RT Journal Article
SR Electronic
T1 Antibody Display of cell surface receptor Tetraspanin12 and SARS-CoV-2 spike protein
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2021.05.29.446300
DO 10.1101/2021.05.29.446300
A1 Fu-Lien Hsieh
A1 Tao-Hsin Chang
YR 2021
UL http://biorxiv.org/content/early/2021/05/30/2021.05.29.446300.abstract
AB In previous work, Hsieh and Higgins presented a novel structure of antibodies identified from malaria-exposed individuals, in which the extracellular immunoglobulin (Ig)-like domain of leukocyte-associated immunoglobulin-like receptor 1 (LAIR1) is presented on the third complementarity determining regions (CDR3) of the Ig heavy chain. Here we develop an Antibody Display technology based on this LAIR1-containing antibody, by grafting proteins of interest (POI) onto the heavy chain CDR3 while retaining the biological properties of the POI. As a proof of principle, we displayed the second extracellular domain of Tetraspanin12 (Tspan12EC2) and the receptor-binding domain (RBD) of SARS-CoV-2 spike protein on the heavy chain CDR3. Our data revealed that Antibody Display Tspan12EC2 bound to Norrie Disease Protein (Norrin) and Antibody Display SARS-CoV-2 RBD bound to angiotensin-converting enzyme 2 (ACE2) and neutralizing nanobodies. Collectively, Antibody Display technology offers the general strategy of designing novel antibodies by grafting POI onto the CDR3.Competing Interest StatementThe authors have declared no competing interest.