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Article ; Online: A dual-functional oncolytic adenovirus ZD55-aPD-L1 scFv armed with PD-L1 inhibitor potentiates its antitumor activity.

Mei, Shengsheng / Peng, Shanshan / Vong, Eu Gene / Zhan, Jinbiao

2024 Volume 128, Page(s) 111579

Abstract: Background: Clinical data indicate that a substantial portion of cancer patients, though eligible for immune checkpoint inhibitor (ICI) therapy, cannot fully benefit from ICI monotherapy due to the poor immunogenicity of tumors and lack of tumor- ... ...

Abstract	Background: Clinical data indicate that a substantial portion of cancer patients, though eligible for immune checkpoint inhibitor (ICI) therapy, cannot fully benefit from ICI monotherapy due to the poor immunogenicity of tumors and lack of tumor-infiltrating lymphocytes within the 'cold' tumor microenvironment (TME). In addition to poor antibody penetrance into the TME, systemic delivery of ICIs is associated with immune-related adverse events (irAEs) among recipients, some of which are life-threatening. Oncolytic virotherapy is a potentially viable approach to improving the efficacy of ICI therapy because of their ability to selectively replicate and lyse tumor cells, release tumor-associated antigens (TAAs), induce inflammatory response and promote lymphocyte infiltration in tumors. Methods: A recombinant oncolytic adenoviruses (OAd), denoted ZD55-aPD-L1 scFv, which carried the expression cassette for anti-PD-L1 scFv was constructed by molecular cloning. Western blot and ELISA assay were performed to detect aPD-L1 scFv expression. Flow cytometry were used to analyse PD-L1 expression and count tumor cells. Co-culture assay of human peripheral blood mononuclear cells (PBMCs) with tumor cells in vitro and triple-negative breast cancer (TNBC) MDA-MB-231 tumor-bearing model in vivo were evaluated the antitumor effects of recombinant oncolytic adenoviruses ZD55-aPD-L1 scFv. Results: We found that cells infected with recombinant oncolytic adenovirus ZD55-aPD-L1 scFv can effectively express aPD-L1 scFv, which function similarly to its full-length anti-PD-L1 antibody. PBMCs have inherently very limited killing effect on tumor cells even with administration of anti-PD-L1 antibody as observed from our in vitro co-cultures. Treatment consisting of ZD55 alone or ZD55 combined with anti-PD-L1 antibody yielded mediocre antitumor efficacy in subsequent in vitro and in vivo investigations, but were all substantially surpassed by the synergistic antitumor effects observed with ZD55-aPD-L1 scFv treatment. We show that the concomitant direct oncolysis by the recombinant OAd and localized autocrine/paracrine interception of PD-1:PD-L1 checkpoint interaction mediated by ZD55-aPD-L1 scFv-infected cells is exceedingly superior to co-administration of ZD55 and anti-PD-L1 antibody in the human TNBC mice model. Conclusions: Our results provided evidence for the development of novel strategies, in this case an anti-PD-L1 scFv-armed OAd, to bolster immune responses to 'cold' tumors and to improve therapeutic responsiveness to ICIs.
MeSH term(s)	Animals ; Mice ; Humans ; Immune Checkpoint Inhibitors ; Adenoviridae ; B7-H1 Antigen ; Leukocytes, Mononuclear ; Triple Negative Breast Neoplasms ; Cell Line, Tumor ; Tumor Microenvironment
Chemical Substances	Immune Checkpoint Inhibitors ; B7-H1 Antigen
Language	English
Publishing date	2024-01-25
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2043785-7
ISSN	1878-1705 ; 1567-5769
ISSN (online)	1878-1705
ISSN	1567-5769
DOI	10.1016/j.intimp.2024.111579
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Article ; Online: Programmed cell death ligand-1: A dynamic immune checkpoint in cancer therapy.

Kalim, Muhammad / Iqbal Khan, Muhammad Saleem / Zhan, Jinbiao

Chemical biology & drug design

2020 Volume 95, Issue 6, Page(s) 552–566

Abstract: Antibody-based immunotherapies play a pivotal role in cancer research with efficient achievements in tumor suppression. Tumor survival is assisted by modulation of immune checkpoints to create imbalances between immune cells and cancer cell's environment. ...

