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  • About Us
  • Our Approach
  • Discovery Platform
  • Pipeline
    • HMBD-001
    • HMBD-002
    • Covid-19 mAb
  • News
  • Careers

DISCOVERY PLATFORM

A Pioneering Platform


Hummingbird’s Rational Antibody Discovery platform leverages data rich, systems biology approaches to identify critical functional regions of a target protein, drive production of antibodies against these epitopes, and then isolate the antibodies that bind to them, thereby optimizing the therapeutic potential of a target.

This systematic and rational approach overcomes many of the common challenges of antibody discovery and allows us to efficiently and precisely engineer next-generation therapies that uniquely hit the right targets for the right patients.

Overcomes

  • Immunodominance
  • Tolerance
  • Epitope Instability

Unlocks

  • Multipass Proteins
  • Agonists

mAbHits is an immuno-engineering system to manipulate an immune response in order to control and optimize the production of antibodies against the desired optimal yet elusive epitopes. mAbHits results in a much higher proportion of usable therapeutic antibodies.

mAbPredict uses computational biology to integrate and analyze data from multidisciplinary sources to produce validated insights into the biology of the disease and provide predictions regarding which epitopes should be targeted for optimal efficacy and safety profiles

mAbHits is an immuno-engineering system to manipulate an immune response in order to control and optimize the production of antibodies against the desired optimal yet elusive epitopes. mAbHits results in a much higher proportion of usable therapeutic antibodies.

Classical Approaches vs. Rational Antibody Discovery


Missing the Mark
Classical approaches to antibody discovery generally lead to the majority of antibodies produced missing the optimal epitopes

Optimal Yet Elusive Epitope

Hitting the Spot
Our Rational Antibody Discovery platform systematically identifies optimal target epitopes, and immuno-engineers an immune response that results in the majority of antibodies hitting the desired epitopes

Missing the Mark
Classical approaches to antibody discovery generally lead to the majority of antibodies produced missing the optimal epitopes

Optimal Yet Elusive Epitope

Hitting the Spot
Our Rational Antibody Discovery platform systematically identifies optimal target epitopes, and immuno-engineers an immune response that results in the majority of antibodies hitting the desired epitopes

Applications of Our Platform


Stable Regions of Viral Targets

Rapid mutation of viral proteins allows viruses to evolve and evade the immune system and also makes it challenging to develop successful antiviral therapies, including antibodies. Our platform tackles this by predicting epitopes on key viral proteins that are unlikely to mutate and then immuno-engineers an immune response to those conserved epitopes.

Design of Functional Antibodies

The challenges in discovering functional antibodies are two-fold: knowing where antibodies must bind on a disease-related protein to provide therapeutic benefit and isolating antibodies that bind these optimal and often elusive epitopes. Our platform integrates computational biology and a mechanistic understanding of disease, gains insights into protein structure and function relationships and predicts ways to manipulate the system through antibody binding, then immuno-engineers an antibody response against these epitopes.

Drugging Multipass Transmembrane Proteins

Multipass transmembrane proteins, such as GPCRs and ion channels, are difficult to drug because the cell membrane contains many competing immunogenic epitopes, but if removed from the membrane, the protein becomes distorted from its natural shape. Our platform overcomes this issue of competition by immuno-engineering an antibody response towards optimal epitopes on the multipass protein when it is in the membrane.

Learn more – with our GPCR-like example

Agonist Antibodies

Most antibody drugs are effective by disrupting a protein’s function. “Agonism” is the opposite - when an antibody activates a protein's function for a therapeutic benefit. This can be a highly desirable attribute for a drug, for example, when we want to activate the patient’s own immune system to attack the tumor, however, to achieve agonism the antibody must bind to a very specific region of the target protein. Our platform immuno-engineers an antibody response towards these specific epitopes to achieve potent activation.

Overcoming Immunodominance

Immunodominance occurs when certain epitopes of a target protein are more likely than others to generate an immune response, resulting in most antibodies binding to those dominant epitopes. However, the elusive epitopes against which no antibodies were produced are often optimal for correcting disease mechanisms. Immunodominance is a common reason classical approaches fail and an important challenge that our platform overcomes by immuno-engineering an antibody response towards these elusive epitopes.

Overcoming Tolerance

Tolerance is the immune system’s failure to recognize and raise antibodies to a foreign protein because the protein is too similar to the host’s own proteins. Classical approaches to overcoming tolerance are often time- and resource-intensive as they involve changing the host itself. Our platform overcomes this by immuno-engineering an immune response to these conserved epitopes no matter the host.

