Ling WL

Role of the IgE variable heavy chain in FcεRIa and superantigen binding in allergy and immunotherapy

Published date : 14 Apr 2019

Background
Variable heavy chain (VH) family frameworks (FWRs) have been reported to affect antibody receptor and superantigen binding; however, such effects in IgE remain largely unknown. Given that VH family biases have been previously reported in IgE of certain allergies, there is a need to investigate this phenomenon for biotechnological and therapeutic purposes.

type
Journal Paper
journal
Journal of Allergy and Clinical Immunology, April 2019, doi : 10.1016/j.jaci.2019.03.028
Impact Factor
13.258

Allosteric Effects between the Antibody Constant and Variable Regions: A Study of IgA Fc Mutations on Antigen Binding

Published date : 08 Jun 2018

Therapeutic antibodies have shifted the paradigm of disease treatments from small molecules to biologics, especially in cancer therapy. Despite the increasing number of antibody candidates, much remains unknown about the antibody and how its various regions interact. Recent findings showed that the antibody constant region can govern localization effects that are useful in reducing side effects due to systemic circulation by the commonly used IgG isotypes. Given their localized mucosal effects, IgA antibodies are increasingly promising therapeutic biologics.

type
Journal Paper
journal
Antibodies 2018, 7(2), 20, doi: 10.3390/antib7020020

Effect of VH–VL Families in Pertuzumab and Trastuzumab Recombinant Production, Her2 and FcγIIA Binding

Published date : 14 Mar 2018

Many therapeutic antibodies are humanized from animal sources. In the humanization process, complementarity determining region grafting is tedious and highly prone to failure. With seven known VH families, and up to six known κ VL families, there are choices aplenty. However, the functions of these families remain largely enigmatic. To study the role of these V-region families, we made 84 recombinant combinations of the various VH and VL family whole IgG1 variants of both Trastuzumab and Pertuzumab.

type
Journal Paper
journal
Frontiers in Immunology, 12 March 2018, Vol. 9, Article: 469, doi: org/10.3389/fimmu.2018.00469
Impact Factor
6.429

The effects of Antibody Engineering CH and CL in Trastuzumab and Pertuzumab recombinant models: Impact on antibody production and antigen-binding

Published date : 15 Jan 2018

Current therapeutic antibodies such as Trastuzumab, are typically of the blood circulatory IgG1 class (Cκ/ CHγ1). Due to the binding to Her2 also present on normal cell surfaces, side effects such as cardiac failure can sometimes be associated with such targeted therapy. Using antibody isotype swapping, it may be possible to reduce systemic circulation through increased tissue localization, thereby minimising unwanted side effects. However, the effects of such modifications have yet to be fully characterized, particularly with regards to their biophysical properties in antigen binding.

type
Journal Paper
journal
Scientific Reports 8, Article no 718, 2018, doi:10.1038/s41598-017-18892-9
Impact Factor
4.259

The role of Antibody Vκ Framework 3 region towards Antigen binding: Effects on recombinant production and Protein L binding

Published date : 19 Jun 2017

Antibody research has traditionally focused on heavy chains, often neglecting the important complementary role of light chains in antibody formation and secretion. In the light chain, the complementarity-determining region 3 (VL-CDR3) is specifically implicated in disease states. By modulating VL-CDR3 exposure on the scaffold through deletions in the framework region 3 (VL-FWR3), we further investigated the effects on secretion in recombinant production and antigen binding kinetics.

type
Journal Paper
journal
Scientific Reports 7, Article no: 3766 (2017), doi:10.1038/s41598-017-02756-3
Impact Factor
4.259

Discovery of a novel splice variant of Fcar (CD89) unravels sequence segments necessary for efficient secretion: a story of bad signal peptides and good ones that nevertheless do not make it

Published date : 19 Jan 2017

The IgA receptor, Fcar (CD89) consists of five sequence segments: two segments (S1, S2) forming the potential signal peptide, two extracellular EC domains that include the IgA binding site, and the transmembrane and cytoplasmic tail (TM/C) region. Numerous Fcar splice variants have been reported with various combinations of the sequence segments mentioned above. Here, we report a novel splice variant termed variant APD isolated from a healthy volunteer that lacks only the IgA-binding EC1 domain.

type
Journal Paper
journal
Cell Cycle 2016, doi: 10.1080/15384101.2017.1281480
Impact Factor
3.952

Structural analyses of 2015-updated drugresistant mutations in HIV-1 protease: an implication of protease inhibitor crossresistance

Published date : 16 Dec 2016

Background: Strategies to control HIV for improving the quality of patient lives have been aided by the Highly Active Anti-Retroviral Therapy (HAART), which consists of a cocktail of inhibitors targeting key viral enzymes. Numerous new drugs have been developed over the past few decades but viral resistances to these drugs in the targeted viral enzymes are increasingly reported. Nonetheless the acquired mutations often reduce viral fitness and infectivity.

type
Journal Paper
journal
BMC Bioinformatics 2016, 17(Suppl 19):500 doi: 10.1186/s12859-016-1372-3
Impact Factor
2.435

Fast Reversible Single-Step Method for Enhanced Band Contrast of Polyacrylamide Gels for Automated Detection

Published date : 17 Mar 2015

Staining SDS-PAGE is commonly used in protein analysis for many downstream characterization processes. Although staining and de-staining protocols can be adjusted, they can be laborious, and faint bands often become false negatives. Similarly, these faint bands hinder automated software band detections that are necessary for quantitative analyses. To overcome these problems, we describe a single-step rapid and reversible method to increase (up to 500%) band contrast in stained gels.

type
Journal Paper
journal
Electrophoresis 2015, doi: 10.1002/elps.201500094