Anti-idiotypic antibodies: a new approach in prion research

Venturini, Anja Colja; Bresjanac, Maja; Vranac, Tanja; Koren, Simon; Narat, Mojca; Popović, Mara; Šerbec, Vladka Čurin

doi:10.1186/1471-2172-10-16

Cited by 8 publications

(5 citation statements)

References 55 publications

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“…Paraprotein, as an idiotype protein, is expressed on the cell membrane of malignant plasma cells in the MRD stage of multiple myeloma (107). The idiotype involves the presence of a specific set of antigen-binding sites which characterizes an antibody produced by a particular clone (108). The paraprotein sequence is unique to an individual, which makes paraprotein valuable tumor antigens to develop personalized targeted radionuclides.…”

Section: Targeted Radionuclide Therapy With Vhhsmentioning

confidence: 99%

Single domain Camelid antibody fragments for molecular imaging and therapy of cancer

Li,

Hoefnagel,

Krishnadath

2023

Front. Oncol.

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Despite innovations in cancer therapeutics, cancer remains associated with high mortality and is one of biggest health challenges worldwide. Therefore, developing precise cancer imaging and effective treatments is an unmet clinical need. A relatively novel type of therapeutics are heavy chain variable domain antibody fragments (VHHs) derived from llamas. Here, we explored the suitability of VHHs for cancer imaging and therapy through reviewing the existing literature. We searched the MEDLINE, EMBASE and Cochrane databases and identified 32 papers on molecular imaging and 41 papers on therapy that were suitable for comprehensive reviewing. We found that VHHs harbor a higher specificity and affinity compared to mAbs, which contributes to high-quality imaging and less side-effects on healthy cells. The employment of VHHs in cancer imaging showed remarkably shorter times between administration and imaging. Studies showed that 18F and 99mTc are two optimal radionuclides for imaging with VHHs and that site-specific labelling is the optimal conjugation modality for VHHs with radionuclide or fluorescent molecules. We found different solutions for reducing kidney retention and immunogenicity of VHHs. VHHs as anticancer therapeutics have been tested in photodynamic therapy, targeted radionuclide therapy, immunotherapy and molecular targeted therapy. These studies showed that VHHs target unique antigen epitopes, which are distinct from the ones recognized by mAbs. This advantage means that VHHs may be more effective for targeted anticancer therapy and can be combined with mAbs. We found that high cellular internalization and specificity of VHHs contributes to the effectiveness and safety of VHHs as anticancer therapeutics. Two clinical trials have confirmed that VHHs are effective and safe for cancer imaging and therapy. Together, VHHs seem to harbor several advantages compared to mAbs and show potential for application in personalized treatment for cancer patients. VHH-based imaging and therapy are promising options for improving outcomes of cancer patients.

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Section: Targeted Radionuclide Therapy With Vhhsmentioning

confidence: 99%

Single domain Camelid antibody fragments for molecular imaging and therapy of cancer

Li,

Hoefnagel,

Krishnadath

2023

Front. Oncol.

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“…Generally, animals are immunized with antibodies particular for a given antigen for the development of anti-idiotypes. Biochemically antibodies are defined on the basis of their idiotypic counterparts [7]. Functional characteristics of antibodies particularly idiotype expression and identification of antigen are determined by the structural organization of antibodies.…”

Section: Concept Of Idiotype and Anti-idiotype Antibodiesmentioning

confidence: 99%

Recapitulation of the anti-Idiotype antibodies as vaccine candidate

et al. 2018

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The foreign antigen that enters into the body is detected by the immune system through antigen presenting cells leading to the production of antibodies. The use of anti-idiotype antibodies is a new way to excite the immune response that identifies and eliminates the foreign antigens entered into the body. These Anti-idiotype antibodies have the ability to decrease the non-specific binding of the antigenic protein epitopes because of high specificity for the antigenic determinants. The anti-idiotype antibodies attach to the paratope of idiotype antibody and stimulate a precise immune reaction same as that of external antigen. The anti-idiotype antibodies are the peerless therapeutic candidate as they mimic the antigenic structure and potentiate antibody and cell-mediated immunity. Even in the absence of foreign antigen, these anti-idiotype antibodies have the potential to provide long-lasting immunity. The present review is about immune regulations by anti-idiotype antibodies with some success therapeutic stories. The previous research analysis is evidence of anti-idiotype antibodies as an excellent candidate for the development of both human and animal vaccines although it has some gaps that are needed to be addressed.

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“…Recent evidence has shown that Ab2s are more effectively induced by the Fab fragment of V5B2 than by the entire antibody, or by the Fab fragment that binds to the keyhole limpet hemocyanin (KLH) antigen [8]. The Ab2s 5D12 and 4F8 are induced by the V5B2-Fab fragment, and these Ab2s have such high affinity for V5B2 that they can competitively inhibit the binding of the P1 immunogen.…”

Section: Anti-idiotypic (Anti-id) Antibodiesmentioning

confidence: 99%

Progress in the development of therapeutic antibodies targeting prion proteins and β-amyloid peptides

Zhang

Hong

2010

Sci. China Life Sci.

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Prion diseases and Alzheimer's disease (AD) are characterized by protein misfolding, and can lead to dementia. However, prion diseases are infectious and transmissible, while AD is not. The similarities and differences between these diseases have led researchers to perform comparative studies. In the last 2 decades, progress has been made in immunotherapy using anti-prion protein and anti-beta-amyloid antibodies. In this study, we review new ideas and strategies for therapeutic antibodies targeting prion diseases and AD through conformation dependence.

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Anti-idiotypic antibodies: a new approach in prion research

Cited by 8 publications

References 55 publications

Single domain Camelid antibody fragments for molecular imaging and therapy of cancer

Single domain Camelid antibody fragments for molecular imaging and therapy of cancer

Recapitulation of the anti-Idiotype antibodies as vaccine candidate

Progress in the development of therapeutic antibodies targeting prion proteins and β-amyloid peptides

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