Research and Reports on Genetics

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Mini Review - Research and Reports on Genetics (2023) Volume 5, Issue 2

Revolutionizing Targeted Therapy and Disease Treatment on Monoclonal Antibodies

Michael Kinch *

Department of Biomedical, University of Technology, Netherland.

*Corresponding Author:
Michael Kinch
Department of Biomedical,
University of Technology
Netherland
E-mail:michael.kinch@liu.edu

Received:25-Feb-2023,Manuscript No. AARRGS-23-90056; Editor assigned:28-Feb-2023,PreQC No. AARRGS-23-90056(PQ); Reviewed:14-Mar-2023,QC No. AARRGS-23-90056; Revised:18-Mar-2023, Manuscript No. AARRGS-23-90056(R); Published:25-Mar-2023,DOI:10.35841/aarrgs-5.2.137

Citation: Kinch M. Revolutionizing targeted therapy and disease treatment on monoclonal antibodies. J Res Rep Genet.2023;5(2):137

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Abstract

Monoclonal antibodies are a type of protein that is produced in the laboratory to mimic the natural antibodies that our immune system produces to fight off infections. These antibodies are designed to recognize and bind to specific antigens on the surface of cells, viruses, or bacteria, thereby triggering an immune response that can destroy the invading pathogen. Monoclonal antibodies have been used in a wide range of applications, from cancer treatment to autoimmune disease therapy to infectious disease prevention and treatment.

Introduction

Monoclonal antibodies, also known as mAbs, are laboratory-produced antibodies that are designed to mimic the natural immune response of the body to fight against harmful pathogens, such as bacteria, viruses, and cancer cells. Monoclonal antibodies are unique in their ability to target specific proteins on the surface of cells, making them a powerful tool in both diagnosis and treatment of diseases. In this article, we will explore the science behind monoclonal antibodies, their uses, and their potential impact on healthcare.

Mechanism of Action

Monoclonal antibodies work by recognizing and binding to specific antigens on the surface of cells, viruses, or bacteria. This binding can trigger a range of immune responses, including. The antibody can block the antigen's ability to enter or infect a host cell, thereby preventing the spread of the infection. The antibody can tag the antigen for destruction by immune cells, such as macrophages, which engulf and destroy the tagged cell. The antibody can activate the complement system, which is a set of proteins that can destroy the antigen by creating holes in its cell membrane. Antibody-Dependent Cell-mediated Cytotoxicity (ADCC): The antibody can bind to immune cells, such as natural killer (NK) cells, which then recognize and destroy the tagged cell. The antibody can trigger programmed cell death in the tagged cell, which can be useful in treating cancer. Monoclonal antibodies have a wide range of applications in medicine, research, and industry.[1].

Monoclonal antibodies are used to treat various types of cancer, including breast cancer, colorectal cancer, and leukemia. These antibodies can target specific antigens on cancer cells, triggering an immune response that can destroy the cancerous cells. Examples of monoclonal antibody drugs used in cancer therapy include trastuzumab, which targets the HER2 protein in breast cancer, and rituximab, which targets the CD20 protein in B-cell lymphoma. Monoclonal antibodies are used to treat autoimmune diseases, such as rheumatoid arthritis, psoriasis, and multiple sclerosis. These antibodies can target specific immune cells or proteins that are involved in the autoimmune response, thereby reducing inflammation and disease symptoms. Examples of monoclonal antibody drugs used in autoimmune disease therapy include adalimumab, which targets Tumour Necrosis Factor (TNF) in rheumatoid arthritis, and natalizumab, which targets alpha-4 integrin in multiple sclerosis. Monoclonal antibodies can be used to prevent or treat infectious diseases, such as COVID-19.[2,3].

Antibodies are proteins produced by the immune system to recognize and neutralize foreign invaders, such as viruses and bacteria. Each antibody is designed to recognize a specific protein on the surface of the pathogen, called an antigen. When an antibody binds to an antigen, it triggers a series of events that lead to the destruction of the pathogen. Monoclonal antibodies are laboratory-produced antibodies that are designed to mimic the natural immune response of the body. They are created by fusing a specific type of immune cell, called a B cell, with a cancer cell to form a hybridoma cell. The hybridoma cell can produce large quantities of identical antibodies, which are then harvested and purified for use in diagnosis and treatment. The production of monoclonal antibodies starts with the identification of a specific antigen that is present on the surface of the pathogen or diseased cell. Once the antigen is identified, a mouse is immunized with the antigen to stimulate the production of antibodies. The B cells that produce the desired antibody are then isolated from the mouse and fused with a cancer cell to create the hybridoma cell. The hybridoma cell is then grown in a laboratory setting to produce large quantities of identical antibodies.[4,5].

Conclusion

Monoclonal antibodies have a wide range of uses in medicine, from diagnosis to treatment. They are commonly used in the diagnosis of infectious diseases and cancer, as well as in the treatment of autoimmune disorders and cancer. Monoclonal antibodies are used in diagnostic tests to detect the presence of specific antigens in the blood or tissue samples. For example, a monoclonal antibody may be used to detect the presence of a viral antigen in the blood of a patient with a suspected infection. These tests are highly specific and can detect very low levels of antigens, making them useful in early detection of diseases. Monoclonal antibodies have been approved for the treatment of various diseases, including cancer, autoimmune disorders, and infectious diseases. They work by binding to specific proteins on the surface of cells and triggering a response that leads to the destruction of the cell.

 

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