Imperial College London
Alternate

DrWengangChai

Faculty of Medicine, Department of Metabolism, Digestion and Reproduction

Senior Research Fellow
 
 
 
//

Contact

 

+44 (0)20 7594 2596w.chai

 
 
//

Location

 

Burlington DanesHammersmith Campus

//

Summary

 

Publications

Citation

BibTex format

@article{Loureiro:2018:10.1038/s41598-018-30421-w,
author = {Loureiro, LR and Sousa, DP and Ferreira, D and Chai, W and Lima, L and Pereira, C and Lopes, CB and Correia, VG and Silva, LM and Li, C and Santos, LL and Ferreira, JA and Barbas, A and Palma, AS and Novo, C and Videira, PA},
doi = {10.1038/s41598-018-30421-w},
journal = {Scientific Reports},
title = {Novel monoclonal antibody L2A5 specifically targeting sialyl-Tn and short glycans terminated by alpha-2–6 sialic acids},
url = {http://dx.doi.org/10.1038/s41598-018-30421-w},
volume = {8},
year = {2018}
}
Download

RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Incomplete O-glycosylation is a feature associated with malignancy resulting in the expression of truncated glycans such as the sialyl-Tn (STn) antigen. Despite all the progress in the development of potential anti-cancer antibodies, their application is frequently hindered by low specificities and cross-reactivity. In this study, a novel anti-STn monoclonal antibody named L2A5 was developed by hybridoma technology. Flow cytometry analysis showed that L2A5 specifically binds to sialylated structures on the cell surface of STn-expressing breast and bladder cancer cell lines. Moreover, immunoblotting assays demonstrated reactivity to tumour-associated O-glycosylated proteins, such as MUC1. Tumour recognition was further observed using immunohistochemistry assays, which demonstrated a high sensitivity and specificity of L2A5 mAb towards cancer tissue, using bladder and colorectal cancer tissues. L2A5 staining was exclusively tumoural, with a remarkable reactivity in invasive and metastasis sites, not detectable by other anti-STn mAbs. Additionally, it stained 20% of cases of triple-negative breast cancers, suggesting application in diseases with unmet clinical needs. Finally, the fine specificity was assessed using glycan microarrays, demonstrating a highly specific binding of L2A5 to core STn antigens and additional ability to bind 2–6-linked sialyl core-1 probes. In conclusion, this study describes a novel anti-STn antibody with a unique binding specificity that can be applied for cancer diagnostic and future development of new antibody-based therapeutic applications.
AU  - Loureiro,LR
AU  - Sousa,DP
AU  - Ferreira,D
AU  - Chai,W
AU  - Lima,L
AU  - Pereira,C
AU  - Lopes,CB
AU  - Correia,VG
AU  - Silva,LM
AU  - Li,C
AU  - Santos,LL
AU  - Ferreira,JA
AU  - Barbas,A
AU  - Palma,AS
AU  - Novo,C
AU  - Videira,PA
DO  - 10.1038/s41598-018-30421-w
PY  - 2018///
SN  - 2045-2322
TI  - Novel monoclonal antibody L2A5 specifically targeting sialyl-Tn and short glycans terminated by alpha-2–6 sialic acids
T2  - Scientific Reports
UR  - http://dx.doi.org/10.1038/s41598-018-30421-w
UR  - http://hdl.handle.net/10044/1/75152
VL  - 8
ER  -
Download