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Integral Molecular

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Philadelphia, Pennsylvania, US

About Integral Molecular

NEW: SARS-COV-2 Assay for Neutralizing Antibodies. Integral Molecular has developed a new assay to test for SARS-CoV-2 neutralizing antibodies. 


Integral Molecular is a research-driven biotechnology company enabling antibody discovery against complex membrane proteins. The company provides characterization services, reagents, and a full antibody discovery platform optimized to work with membrane protein targets, including GPCRs, ion channels, and transporters.

Founded in 2001, Integral has worked with over 300 different partners and customers, including all top 10 pharmaceutical companies.

Our Services (5)


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Reporter Virus Particles

Price on request

Integral Molecular offers pseudotyped Reporter Virus Particles to test infectivity and neutralization for:

• SARS-CoV-2

• SARS-CoV-2 D614G

• SARS-CoV-1

• MERS-CoV

• Dengue serotypes 1-4

• Zika

Reporter Virus Particles (RVPs) are replication-incompetent pseudotyped virus particles that enable safe (BSL-2), easy, and high-throughput viral infectivity and neutralization assays using standard detection instrumentation. RVPs display antigenically correct envelope/spike protein and carry a modified genome that expresses a convenient optical reporter gene (GFP or luciferase) within 24 hours of cellular infection.

RVPs are available as a ready-to-use reagent that provides a safe and efficient alternative to plaque assays, and are produced under quality-controlled conditions as a critical reagent to enable regulatory submissions.

Applications of RVPs

• Antibody neutralization

• Serum screening

• High-throughput assays

Advantages of SARS-CoV-2 RVPs 

• Safe in a BSL-2 environment

• Quantitative (luciferase) or fluorescent (GFP) read-out

• Compatible with high-throughput plate-based assays

• Quality-controlled production for use as a critical reagent

Click here for additional information on coronavirus RVPS

Click here for additional information on dengue and Zika RVPs


Publications 

Whitbeck ET AL. 2020. Antigenicity, Stability and Reproducibility of Zika Reporter Virus Particles for Long-term Applications. BIORXIV doi.org/10.1101/2020.04.21.047241.

Mattia ET AL. 2011. Dengue Reporter Virus Particles for Measuring Neutralizing Antibodies Against Each of the Four Dengue Serotypes. PLOS ONE 6(11):e27252. doi: 10.1371/journal.pone.0027252.


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Membrane Proteome Array

Price on request

25% of antibodies are polyspecific. De-risk your program by choosing the right lead molecule.

Off-target antibody binding is common and can cause serious adverse events

Off-target drug binding can cause serious side effects or even death. We developed the Membrane Proteome Array as the largest array of membrane proteins yet assembled for deorphaning and specificity profiling of biotherapeutics including antibodies and CAR T-cell therapy.


Why is the Membrane Proteome Array so successful?

  • Encompasses ~95% of the membrane proteome (6,000 native membrane proteins)
  • Flow cytometry for high-sensitivity detection in unfixed human cells
  • Cell-based platform ensures native protein conformation and post-translational modifications
  • Optimized process for rapid 4-week turnaround

What can the Membrane Proteome Array do for you?

Specificity Profiling: We screen your antibody to determine its membrane proteome binding profile, identifying target and off-target interactions

Antibody Deorphaning: We screen your antibody of unknown specificity to identify which protein(s) on the MPA your antibody binds

Membrane Proteome Array Case Studies

  • Click here to see how FairJourney established that their antibodies do not demonstrate off-target binding
  • Click here to understand how a MAb can cross-react with a completely unrelated protein
  • Click here to learn how the Membrane Proteome Array was used to deorphan panels of antibodies with unknown targets

Toxicology Biopharmaceutical Characterization Profiling Target Identification Antibodies membrane protein GPCR Ion Channel flow cytometry specificity profiling high throughput monoclonal antibody Show 12 more tags Show less

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Epitope Mapping

Price on request

We Map Conformational Epitopes at Single Amino Acid Resolution with > 95% Success

Integral Molecular’s proprietary Shotgun Mutagenesis technology is the only high-throughput technique that can reliably map conformational epitopes at single amino acid resolution. We have mapped 1,000+ epitopes to date with > 95% success, including:

  • Epitopes on GPCRs, transporters, and viral envelope proteins
  • Conformational epitopes
  • Epitopes on multi-subunit proteins
  • Receptor state-dependent epitopes

High-resolution epitope mapping enables

  • Lead candidate selection by uncovering mechanisms of action
  • MAb protection by strengthening IP

How Does Shotgun Mutagenesis Work?

We mutate each residue of a target protein and measure the precise binding of an antibody to the target within intact cells.

