Retro-inverso peptide analogues of Trypanosoma cruzi B13 protein epitopes fail to be recognized by human sera and peripheral blood mononuclear cells

Iwai, Leo Kei; Duranti, M A; Abel, L.; Juliano, María A.; Kalil, Jorge; Juliano, Luiz; Cunha-Neto, Edécio

doi:10.1016/s0196-9781(01)00409-0

Cited by 16 publications

(8 citation statements)

References 42 publications

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“…(3) Y171(4) E63 (5) E63(3) Y159 (4) Y159 (3) K66 (2) T163 (2) Ile2P Y159 (2) Y159 (5) E63 (1) E63 (5) K66 (6) K66(3) E24 (5) E24 (4) Y45 (1) N70 (4) K66 (2) Ile3P Y159 (11) Y159 (17) R155 (2) S99 (2) L156 (1) Q114 (3) L156 (1) Asn4P N70 (6) N70 (2) R155 (6) R155 (6) Phe5P N70 (7) N70 (7) Y116 (3) Y116 (2) F74 (3) F74 (5) Q114 (3) Q114 (4) V97 (1) V97 (1) Before our studies, many groups have reported design of ri mimics of immune epitopes. There are several instances of the ri version of a B cell epitope exhibiting similar immune response properties as those of the native peptide, while there are certain other instances where ri analogs did not show functional mimicry (21,22). A critical aspect of designing ri analog of any peptide is the interchange of the N-and the C-termini of the peptide.…”

Section: Discussionmentioning

confidence: 99%

Mimicry of Native Peptide Antigens by the Corresponding Retro-Inverso Analogs Is Dependent on Their Intrinsic Structure and Interaction Propensities

Nair

Kaur

Singh

et al. 2003

The Journal of Immunology

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Retro-inverso (ri) analogs of model T cell and B cell epitopes were predictively designed as mimics and then assayed for activity to understand the basis of functional ri-antigenic peptide mimicry. ri versions of two MHC class I binding peptide epitopes, one from a vesicular stomatitis virus glycoprotein (VSVp) and another from OVA (OVAp), exhibit structural as well as functional mimicry of their native counterparts. The two ri peptides exhibit conformational plasticity and they bind to MHC class I (H-2Kb) similar to their native counterparts both in silico and in vivo. In fact, ri-OVAp is also presented to an OVAp-specific T cell line in a mode similar to native OVAp. In contrast, the ri version of an immunodominant B cell peptide epitope from a hepatitis B virus protein, PS1, exhibits no structural or functional correlation with its native counterpart. PS1 and its ri analog do not exhibit similar conformational propensities. PS1 is less flexible relative to its ri version. These observed structure-function relationships of the ri-peptide epitopes are consistent with the differences in recognition properties between peptide-MHC vs peptide-Ab binding where, while the recognition of the epitope by MHC is pattern based, the exquisitely specific recognition of Ag by Ab arises from the high complementarity between the Ag and the binding site of the Ab. It is evident that the correlation of conformational and interaction propensities of native l-peptides and their ri counterparts depends both on their inherent structural properties and on their mode of recognition.

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Section: Discussionmentioning

confidence: 99%

Mimicry of Native Peptide Antigens by the Corresponding Retro-Inverso Analogs Is Dependent on Their Intrinsic Structure and Interaction Propensities

Nair

Kaur

Singh

et al. 2003

The Journal of Immunology

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“…RI peptides corresponding to the immunodominant B and T cell epitopes of B13 failed to cross-react with anti-B13 antibodies in the sera from T. cruzi-infected patients and was not recognized by peripheral blood mononuclear cells obtained from individuals responding to the specific immunodominant T-cell epitope of B13. 45 This finding suggests that cross-reactivity with the natural epitope and its induced antibody may not be a general property of the corresponding RI peptides, implying that their use as synthetic vaccines and immunotherapeutic agents will be case-dependent.…”

Section: Ri Peptides As Immunogens Immunomodulators and Diagnostic mentioning

confidence: 99%

The partial retro–inverso modification: A road traveled together

Chorev

2005

Biopolymers

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“…It has been reported that peripheral T cells from P. falciparum malaria patients recognize T cell epitopes in EB200, a repetitive region of the P. falciparum antigen Pf332, the Pf155 repetitive domain of ring-infected erythrocyte surface antigen (RESA) and the repetitive domain of circumsporozoite CS protein [14, 15]. We have previously shown that PBMC proliferative and cytokine responses to B13 and its synthetic peptides are frequent among T. cruzi -infected subjects [8, 16]. We also found that T cell responses to B13 protein are restricted to patients carrying certain HLA class II alleles (HLA-DQA1*0501(DQ7), HLA-DR1, and HLA-DR2), which bind and present B13 peptides directly [8].…”

Section: Introductionmentioning

confidence: 99%

Evidence for T Cell Help in the IgG Response against Tandemly RepetitiveTrypanosoma cruziB13 Protein in Chronic Chagas Disease Patients

Duranti

Camargo

Victora

et al. 2012

Journal of Parasitology Research

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The tandemly repetitive Trypanosoma cruzi B13 protein is an immunodominant antigen among Chagas disease patients. Such repetitive domains may behave as T-independent antigens. However, T cells can recognize B13 epitopes in an HLA class II-restricted fashion and could potentially provide cognate T cell help and boost antibody titers. We assessed whether the presence of HLA class II molecules able to present B13 epitopes to T cells could affect anti-B13 IgG levels in a cognate fashion, in both major clinical forms of chronic Chagas disease. We found no difference between anti-B13 IgG antibody levels between patients carrying HLA class II molecules associated to T cell responses or other alleles. The predominant anti-B13 IgG subclass was IgG1, with negligible IgG2, suggesting a T-dependent, noncognate help for antibody production. In addition, the finding of increased anti-B13 IgG levels in sera from CCC patients indicates that clinical presentation is associated with increased anti-B13 antibody levels.

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Retro-inverso peptide analogues of Trypanosoma cruzi B13 protein epitopes fail to be recognized by human sera and peripheral blood mononuclear cells

Cited by 16 publications

References 42 publications

Mimicry of Native Peptide Antigens by the Corresponding Retro-Inverso Analogs Is Dependent on Their Intrinsic Structure and Interaction Propensities

Mimicry of Native Peptide Antigens by the Corresponding Retro-Inverso Analogs Is Dependent on Their Intrinsic Structure and Interaction Propensities

The partial retro–inverso modification: A road traveled together

Evidence for T Cell Help in the IgG Response against Tandemly RepetitiveTrypanosoma cruziB13 Protein in Chronic Chagas Disease Patients

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