Stable Regions of Viral Targets

Rapid mutation of viral proteins allows viruses to evolve and evade the immune system and also makes it challenging to develop successful antiviral therapies, including antibodies. Our platform tackles this by predicting epitopes on key viral proteins that are unlikely to mutate and then immuno-engineers an immune response to those conserved epitopes.

Design of Functional Antibodies

The challenges in discovering functional antibodies are two-fold: knowing where antibodies must bind on a disease-related protein to provide therapeutic benefit and isolating antibodies that bind these optimal and often elusive epitopes. Our platform integrates computational biology and a mechanistic understanding of disease, gains insights into protein structure and function relationships and predicts ways to manipulate the system through antibody binding, then immuno-engineers an antibody response against these epitopes.

Drugging Multipass Transmembrane Proteins

Multipass transmembrane proteins, such as GPCRs and ion channels, are difficult to drug because the cell membrane contains many competing immunogenic epitopes, but if removed from the membrane, the protein becomes distorted from its natural shape. Our platform overcomes this issue of competition by immuno-engineering an antibody response towards optimal epitopes on the multipass protein when it is in the membrane.

Learn more – with our GPCR-like example

Agonist Antibodies

Most antibody drugs are effective by disrupting a protein’s function. “Agonism” is the opposite - when an antibody activates a protein's function for a therapeutic benefit. This can be a highly desirable attribute for a drug, for example, when we want to activate the patient’s own immune system to attack the tumor, however, to achieve agonism the antibody must bind to a very specific region of the target protein. Our platform immuno-engineers an antibody response towards these specific epitopes to achieve potent activation.

Overcoming Immunodominance

Immunodominance occurs when certain epitopes of a target protein are more likely than others to generate an immune response, resulting in most antibodies binding to those dominant epitopes. However, the elusive epitopes against which no antibodies were produced are often optimal for correcting disease mechanisms. Immunodominance is a common reason classical approaches fail and an important challenge that our platform overcomes by immuno-engineering an antibody response towards these elusive epitopes.

Overcoming Tolerance

Tolerance is the immune system’s failure to recognize and raise antibodies to a foreign protein because the protein is too similar to the host’s own proteins. Classical approaches to overcoming tolerance are often time- and resource-intensive as they involve changing the host itself. Our platform overcomes this by immuno-engineering an immune response to these conserved epitopes no matter the host.

Stable Regions of Viral Targets

Rapid mutation of viral proteins allows viruses to evolve and evade the immune system and also makes it challenging to develop successful antiviral therapies, including antibodies. Our platform tackles this by predicting epitopes on key viral proteins that are unlikely to mutate and then immuno-engineers an immune response to those conserved epitopes.

JLABS Texas Medical Center
2450 Holcombe Blvd Suite J Houston, TX 77021

Registered Company No:
201505192N
Temasek Lifescience Laboratories
1 Research Link
Singapore 117604
For general enquiries, please contact contact@hummingbirdbio.com

For career enquiries, please contact careers@hummingbirdbio.com
JLABS Texas Medical Center
2450 Holcombe Blvd Suite J
Houston, TX 77021
Temasek Lifescience Laboratories
1 Research Link
Singapore 117604
Registered Company No: 201505192N
For general enquiries, please contact contact@hummingbirdbio.com
For career enquiries, please contact careers@hummingbirdbio.com
PRIVACY POLICY | © 2020 Hummingbird Bioscience

TM4SF5 ANTIBODY

G protein-coupled receptors (GPCRs) and other multipass transmembrane proteins, including tetraspanins and ion channels, are among the most diverse and well-studied family of cell surface receptors and are involved in growth, metabolism and homeostasis. Despite their prevalence, they are notoriously challenging to target. About 80 percent of the GPCR family is currently not targeted by approved therapies, despite their relevance in many diseases. Hummingbird’s rational antibody discovery platform has demonstrated the ability to generate functional antibodies with high affinity and specificity against these hard-to-drug target classes.

References:https://www.nature.com/scitable/topicpage/gpcr-14047471/
https://www.cell.com/trends/pharmacological-sciences/fulltext/S0165-6147(19)30064-1

Short extracellular loop and HMBD Binding Site

Membrane

Membrane

  • About Us
  • Our Approach
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    • HMBD-002
    • Covid-19 mAb
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