  • Automated point mutation of every residue in the target protein to alanine
  • Native expression of individual mutants in human cells, enabling mapping of conformational epitopes
  • High-throughput expression, antibody reactivity, and functional testing
  • 3D structural visualization of the epitope

Epitope Mapping Projects Include

  • Assay Setup Report, summarizing optimized conditions for screening
  • MAb/ligand screening on the Ala-scan mutation array
  • Final report, containing fully analyzed data package, identification of amino-acid resolution epitope, publication-ready figures

Shotgun Mutagenesis Epitope Mapping Case Studies

  • Click here to see how Novartis characterized the mechanism of action for CXCR2 antibodies
  • Click here to see how Covagen distinguished HER2 antibodies from existing therapeutics
  • Click here to learn how epitope mapping enhances antibody protection 

Select Publications Featuring Shotgun Mutagenesis Epitope Mapping

  • Dussupt et al., 2020. Potent Zika and dengue cross-neutralizing antibodies induced by Zika vaccination in a dengue-experienced donor. NATURE MED 26, 228-235.
  • Zhang et al., 2018. Mxra8 is a receptor for multiple arthritogenic alphaviruses. NATURE 557, 570-574.
  • Zhao et al., 2017. Immunization-elicited broadly protective antibody reveals Ebolavirus fusion loop as a site of vulnerability. CELL 169, 891-904.
  • Davidson and Doranz. 2014. A high-throughput shotgun mutagenesis approach to mapping B-cell antibody epitopes. IMMUNOLOGY 143(1), 13-20.
  • Fong et al., 2014. Exposure of epitope residues on the outer face of the Chikungunya virus envelope trimer determines antibody neutralizing efficacy. J VIROL 88(24), 14364-14379.
  • Paes et al., 2009. Atomic-level mapping of antibody epitopes on a GPCR. J AM CHEM SOC 131(20), 6952-6954.

Drug Discovery Amino Acid Substitution antibodies antibody discovery biologics High-throughput Antibodies Monoclonal antibodies G coupled protein receptor Transporter Membrane proteins Ion Channel Show 12 more tags Show less

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Antibody Discovery

Price on request

The MPS Antibody Discovery platform overcomes the key challenges in isolating antibodies against difficult targets by:

  1. Maintaing antigens in their native conformation.
  2. Isolating diverse panels of MAbs to find rare agonists/antagonists.
  3. Obtaining high-titer responses, even for highly conserved proteins.


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Lipoparticle Production

Price on request

Lipoparticles are virus-like particles that concentrate and present conformationally intact membrane proteins on non-infectious particles. This enables complex membrane proteins to be manipulated as soluble, high-concentration proteins for antibody immunization and screening.


Why are Lipoparticles so effective for antibody discovery?

  • Lipoparticles concentrate proteins at 10-100× (~50-200 pmol/mg) the concentration of cells or membrane preps, resulting in robust immune responses and more successful antibody screens
  • Lipoparticles display properly folded membrane proteins in their native cellular membrane, resulting in the ability to elicit and screen for conformational, functional antibodies
  • Lipoparticles are ~150 nm, the size of most viruses, and so are optimal targets for dendritic cells in vivo and surface attachment for phage display

Lipoparticle applications include:

Immunization

Phage/yeast display

Antibody screening by ELISA

Kinetic analysis by biosensor

Radioligand and fluorescent binding assays

Custom Lipoparticles

Lipoparticles are typically customized to incorporate customers’ specified membrane proteins. Each Lipoparticle batch is assessed by using up to 16 quality-control metrics to ensure homogeneity, purity, and target protein integrity. Hundreds of membrane proteins have been successfully incorporated into Lipoparticles, which can be modified with biotin or fluorescence for detection.


ReadyReceptor Lipoparticles

Pre-validated Lipoparticles contain optimized, highly expressed membrane proteins and are available for rapid delivery. ReadyReceptor Lipoparticles are produced and validated by using the same stringent quality metrics as are used for our Custom Lipoparticle production. See all ReadyReceptor Lipoparticles.

Case Studies

  • Learn how Lipoparticles rescued a CX3CR1 discovery campaign and enabled a clinical stage antibody
  • Learn how Argenx used Lipoparticles to isolate antibodies with diverse epitopes against the GPCR glucagon receptor
  • Learn how AdAlta used our CXCR4 Lipoparticles to isolate i-bodies
  • Learn how Pfizer used Lipoparticles to target the CXCR4 pathway in leukemia

Select publications that feature Lipoparticles

  • Tucker ET AL. 2018. Isolation of state-dependent monoclonal antibodies against the 12-transmembrane domain glucose transporter 4 using virus-like particles. PNAS 115(22):E4990-E4999.
  • Fong ET AL. 2014. Exposure of epitope residues on the outer face of the Chikungunya virus envelope trimer determines antibody neutralizing efficacy. J VIROL 88(24)14364-14379.
  • Willis ET AL. 2008. Virus-like particles as quantitative probes of membrane protein interactions. BIOCHEMISTRY 47(27):6988-6990.
  • Endres ET AL. 1997. Targeting of HIV- and SIV-infected cells by CD4-chemokine receptor pseudotypes. SCIENCE 278(5342): 1462-1464.


GPCR membrane protein Ion Channel Transporter

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