Production and characterization of anti-peptide monoclonal antibodies with specificity for staphylococcal enterotoxins A and B

Bhatti, A. R.; Micusan, V. V.

doi:10.1016/s0167-7012(98)00110-9

Cited by 6 publications

(3 citation statements)

References 27 publications

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“…The identification of B-cell epitopes is rather important to immunotherapeutic and immunodetection applications because an epitope as the minimal immune unit is strong enough to elicit a potent humoral immune response without harmful side effects to the human body [30] . The most reliable methods for the identification of an epitope are monoclonal antibodies, X-ray crystallography and NMR techniques [26] , [31] – [33] . To date, only five linear B cell epitopes of SEB have been identified by these methods, among which the truncated SEB mutant A was used to confirm SEB 252-261 as an SEB epitope [25] ; the anti-peptide monoclonal antibodies were used to reveal SEB 96-103 as an SEB epitope [27] ; the anti-TSST-1 monoclonal antibodies were used to reveal SEB 110-119 as a cross epitope of SEB and TSST-1 [25] ; and SEB 28-41 and SEB 35-40 were identified as SEB epitopes using the commercial anti-SEB monoclonal antibody ab53981 by a phage display approach [24] .…”

Section: Discussionmentioning

confidence: 99%

Fine-Mapping of Immunodominant Linear B-Cell Epitopes of the Staphylococcus Aureus SEB Antigen Using Short Overlapping Peptides

Zhao

Sun

et al. 2014

PLoS ONE

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Staphylococcal enterotoxin B (SEB) is one of the most potent Staphylococcus aureus exotoxins (SEs). Due to its conserved sequence and stable structure, SEB might be a good candidate antigen for MRSA vaccines. Although cellular immune responses to SEB are well-characterized, much less is known regarding SEB-specific humoral immune responses, particularly regarding detailed epitope mapping. In this study, we utilized a recombinant nontoxic mutant of SEB (rSEB) and an AlPO4 adjuvant to immunize BALB/c mice and confirmed that rSEB can induce a high antibody level and effective immune protection against MRSA infection. Next, the antisera of immunized mice were collected, and linear B cell epitopes within SEB were finely mapped using a series of overlapping synthetic peptides. Three immunodominant B cell epitopes of SEB were screened by ELISA, including a novel epitope, SEB205-222, and two known epitopes, SEB97–114 and SEB247-261. Using truncated peptides, an ELISA was performed with peptide-KLH antisera, and the core sequence of the three immunodominant B cell epitopes were verified as SEB97-112, SEB207-222, and SEB247-257. In vitro, all of the immunodominant epitope-specific antisera (anti-SEB97-112, anti-SEB207-222 and anti-SEB247-257) were observed to inhibit SEB-induced T cell mitogenesis and cytokine production from splenic lymphocytes of BALB/c mice. The homology analysis indicated that SEB97–112 and SEB207-222 were well-conserved among different Staphylococcus aureus strains. The 3D crystal structure of SEB indicated that SEB97–112 was in the loop region inside SEB, whereas SEB207-222 and SEB247-257 were in the β-slice region outside SEB. In summary, the fine-mapping of linear B-cell epitopes of the SEB antigen in this study will be useful to understand anti-SEB immunity against MRSA infection further and will be helpful to optimize MRSA vaccine designs that are based on the SEB antigen.

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Section: Discussionmentioning

confidence: 99%

Fine-Mapping of Immunodominant Linear B-Cell Epitopes of the Staphylococcus Aureus SEB Antigen Using Short Overlapping Peptides

Zhao

Sun

et al. 2014

PLoS ONE

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“…Epitope mapping of crucial antigens has been a useful exercise that has been done using multiple methods, including monoclonal antibodies, X-ray crystallography and Nuclear magnetic resonance techniques [ 33 – 36 ]. For example, a peptide was identified from PfRH5 by virus-like particle (VLP) approach and a mAb to the peptide completely inhibited parasite invasion in vitro [ 17 ].…”

Section: Resultsmentioning

confidence: 99%

Characterization of fine specificity of the immune response to a Plasmodium falciparum rhoptry neck protein, PfAARP

