Maintenance of antigen‐specific immunological memory through variable regions of heavy and light chains of anti‐idiotypic antibody

Vani, Janakiraman; Nayak, R.; Shaila, M.S.

doi:10.1111/j.1365-2567.2006.02519.x

Cited by 17 publications

(17 citation statements)

References 48 publications

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“…Subsequently, idiotypic sites and combining sites of antibody overlap extensively by definition. It has been predicted that idiotypic sites exist inside the framework regions, and inside the variable region they play the role to reverse turn structure and the studies confirmed that framework regions contribute as recognition sites in the expression of idiotype [8]. Anti-idiotypes have the ability to block the binding of antigen to vaccinating-idiotypeexpressing antibody.…”

Section: Concept Of Idiotype and Anti-idiotype Antibodiesmentioning

confidence: 77%

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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Section: Concept Of Idiotype and Anti-idiotype Antibodiesmentioning

confidence: 77%

Recapitulation of the anti-Idiotype antibodies as vaccine candidate

et al. 2018

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“…These interactions between T and B cells create an antigen-independent cooperation between T cells and B cells called Id-driven T-B cell collaboration, permitting continuous activation of both Tand B cells even in the absence of antigen [19,24–27]. This antigen-independent cooperation is an essential part of the “Relay Hypothesis” a mechanism proposed to account for the maintenance of the immunological memory in the absence of antigen [28,29]. …”

Section: Development Of An Immune Response To Antibodiesmentioning

confidence: 99%

Protective role of anti-idiotypic antibodies in autoimmunity – Lessons for type 1 diabetes

Hampe

2012

Autoimmunity

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Circulating autoantibodies to beta cell antigens are present in the majority of patients with Type 1 diabetes. These autoantibodies can be detected before and at time of clinical diagnosis of disease. Although the role of autoantibodies in the pathogenesis of the disease is debated, their presence indicates a dysregulation of the humoral immune response. Mechanisms regulating autoantibodies in Type 1 diabetes are not well understood. In contrast, in other autoimmune diseases there is acceptance that autoantibodies are regulated not only by antigen but also by other antibodies that bind to the antigen-binding site of these autoantibodies (anti-idiotypic antibodies). The proposed purpose of this network is to maintain an equilibrium between autoantibodies and their anti-idiotypic antibodies, preventing autoimmunity, while allowing a robust response to exogenous antigen. Anti-idiotypic antibodies regulate both autoantibody binding and their levels by a) neutralizing autoantibodies, and b) inhibiting the secretion of autoantibodies. Because it has been proposed that the B lymphocytes that produce autoantibodies function as autoantigen presenting cells, inhibiting their binding to autoantigen by anti-idiotypic antibodies may prevent development of autoimmune disease. This hypothesis is supported by the presence of anti-idiotypic antibodies in healthy individuals and in patients in remission from autoimmune diseases, and by the lack of anti-idiotypic antibodies during active disease. We recently reported the presence of autoantibodies to glutamate decarboxylase in the majority of healthy individuals, where their binding to autoantigen is prevented by anti-idiotypic antibodies. These anti-idiotypic antibodies are absent at clinical diagnosis of Type 1 diabetes, revealing the presence of autoantibodies. Type 1 diabetes (T1D) is an autoimmune disease characterized by the dysfunction and destruction of insulin-producing beta cells by autoreactive T cells. Although much progress has been made towards understanding the respective roles of effector and regulatory T cells in this beta cell destruction, the development of autoantibodies to beta cell proteins is widely considered simply a by-product of the autoimmune destruction of the beta cells, rather than having an active role in the pathogenesis. This view is starting to change based on increasing recognition that autoantibodies can have defined roles in other autoimmune diseases, and the emergence of new data on their role in T1D. This exploration of the role of autoantibodies in autoimmune disease has been spurred, in part, by increasing recognition that development of autoimmune diseases is influenced by regulatory antibodies (anti-idiotypic antibodies) directed against the unique binding site of autoantibodies. This review provides an overview of the development and function of these anti-idiotypic antibodies, and present evidence supporting their role in the development of autoimmune diseases. Finally, we conclude this review with a model of the events that may cause ...

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“…H protein is a protective antigen of the virus and is one of the envelope glycoproteins. We have previously produced and characterized an anti-idiotypic monoclonal antibody (Ab 2 ) D9D8 (Vani et al, 2007a) generated using a monoclonal antibody A12A9 (Ab 1 ) specific for H protein . D9D8 behaves as an 'internal image' of H protein as shown by its ability to induce antianti-idiotypic antibodies (Ab 3 ) in mice and rats (Vani et al, 2007a).…”

Section: Introductionmentioning

confidence: 99%

“…We have previously produced and characterized an anti-idiotypic monoclonal antibody (Ab 2 ) D9D8 (Vani et al, 2007a) generated using a monoclonal antibody A12A9 (Ab 1 ) specific for H protein . D9D8 behaves as an 'internal image' of H protein as shown by its ability to induce antianti-idiotypic antibodies (Ab 3 ) in mice and rats (Vani et al, 2007a). It has also been shown to mimic H protein in terms of both B and T cell responses (Vani et al, 2007a) suggesting that besides the functional homology, a structural homology may be underlying the Ab 1 defined H-epitope mimicry by the Ab 2 D9D8.…”

Section: Introductionmentioning

confidence: 99%

“…D9D8 behaves as an 'internal image' of H protein as shown by its ability to induce antianti-idiotypic antibodies (Ab 3 ) in mice and rats (Vani et al, 2007a). It has also been shown to mimic H protein in terms of both B and T cell responses (Vani et al, 2007a) suggesting that besides the functional homology, a structural homology may be underlying the Ab 1 defined H-epitope mimicry by the Ab 2 D9D8. In the variable regions of D9D8, regions with primary sequence similarity with the epitope on H were detected.…”

Section: Introductionmentioning

confidence: 99%

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Structural basis for the function of anti-idiotypic antibody in immune memory

Vani

Chatterjee

Shaila

et al. 2009

Molecular Immunology

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We had earlier proposed a hypothesis to explain the mechanism of perpetuation of immunological memory based on the operation of idiotypic network in the complete absence of antigen. Experimental evidences were provided for memory maintenance through anti-idiotypic antibody (Ab(2)) carrying the internal image of the antigen. In the present work, we describe a structural basis for such memory perpetuation by molecular modeling and structural analysis studies. A three-dimensional model of Ab(2) was generated and the structure of the antigenic site on the hemagglutinin protein H of Rinderpest virus was modeled using the structural template of hemagglutinin protein of Measles virus. Our results show that a large portion of heavy chain containing the CDR regions of Ab(2) resembles the domain of the hemagglutinin housing the epitope regions. The similarity demonstrates that an internal image of the H antigen is formed in Ab(2), which provides a structural basis for functional mimicry demonstrated earlier. This work brings out the importance of the structural similarity between a domain of hemagglutinin protein to that of its corresponding Ab(2). It provides evidence that Ab(2) is indeed capable of functioning as surrogate antigen and provides support to earlier proposed relay hypothesis which has provided a mechanism for the maintenance of immunological memory.

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Maintenance of antigen‐specific immunological memory through variable regions of heavy and light chains of anti‐idiotypic antibody

Cited by 17 publications

References 48 publications

Recapitulation of the anti-Idiotype antibodies as vaccine candidate

Recapitulation of the anti-Idiotype antibodies as vaccine candidate

Protective role of anti-idiotypic antibodies in autoimmunity – Lessons for type 1 diabetes

Structural basis for the function of anti-idiotypic antibody in immune memory

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