Abstract	Antibody-based immunotherapies play a pivotal role in cancer research with efficient achievements in tumor suppression. Tumor survival is assisted by modulation of immune checkpoints to create imbalances between immune cells and cancer cell's environment. The modulation results in T-cell signal inhibition ultimately inert its proliferation and activation against various tumor cells. PD-L1, a 40 kDa transmembrane protein of B7 family, binds with PD-1 on the membrane of T cells which results in inhibition of T-cell proliferation and activation. PD-L1/PD-1 pathway has generated novel target sites for antibodies that can block PD-L1/PD-1 interactions. The blockage results in T-cell proliferation and tumor cell suppression. The PD-L1 immune checkpoint strategies' development, expression and regulations, signal inhibitions, and developmental stages of PD-L1/PD-1 antibodies are briefly discussed here in this review. All this information will provide a base for new therapeutic development against PD-L1 and PD-1 immune checkpoint interactions and will make available promising treatment options.
MeSH term(s)	Animals ; Antibodies, Monoclonal/chemistry ; Antibodies, Monoclonal/pharmacology ; Antineoplastic Agents/chemistry ; Antineoplastic Agents/metabolism ; Antineoplastic Agents/pharmacology ; Apoptosis/drug effects ; Cell Proliferation/drug effects ; Cytokines/metabolism ; Gene Expression Regulation/drug effects ; Humans ; Immune Checkpoint Inhibitors/chemistry ; Immune Checkpoint Inhibitors/metabolism ; Immune Checkpoint Inhibitors/pharmacology ; Immunotherapy/methods ; Ligands ; Lymphocyte Activation/drug effects ; Pharmaceutical Preparations/chemistry ; Programmed Cell Death 1 Receptor/antagonists & inhibitors ; Programmed Cell Death 1 Receptor/genetics ; T-Lymphocytes/drug effects ; T-Lymphocytes/immunology
Chemical Substances	Antibodies, Monoclonal ; Antineoplastic Agents ; Cytokines ; Immune Checkpoint Inhibitors ; Ligands ; Pharmaceutical Preparations ; Programmed Cell Death 1 Receptor
Language	English
Publishing date	2020-03-28
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2216600-2
ISSN	1747-0285 ; 1747-0277
ISSN (online)	1747-0285
ISSN	1747-0277
DOI	10.1111/cbdd.13677
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Article ; Online: Dynamics of Endocytosis and Degradation of Antibody-Drug Conjugate T-DM1 in HER2 Positive Cancer Cells.

Liang, Keying / Mei, Shengsheng / Gao, Xiangzheng / Peng, Shanshan / Zhan, Jinbiao

Drug design, development and therapy

2021 Volume 15, Page(s) 5135–5150

Abstract: Purpose: T-DM1 is an antibody-drug conjugate (ADC) consisting of trastuzumab and DM1 linked together. T-DM1 binds to human epidermal growth factor receptor-2 (HER2) in tumors and then triggers the endocytosis of T-DM1 and release of payload. Therefore, ... ...

