(2021) Isolation and characterization of a novel nanobody for detection of GRP78 expressing cancer cells. Biotechnology and Applied Biochemistry. pp. 239-246. ISSN 0885-4513
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Abstract
Glucose-regulated protein 78 (GRP78) is an endoplasmic reticulum (ER) chaperone that has been shown that is overexpressed in cancer cells. Overexpression of GRP78 on cancer cells makes this molecule a suitable candidate for cancer detection and targeted therapy. VHH is the binding fragment of camelid heavy-chain antibodies also known as "nanobody." The aim of this study is to isolate and produce a new recombinant nanobody using phage display technique to detect cancer cells. Using the c-terminal domain of GRP78 (CGRP) as an antigen, four rounds of biopanning were performed, and high-affinity binders were selected by ELISA. Their affinity and functionality were characterized by surface plasmon resonance (SPR) cell ELISA and immunocytochemistry. A unique nanobody named V80 was purified. ELISA and SPR showed that this antibody had high specificity and affinity to the GRP78. Immunofluorescence analysis showed that V80 could specifically bind to the HepG2 and A549 cancer cell lines. This novel recombinant nanobody could bind to the cell surface of different cancer cells. After further evaluation, this nanobody can be used as a new tool for cancer detection and tumor therapy.
Item Type: | Article |
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Keywords: | glucose-regulated protein 78 Camelidae antibody cancer detection nanobody unfold protein response UNFOLDED PROTEIN RESPONSE ENDOPLASMIC-RETICULUM CHAPERONE BREAST-CANCER MONOCLONAL-ANTIBODY VARIABLE FRAGMENTS TERMINAL DOMAIN SURFACE GRP78 VHH NANOBODY BINDING IDENTIFICATION |
Page Range: | pp. 239-246 |
Journal or Publication Title: | Biotechnology and Applied Biochemistry |
Journal Index: | ISI |
Volume: | 68 |
Number: | 2 |
Identification Number: | https://doi.org/10.1002/bab.1916 |
ISSN: | 0885-4513 |
Depositing User: | Zahra Otroj |
URI: | http://eprints.mui.ac.ir/id/eprint/13965 |
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