Reviews, 26(3), 422–447.
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