Therapeutic Antibodies ‐ From Past to Future

Dübel, Stefan; Reichert, Janice M.

doi:10.1002/9783527619740.ch1

Cited by 3 publications

(2 citation statements)

References 8 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…

In 1975, Köhler and Milstein published their seminal manuscript on hybridoma technology enabling the production of mouse monoclonal antibodies (mAbs) 1,2 . Since then, technical advances have allowed the transition from mouse, via chimeric and humanized, to fully human mAbs 3,4 , with a reduction in potentially immunogenic mouse components (FIG. 1a).

…”

mentioning

confidence: 99%

The safety and side effects of monoclonal antibodies

Hansel

Kropshofer

Singer

et al. 2010

Nat Rev Drug Discov

932

671

View full text Add to dashboard Cite

Monoclonal antibodies (mAbs) are now established as targeted therapies for malignancies, transplant rejection, autoimmune and infectious diseases, as well as a range of new indications. However, administration of mAbs carries the risk of immune reactions such as acute anaphylaxis, serum sickness and the generation of antibodies. In addition, there are numerous adverse effects of mAbs that are related to their specific targets, including infections and cancer, autoimmune disease, and organ-specific adverse events such as cardiotoxicity. In March 2006, a life-threatening cytokine release syndrome occurred during a first-in-human study with TGN1412 (a CD28-specific superagonist mAb), resulting in a range of recommendations to improve the safety of initial human clinical studies with mAbs. Here, we review some of the adverse effects encountered with mAb therapies, and discuss advances in preclinical testing and antibody technology aimed at minimizing the risk of these events.

show abstract

“…

…”

mentioning

confidence: 99%

The safety and side effects of monoclonal antibodies

Hansel

Kropshofer

Singer

et al. 2010

Nat Rev Drug Discov

932

671

View full text Add to dashboard Cite

show abstract

“…The molecular mass of IgG is approximately 160 kDa, which happens to be due to the presence of light and heavy chains each being two in number [ 10 , 11 ]. The fragment antigen binding (Fab) region present inside the IgG structure contains a paratope and can help in pathogen inhibition through recognition events whereas the fragment crystallizable (Fc) region is in charge of the interaction with different accessory molecules to moderate indirect effector operations, including the complement–dependent cytotoxicity mechanism (CDC), antibody-dependent cellular cytotoxicity, and phagocytosis (ADCC and ADCP) [ 12 , 13 ].…”

Section: Introductionmentioning

confidence: 99%

Emerging Methods in Biosensing of Immunoglobin G—A Review

Azam

Bukhari

Liaqat

et al. 2023

Sensors

View full text Add to dashboard Cite

Human antibodies are produced due to the activation of immune system components upon exposure to an external agent or antigen. Human antibody G, or immunoglobin G (IgG), accounts for 75% of total serum antibody content. IgG controls several infections by eradicating disease-causing pathogens from the body through complementary interactions with toxins. Additionally, IgG is an important diagnostic tool for certain pathological conditions, such as autoimmune hepatitis, hepatitis B virus (HBV), chickenpox and MMR (measles, mumps, and rubella), and coronavirus-induced disease 19 (COVID-19). As an important biomarker, IgG has sparked interest in conducting research to produce robust, sensitive, selective, and economical biosensors for its detection. To date, researchers have used different strategies and explored various materials from macro- to nanoscale to be used in IgG biosensing. In this review, emerging biosensors for IgG detection have been reviewed along with their detection limits, especially electrochemical biosensors that, when coupled with nanomaterials, can help to achieve the characteristics of a reliable IgG biosensor. Furthermore, this review can assist scientists in developing strategies for future research not only for IgG biosensors but also for the development of other biosensing systems for diverse targets.

show abstract

Review on Antibody as A Drug of Choice

Yimer¹,

Mideksa²,

Ferede³

2017

Arch Vet Sci Technol

View full text Add to dashboard Cite

During the last 20 years, infectious diseases have indeed made a staggering comeback for a variety of reasons, including resistance against existing antibiotics. As a consequence, several alternatives to antibiotics are currently being considered or reconsidered. The modification of antibodies is of major interest since changes in their functionality and physico-chemical properties will broaden their application area. The features that make antibodies attractive drug candidates are high target specificity and their organization into distinct structural and functional domains. Antibody therapy has an increasing number of applications in which it is possible to use inexpensive sources of animal antibodies, such as bovine colostral antibodies and egg yolk antibodies. A powerful way to fight infections in our days will be to use immune system as complement or replacement to antibiotics. The immune system and microorganisms have coexisted for millions of years and microorganisms have not become resistant towards them. But, its use is less than expected value still in developing countries including Ethiopia. Therefore, it is better if therapeutic and prophylactic antibodies are considered rather than antibiotics.

show abstract

Therapeutic Antibodies ‐ From Past to Future

Cited by 3 publications

References 8 publications

The safety and side effects of monoclonal antibodies

The safety and side effects of monoclonal antibodies

Emerging Methods in Biosensing of Immunoglobin G—A Review

Review on Antibody as A Drug of Choice

Contact Info

Product

Resources

About