Abstract	Purpose: T-DM1 is an antibody-drug conjugate (ADC) consisting of trastuzumab and DM1 linked together. T-DM1 binds to human epidermal growth factor receptor-2 (HER2) in tumors and then triggers the endocytosis of T-DM1 and release of payload. Therefore, endocytosis efficacy is considered as a critical step for the initiation of T-DM1 therapy; however, the endocytosis mechanism of T-DM1 remains poorly understood. Meanwhile, HER2 is regarded as an internalization-resistant receptor, which hinders the endocytosis and effectiveness of T-DM1. The present study is to explore the T-DM1 endocytosis pathway, which may provide insights into the internalization mechanism of ADCs and help to improve efficacy. Methods: Confocal microscopy and flow cytometry were used to analyse T-DM1 intracellular trafficking and endocytosis efficiency, while Western blot assay was performed to detect T-DM1 degradation. Results: We found that intracellular T-DM1 was increased to 50% within 12 h. T-DM1 was colocalized with cholera toxin B (CTxB), a lipid raft marker, within 2 h and then degraded in lysosome. Upon overexpression of caveolin-1 (CAV-1) and utilization of caveolae/lipid-raft disruptors, we found that temporal CAV-1 upregulation significantly facilitated T-DM1 endocytosis and degradation, whereas nystatin and lovastatin disrupted caveolae/lipid-raft structure and inhibited T-DM1 degradation. We demonstrate that T-DM1 internalizes through the lipid raft-mediated endocytosis in a CAV-1 dependent manner, rather than through the clathrin-mediated endocytosis in HER2-positive cancer cells. Conclusion: Our findings suggest that modulation of the caveolae/lipid-raft mediated endocytosis may be a possible option for improving the clinical therapeutic effect of T-DM1 because it plays a key role in regulating T-DM1 internalization.
MeSH term(s)	Ado-Trastuzumab Emtansine/pharmacology ; Breast Neoplasms/drug therapy ; Drug Resistance, Neoplasm/drug effects ; Endocytosis/drug effects ; Female ; Humans ; Immunoconjugates/pharmacology ; Receptor, ErbB-2 ; Stomach Neoplasms/drug therapy ; Tumor Cells, Cultured
Chemical Substances	Immunoconjugates ; ERBB2 protein, human (EC 2.7.10.1) ; Receptor, ErbB-2 (EC 2.7.10.1) ; Ado-Trastuzumab Emtansine (SE2KH7T06F)
Language	English
Publishing date	2021-12-24
Publishing country	New Zealand
Document type	Journal Article
ZDB-ID	2451346-5
ISSN	1177-8881 ; 1177-8881
ISSN (online)	1177-8881
ISSN	1177-8881
DOI	10.2147/DDDT.S344052
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Article ; Online: Bioengineering and computational analysis of programmed cell death ligand-1 monoclonal antibody.

Kalim, Muhammad / Ali, Hamid / Rehman, Ashfaq Ur / Lu, Yong / Zhan, Jinbiao

Frontiers in immunology

2022 Volume 13, Page(s) 1012499

Abstract: The trans-membrane proteins of the B7 family programmed cell death ligand-1 (PD-L1) and programmed death-1 (PD-1) play important roles in inhibiting immune responses and enhancing self-tolerance ... via ... T-cell modulation. Several therapeutic ... ...

Abstract	The trans-membrane proteins of the B7 family programmed cell death ligand-1 (PD-L1) and programmed death-1 (PD-1) play important roles in inhibiting immune responses and enhancing self-tolerance via T-cell modulation. Several therapeutic antibodies are used to promote T-cell proliferation by preventing interactions between PD-1/PD-L1. Recombinant technology appears to be quite useful in the production of such potent antibodies. In this study, we constructed recombinant molecules by cloning variable regions of the PD-L1 molecule into pMH3 vectors and transferring them into mammalian cell lines for expression. G418 supplementation was used to screen the recombinant clones, which were then maintained on serum-free medium. The full-length antibody was isolated and purified from the medium supernatant at a concentration of 0.5-0.8 mg/ml. Antibody binding affinity was investigated using ELISA and immunofluorescence methods. The protein-protein interactions (PPI) were determined using a docking approach. The SWISS model was utilized for homology modeling, while ZDOCK, Chimera, and PyMOL were used to validate 3D models. The Ramachandran plots were constructed using the SWISS model, which revealed that high-quality structures had a value of more than 90%. Current technologies allow for the accurate determination of antigen-antibody interactions.
MeSH term(s)	Animals ; Antibodies, Monoclonal/therapeutic use ; B7-H1 Antigen/metabolism ; Programmed Cell Death 1 Receptor/metabolism ; Ligands ; Bioengineering ; Apoptosis ; Mammals
Chemical Substances	Antibodies, Monoclonal ; B7-H1 Antigen ; Programmed Cell Death 1 Receptor ; Ligands
Language	English
Publishing date	2022-10-21
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2606827-8
ISSN	1664-3224 ; 1664-3224
ISSN (online)	1664-3224
ISSN	1664-3224
DOI	10.3389/fimmu.2022.1012499
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Article ; Online: RBD-specific single-chain antibody protects against acute lung injury in mice.

