A Precisely Designed Immunotoxin Against VCAM1 Consisting of a Humanized Antibody Variable Domain Fused to Granzyme: An In Silico Approach

BackgroundProgrammed death-ligand 1 (PD-L1), also called B7 homolog 1 (B7-H1), is a human protein playing an important biomarker role in highly proliferation cells (like cancer cells) which is encoded by the CD274 gene. The interaction between PD-1 and PD-L1 inhibits T cell growth and cytokine secretion. Therefore, PD-L1 negatively regulates immune responses and permits tumor cells to evade immune surveillance.Thus, PD-L1 seems to be a suitable target for designing the immune-therapeutics. ResultsThe predicted structure of this protein indicated that the chains were linked by (Gly4Ser)3 linker. In that line, using different simulation software, the structure of Granzyme B (GrB), a serine protease exists in cytotoxic lymphocytes granules as an apoptosis mediator, was attached to its speci c antibody structure (Atezolizumab) via an adaptor sequence. Evaluation of accuracy, energy minimization and characterization of biological properties of the nal processed structure were done. Our computational outcomes showed that the method of employed structure prediction has been successfully managed to design the immunotoxin structure. ConclusionIt is necessary to mention that the precise and accurate design of the immune-therapeutic agents against cancer cells, can be con rmed by employed in-silico approach. So, using this method, we have designed a capable immunotoxin targeting the PD-L1 in an accurate orientation and cause the cancer cell destruction by its toxin domain.

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A Precisely Designed Immunotoxin Against VCAM1 Consisting of a Humanized Antibody Variable Domain Fused to Granzyme: An In Silico Approach

Cited by 4 publications

References 27 publications

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Computational Design and Analysis of a Poly-Epitope Fusion Protein: A New Vaccine Candidate for Hepatitis and Poliovirus

Expression and Purification of Membrane Proteins in Different Hosts

Atezolizumab and granzyme B as immunotoxin against PD-L1 antigen; an insilico study

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