Glycan biomarkers / in vitro diagnostics (IVDs) from innovative technologies in glycoscience contribute to human healthcare
◆ Glycan Biomarkers / In Vitro Diagnostics
Biomarkers and IVDs Targeting Glycan Structures
Glycans — the fourth chain of life — define differences between cells, organs, and individuals, and change in a disease-specific manner in conditions such as infections and cancer.
Unlike conventional protein-quantity-based biomarkers, glycan-based “qualitative changes” offer a powerful new dimension for disease detection, making glycobiomarkers critically important tools for precision medicine.
Leveraging our proprietary technologies in glycoprotein analysis and target-specific antibody generation, we are developing novel biomarkers and IVDs for the next generation of personalized medicine.
Our company possesses technologies including glycan structure analysis of glycoproteins and antibody generation against target glycoproteins, and we are engaged in the development of novel biomarkers and in vitro diagnostics.
HBV Glycan Biomarker HBsAgGi
Hepatitis B virus (HBV) infection can progress from chronic hepatitis to cirrhosis and hepatocellular carcinoma, posing a major global health burden — particularly in East Asia including Japan and China, where Genotype C is prevalent. 1
HBV particles are modified by N-linked and O-linked glycans involved in viral secretion and stability. In the blood of chronic hepatitis B patients, infectious particles (DNA virions and RNA virions) represent only 1/100 to 1/10,000 of non-infectious particles, highlighting the unmet need for infectious-particle-specific detection. 2-4
We demonstrated that in Genotype C HBV, the PreS2 domain of M-HBsAg is O-glycosylated specifically on infectious particles. ² Our monoclonal antibody HBsAgGi targets this modification, enabling specific detection of infectious HBV particles — including those carrying HBV-RNA in patients with suppressed HBV-DNA under nucleos(t)ide analogue therapy. 5-7
HBsAgGi has received regulatory approval as an IVD and is also available as a research reagent with contract measurement services.
References:
1. https://www.who.int/news-room/fact-sheets/detail/hepatitis-b
2. Schadler and Hildt (2009) Viruses 1:185-209. doi: 10.3390/v1020185.
3. Schmitt et al. (2004) J Gen Virol 85:2045-2053. doi: 10.1099/vir.0.79932-0.
4. Dobrica et al. (2020) Cells 9:1404. doi: 10.3390/cells9061404.
5. Wagatsuma et al. (2018) Anal Chem 90:10196-10203. doi: 10.1021/acs.analchem.8b01030
6. Angata et al. (2021) Biochim Biophys Acta Gen Subj. 1866:130020, 2022. doi:10.1016/j.bbagen.2021.130020
7. Wang et al. (2016) J Hepatol. 65:700-710. doi: 10.1016/j.jhep.2016.05.029.
Antibody Therapeutics Targeting Glycan Structures
◆ Contract Service for Glycan-Targeted Therapeutic Antibodies
N-glycosylation — due to its highly branched structure — is a well-recognized driver of immune evasion, hindering therapeutic antibody binding and reducing pharmacological efficacy.
Generating antibodies against such N-glycosylated targets has long been considered technically challenging.
Drawing on our deep expertise in glycan research, we have established the Glea™ platform — a proprietary technology enabling the development of highly specific antibodies and antibody-lectin chimeras against N-glycosylated therapeutic targets.
We offer this as a contract service for customers seeking antibodies against targets of interest.