Kalra

Mukherjee

Chauhan

2016

Malar J

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BackgroundImmunological characterization of potential blood-stage malaria antigens would be a valuable strategy in the development of an effective vaccine. Identifying B and CD4+ T cell epitopes will be important in understanding the nature of immune response. A previous study has shown that Plasmodium falciparum apical asparagine-rich protein (PfAARP) stimulates immune response and induces potent invasion-inhibitory antibodies. Antibodies to PfAARP provide synergistic effects in inhibition of parasite invasion when used in combination with antibodies to other antigens. In the present study, an attempt was made to identify B cell and CD4+ T cell epitopes of PfAARP.MethodsBalb/c mice were immunized with recombinant PfAARP and both cellular and humoral responses were analysed at various time points. Computerized databases [immune epitope database (IEDB) and B cell epitope prediction (BCEPred)] were used to predict epitope sequences within PfAARP and predicted peptides were synthesized. In addition, nine 18 amino acid, long-overlapping peptides spanning the entire length of PfAARP were synthesized. Using these peptides, B cell and CD4+ T cell responses in PfAARP immunized mice were measured by ELISA and ELISPOT assays.ResultsHere, it is demonstrated that immunization of mice with PfAARP induced long-lasting, high-titre antibodies (4 months post immunization). Also, the recombinant protein was effective in inducing a pronounced Th1 type of immune response quantified by IFN-γ ELISA and ELISPOT. It was found that the predicted peptides did not represent the immunogenic regions of PfAARP. However, of the nine overlapping peptides, three peptides (peptides 3, 5 and 7) were strongly recognized by PfAARP-immunized sera and represented B cell epitopes. Also, peptide 3 elicited IFN- γ response, suggesting it to be a T-cell epitope.ConclusionsInduction of long-lasting humoral and cellular response on PfAARP immunization in mice underscores its possible use as a blood-stage malaria vaccine candidate. Mapping of immunogenic regions may help in designing fusion chimera containing immunologically relevant regions of other vaccine target antigens and/or for multi-component vaccine candidates.

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“…One of the directions is convenient serological tests based on epitopes. As early as the last century, experiments have shown that ELISA methods for quantitative detection of toxins have been developed by selecting epitopes of S. aureus enterotoxins to synthesize peptides that can be used to produce mAbs [ 62 ]. Besides, it was found that the pentasacyl bridge of peptidoglycan of S. aureus has high antigenic specificity.…”

Section: Applications In Diagnosismentioning

confidence: 99%

A Promising Tool in Serological Diagnosis: Current Research Progress of Antigenic Epitopes in Infectious Diseases

et al. 2022

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Infectious diseases, caused by various pathogens in the clinic, threaten the safety of human life, are harmful to physical and mental health, and also increase economic burdens on society. Infections are a complex mechanism of interaction between pathogenic microorganisms and their host. Identification of the causative agent of the infection is vital for the diagnosis and treatment of diseases. Etiological laboratory diagnostic tests are therefore essential to identify pathogens. However, due to its rapidity and automation, the serological diagnostic test is among the methods of great significance for the diagnosis of infections with the basis of detecting antigens or antibodies in body fluids clinically. Epitopes, as a special chemical group that determines the specificity of antigens and the basic unit of inducing immune responses, play an important role in the study of immune responses. Identifying the epitopes of a pathogen may contribute to the development of a vaccine to prevent disease, the diagnosis of the corresponding disease, and the determination of different stages of the disease. Moreover, both the preparation of neutralizing antibodies based on useful epitopes and the assembly of several associated epitopes can be used in the treatment of disease. Epitopes can be divided into B cell epitopes and T cell epitopes; B cell epitopes stimulate the body to produce antibodies and are therefore commonly used as targets for the design of serological diagnostic experiments. Meanwhile, epitopes can fall into two possible categories: linear and conformational. This article reviews the role of B cell epitopes in the clinical diagnosis of infectious diseases.

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Production and characterization of anti-peptide monoclonal antibodies with specificity for staphylococcal enterotoxins A and B

Cited by 6 publications

References 27 publications

Fine-Mapping of Immunodominant Linear B-Cell Epitopes of the Staphylococcus Aureus SEB Antigen Using Short Overlapping Peptides

Fine-Mapping of Immunodominant Linear B-Cell Epitopes of the Staphylococcus Aureus SEB Antigen Using Short Overlapping Peptides

Characterization of fine specificity of the immune response to a Plasmodium falciparum rhoptry neck protein, PfAARP

A Promising Tool in Serological Diagnosis: Current Research Progress of Antigenic Epitopes in Infectious Diseases

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