Peng, Shanshan / Husnain Raza Shah, Syed / Mei, Shengsheng / Gene Vong, Eu / Sun, Yisheng / Zhan, Jinbiao

International immunopharmacology

2023 Volume 124, Issue Pt B, Page(s) 111020

Abstract: As SARS-CoV-2 variants continue spreading globally, the discovery of broad spectrum therapeutically active antibodies with retaining good protective activity is a global priority. It was reported that infection with SARS-CoV-2 could cause acute lung ... ...

Abstract	As SARS-CoV-2 variants continue spreading globally, the discovery of broad spectrum therapeutically active antibodies with retaining good protective activity is a global priority. It was reported that infection with SARS-CoV-2 could cause acute lung injury (ALI) in clinical investigations. Therefore, we discovered that anti-RBD scFv is effective against SARS-CoV-2-induced ALI. To begin, we utilized the receptor binding domain (RBD) of spike glycoprotein as a target to produce single-chain antibodies (scFvs) through an intensive phage display technology. The binding affinity and inhibitory effect of the scFvs were evaluated via ELISA and flow cytometry. Moreover, anti-RBD scFv No.35 significantly prevented ALI caused by LPS and SARS-CoV-2 spike RBD protein in mouse model. Thus, the anti-RBD scFv will aid the development of potential antibody treatments and reduce the inflammatory response of SARS-CoV-2.
MeSH term(s)	Animals ; Mice ; Antibodies, Viral/therapeutic use ; Protein Binding ; Single-Chain Antibodies/therapeutic use ; Acute Lung Injury/drug therapy ; Antibodies, Neutralizing/therapeutic use
Chemical Substances	Antibodies, Viral ; Single-Chain Antibodies ; Antibodies, Neutralizing
Language	English
Publishing date	2023-10-07
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2043785-7
ISSN	1878-1705 ; 1567-5769
ISSN (online)	1878-1705
ISSN	1567-5769
DOI	10.1016/j.intimp.2023.111020
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Article: Expression and functional identification of recombinant SARS-CoV-2 receptor binding domain (RBD) from E. coli system

Gao, Xiangzheng / Peng, Shanshan / Mei, Shengsheng / Liang, Keying / Khan, Muhammad Saleem Iqbal / Vong, Eu Gene / Zhan, Jinbiao

Preparative biochemistry & biotechnology. 2022 Mar. 1, v. 52, no. 3

2022

Abstract: The receptor binding domain (RBD) of SARS-CoV-2 is located in the C-terminal of S1 subunit of the spike (S) protein which is responsible for recognizing and binding to the angiotensin-converting enzyme 2 (ACE2) receptor. The DNA encoding the SARS-CoV-2 ... ...

Abstract	The receptor binding domain (RBD) of SARS-CoV-2 is located in the C-terminal of S1 subunit of the spike (S) protein which is responsible for recognizing and binding to the angiotensin-converting enzyme 2 (ACE2) receptor. The DNA encoding the SARS-CoV-2 RBD was inserted into pET-28a (+) to construct expression plasmid pET-28a (+)/RBD. The desired RBD protein was produced in E. coli Rosetta (DE) and purified by a Ni-NTA column. The recombinant RBD was analyzed by SDS-PAGE and Western blot. The flow cytometry analysis indicated that the recombinant RBD is capable of binding to human ACE2 (hACE2) in the ACE2-overexpressed HEK293A-hACE2 cells. Our results demonstrated that recombinant RBD expressed in E. coli Rosetta (DE) strain has bioactivities and can be used as an antigen for diagnosis and as a tool for the development of novel anti-viral drugs against SASR-CoV-2.
Keywords	Escherichia coli ; Severe acute respiratory syndrome coronavirus 2 ; Western blotting ; antigens ; biotechnology ; flow cytometry ; humans ; peptidyl-dipeptidase A ; plasmids ; polyacrylamide gel electrophoresis
Language	English
Dates of publication	2022-0301
Size	p. 318-324.
Publishing place	Taylor & Francis
Document type	Article
ZDB-ID	1322522-4
ISSN	1532-2297 ; 1082-6068
ISSN (online)	1532-2297
ISSN	1082-6068
DOI	10.1080/10826068.2021.1941106
Database	NAL-Catalogue (AGRICOLA)

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Article: Virulent

Khan, Muhammad Saleem Iqbal / Gao, Xiangzheng / Liang, Keying / Mei, Shengsheng / Zhan, Jinbiao

Frontiers in microbiology

2021 Volume 12, Page(s) 706700

Abstract: Phage-host interactions are likely to have the most critical aspect of phage biology. Phages are the most abundant and ubiquitous infectious acellular entities in the biosphere, where their presence remains elusive. Here, the ... ...

Abstract	Phage-host interactions are likely to have the most critical aspect of phage biology. Phages are the most abundant and ubiquitous infectious acellular entities in the biosphere, where their presence remains elusive. Here, the novel
Language	English
Publishing date	2021-08-24
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2587354-4
ISSN	1664-302X
ISSN	1664-302X
DOI	10.3389/fmicb.2021.706700
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Article ; Online: An efficient system to generate truncated human angiotensin converting enzyme 2 (hACE2) capable of binding RBD and spike protein of SARS-CoV2.

Gao, Xiangzheng / Liang, Keying / Mei, Shengsheng / Peng, Shanshan / Vong, Eu Gene / Zhan, Jinbiao

Protein expression and purification

2021 Volume 184, Page(s) 105889

Abstract: Human angiotensin converting enzyme 2 (hACE2) mediates the cell entry of both SARS-CoV and SARS-CoV2 and can be used as a drug target. The DNA encoding the truncated hACE2 (30-356aa) was cloned into pET-28a (+) and expressed in Escherichia coli Rosetta ( ... ...

Abstract	Human angiotensin converting enzyme 2 (hACE2) mediates the cell entry of both SARS-CoV and SARS-CoV2 and can be used as a drug target. The DNA encoding the truncated hACE2 (30-356aa) was cloned into pET-28a (+) and expressed in Escherichia coli Rosetta (DE3). The recombinant hACE2 (rhACE2) was purified by affinity chromatography on a Ni-NTA column and characterized with SDS-PAGE and Western blot. The binding activity of rhACE2 to Spike protein of SARS-CoV2 was evaluated in S protein-overexpressed HEK293A cells (HEK293A-SP cells) through flow cytometry. The prokaryotic expression system is able to produce approximately 75 mg protein per liter, which would be useful for infection mechanism study, and drug screening and development of SARS-CoV2.
MeSH term(s)	Angiotensin-Converting Enzyme 2/chemistry ; Angiotensin-Converting Enzyme 2/genetics ; Angiotensin-Converting Enzyme 2/isolation & purification ; Angiotensin-Converting Enzyme 2/metabolism ; COVID-19/virology ; Chromatography, Affinity ; Cloning, Molecular ; Escherichia coli/genetics ; HEK293 Cells ; Humans ; Protein Binding ; Protein Domains ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/isolation & purification ; Recombinant Proteins/metabolism ; Spike Glycoprotein, Coronavirus/metabolism
Chemical Substances	Recombinant Proteins ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2 ; ACE2 protein, human (EC 3.4.17.23) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
Language	English
Publishing date	2021-04-11
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1055455-5
ISSN	1096-0279 ; 1046-5928
ISSN (online)	1096-0279
ISSN	1046-5928
DOI	10.1016/j.pep.2021.105889
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Article ; Online: Polyclonal antibody production against rGPC3 and their application in diagnosis of hepatocellular carcinoma.

Wang, Shenghao / Kalim, Muhammad / Liang, Keying / Zhan, Jinbiao

Preparative biochemistry & biotechnology

2018 Volume 48, Issue 5, Page(s) 435–445

Abstract: Glypican-3 (GPC3) is an integral membrane proteoglycan, which contains a core protein anchored to the cytoplasmic membrane through a glycosylphosphatidylinositol linkage. The glypican-3 can regulate the signaling pathways, thereby enhances cell division, ...

Abstract	Glypican-3 (GPC3) is an integral membrane proteoglycan, which contains a core protein anchored to the cytoplasmic membrane through a glycosylphosphatidylinositol linkage. The glypican-3 can regulate the signaling pathways, thereby enhances cell division, growth, and apoptosis in certain cell types. It is almost nonexistent on the surface of the human normal cell membrane and highly expresses on the membrane of hepatocellular carcinoma (HCC) cells. It has been well established that GPC3 provides a useful diagnostic marker. For generating the polyclonal antibody of GPC3, we expected that GPC3 N-terminal region (amino acid sequence 26-358) could be expressed in Escherichia coli system, however, no active expression was observed after IPTG induction. Interestingly, after deletion of six proline residues from position 26 to 31 in the N-terminus, expression of recombinant GPC3 was clearly detected. We further analyzed the expressed protein deprived of six prolines, to immunize the New Zealand male rabbits for production of active antibodies. The binding affinity of antibody was analyzed by immunofluorescence analysis, immunohistochemical detection, and western blotting. The functional GPC3 N-terminal protein recombinant development, expression, purification, and the polyclonal antibody have been generated provide the basis for the diagnosis of HCC in cancer therapy.
MeSH term(s)	Animals ; Antibodies/analysis ; Antibody Formation ; Biomarkers, Tumor/analysis ; Carcinoma, Hepatocellular/diagnosis ; Cell Line, Tumor ; Cloning, Molecular/methods ; Escherichia coli/genetics ; Fluorescent Antibody Technique ; Glypicans/analysis ; Glypicans/genetics ; Humans ; Liver Neoplasms/diagnosis ; Male ; Protein Domains ; Rabbits ; Recombinant Proteins/analysis ; Recombinant Proteins/genetics
Chemical Substances	Antibodies ; Biomarkers, Tumor ; GPC3 protein, human ; Glypicans ; Recombinant Proteins
Language	English
Publishing date	2018-05-28
Publishing country	England
Document type	Journal Article
ZDB-ID	1322522-4
ISSN	1532-2297 ; 1082-6068
ISSN (online)	1532-2297
ISSN	1082-6068
DOI	10.1080/10826068.2018.1452258
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Article: Efficient development and expression of scFv recombinant proteins against PD-L1 surface domain and potency in cancer therapy.

Kalim, Muhammad / Liang, Keying / Khan, Muhammad Saleem Iqbal / Zhan, Jinbiao

Cytotechnology

2019 Volume 71, Issue 3, Page(s) 705–722

Abstract: PD-L1 is a 40 kDa trans-membrane protein of B7 family and an important T cell regulator. Binding of PD-L1 and PD-1 inhibits proliferation and activation of T cell results cell exhaustion. This phenomenon can be reversed by blocking PD-L1/PD-1 ... ...

Abstract	PD-L1 is a 40 kDa trans-membrane protein of B7 family and an important T cell regulator. Binding of PD-L1 and PD-1 inhibits proliferation and activation of T cell results cell exhaustion. This phenomenon can be reversed by blocking PD-L1/PD-1 interactions with single chain variables fragment (scFv) fusion proteins and by direct inhibition of tumor cells with drug conjugates. The human phage-displayed scFv library was utilized to generate scFv against the PD-L1 antigen by affinity bio-panning. The positive clones were selected by continuous transfection of bacterial cells and sequence analysis. The binding affinity and specificity of the scFv and antibody fragments were determined by using surface plasmon resonance biosensor, western blot analysis, and immunofluorescence assay. After three rounds of panning selection, about 30% of clones have a binding affinity with targeted PD-L1 antigen. Eight positive clones with accurate sequences were isolated and analyzed for binding affinity with PD-L1 antigen. Three of those with accurate sequences and binding affinity were selected for the recombinant formation and soluble expression by Escherichia coli host machinery. The highly positive recombinant clones with the exact orientation of FR and CDR domains were developed and can be used as a drug carrier tools in ADC formation or direct inhibition of immune checkpoint in cancer immunotherapy. The conjugate achieved its initial potency and need efficient improvement to enhance direct tumor suppression and bio-therapeutics strategies enrichment.
Language	English
Publishing date	2019-05-16
Publishing country	United States
Document type	Journal Article
ZDB-ID	1035772-5
ISSN	0920-9069
ISSN	0920-9069
DOI	10.1007/s10616-019-00316-3
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