Analysis of antibody response to the measles virus using synthetic peptides of the fusion protein

Handtmann, D.; Brons, Nicolaas H. C.; Weinmann, Martin; Wiesmüller, Karl‐Heinz; Spahn, Günther; Wiesneth, M.; Schneider, François; Jung, Günther

doi:10.1016/0168-1702(93)90095-5

Cited by 14 publications

(17 citation statements)

References 31 publications

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“…Indeed, a series of published reports have provided data in support of the view that the HEMA epitopes are mostly conformational and difficult to mimic with synthetic peptides [23,24,54]. Nevertheless, those studies included data clearly demonstrating that core epitopic regions within the large epitopes of HEMA and VGLF are identical to, or largely overlap with, those identified in the current study.…”

Section: Discussionsupporting

confidence: 71%

“…This can be easily explained given that previously reported B-cell epitope mapping studies have also reported these to be dominant epitopes [23,24,54,55]. However, the intestinal mimics of the measles epitopes are virtually unreactive.…”

Section: Discussionmentioning

confidence: 90%

“…Measles vaccines develop neutralizing antibodies against measles hemagglutinin (HEMA) [20-22]. Vaccinated individuals, as well as those individuals infected by measles virus, also develop antibodies against measles virus glycoprotein (VGLF), an immunodominant viral antigen [23,24]. …”

Section: Introductionmentioning

confidence: 99%

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Bioinformatic and immunological analysis reveals lack of support for measles virus related mimicry in Crohn’s disease

Polymeros

Tsiamoulos

Κουτσουμπασ

et al. 2014

BMC Med

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BackgroundA link between measles virus and Crohn’s disease (CD) has been postulated. We assessed through bioinformatic and immunological approaches whether measles is implicated in CD induction, through molecular mimicry.MethodsThe BLAST2p program was used to identify amino acid sequence similarities between five measles virus and 56 intestinal proteins. Antibody responses to measles/human mimics were tested by an in-house ELISA using serum samples from 50 patients with CD, 50 with ulcerative colitis (UC), and 38 matched healthy controls (HCs).ResultsWe identified 15 sets of significant (>70%) local amino acid homologies from two measles antigens, hemagglutinin-neuraminidase and fusion-glycoprotein, and ten human intestinal proteins. Reactivity to at least one measles 15-meric mimicking peptide was present in 27 out of 50 (54%) of patients with CD, 24 out of 50 (48%) with UC (CD versus UC, p = 0.68), and 13 out of 38 (34.2%) HCs (CD versus HC, p = 0.08). Double reactivity to at least one measles/human pair was present in four out of 50 (8%) patients with CD, three out of 50 (6%) with UC (p = 0.99), and in three out of 38 (7.9%) HCs (p >0.05 for all). Titration experiments yielded different extinction curves for anti-measles and anti-human intestinal double-reactive antibodies. Epitope prediction algorithms and three-dimensional modeling provided bioinformatic confirmation for the observed antigenicity of the main measles virus epitopic regions.ConclusionsMeasles sequences mimicking intestinal proteins are frequent targets of antibody responses in patients with CD, but this reactivity lacks disease specificity and does not initiate cross-reactive responses to intestinal mimics. We conclude that there is no involvement of measles/human molecular mimicry in the etiopathogenesis of CD.Electronic supplementary materialThe online version of this article (doi:10.1186/s12916-014-0139-9) contains supplementary material, which is available to authorized users.

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Section: Discussionsupporting

confidence: 71%

Section: Discussionmentioning

confidence: 90%

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Bioinformatic and immunological analysis reveals lack of support for measles virus related mimicry in Crohn’s disease

Polymeros

Tsiamoulos

Κουτσουμπασ

et al. 2014

BMC Med

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“…Peptide synthesis. One-hundred and eight overlapping N-fluorenylmethoxycarbonyl (Fmoc) protected peptides covering the whole sequence of the MV-F protein were prepared by solid-phase synthesis as described earlier [9,10]. Sequential pentadecapeptides overlapped by 10 amino acid residues.…”

Section: Methodsmentioning

confidence: 99%

Hierarchic T‐Cell Help to Non‐Linked B‐Cell Epitopes

et al. 1996

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The induction of antibodies against peptides requires the presence of a T helper cell epitope. In the absence of an added T-cell epitope only 10% of the mice, or less depending on the strain, gave an antibody response to a series of peptides of the measles virus (MV) fusion (F) protein. After coimmunization with a non-covalently coupled T-cell epitope more than 60% of the peptides became immunogenic. Considerable differences became apparent when BALB/c mice were immunized with peptides in the presence of different T-cell epitopes. An immunodominant T-cell epitope of the MV-F protein was more efficient than a subdominant or a cryptic T-cell epitope in providing help to a non-linked B-cell epitope. There is both a ranking order of the amount of help which B-cell epitopes require and a ranking order for the help T-cell epitopes are able to provide. The capability of a T-cell epitope to provide help to a B-cell epitope correlated with its own immunogenicity, i.e. the intensity of the antibody response to the peptide representing the T-cell epitope. The data suggest that for each MHC class II allele there is an optimal T-cell epitope which can provide help to a maximal number of B-cell epitopes and that such a peptide can be identified by its ability to induce antibodies against itself. By using this strategy, the authors were able to induce antibodies which cross-reacted with the MV.

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“…To date there is little knowledge of the interactions of B and T cell immune responses and of the distribution of B and T cell epitopes in viral infections. In measles [31] and influenza [32] virus infections there is evidence for adjacent or overlapping B and T cell epitopes. In a persisting viral infection, as in other secondary immune responses, B cells might act as highly efficient APC which present antigen, provide a second signal for T cell activation and secrete cytokines [33, 34].…”

Section: Discussionmentioning

confidence: 99%

Human CD4+ T lymphocytes recognize a highly conserved epitope of human T lymphotropic virus type 1 (HTLV-1)envgp21 restricted by HLA DRB1*0101

Kitze

Usuku

Yamano

et al. 1998

Clinical and Experimental Immunology

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HTLV-1 causes two distinct human diseases, HTLV-1-associated myelopathy/tropical spastic paraparesis (HAM/TSP) and adult T cell leukaemia/lymphoma (ATL). Persistently infected individuals carry a risk of <1% of developing either disease. These basic epidemiological data imply that virus-host interactions, especially immunogenetic factors, influence the outcome of infection. Several studies showed that the HLA class II DR1 DQ5 haplotype is over-represented in HAM/TSP, but rare in ATL. Therefore, we selected four patients with HAM/TSP and one seronegative control who all carried the HLA DR1 DQ5 haplotype. We analysed the CD4+ T lymphocyte response against eight synthetic peptides of HTLV-1 envelope (env) glycoprotein gp21, a crucial target antigen in HAM/TSP. The first of two immunodominant epitopes corresponded to a domain of the HTLV-1 envelope protein which had previously been shown to be essential for HTLV-1 envelope function. The second immunodominant epitope overlapped a highly conserved sequence of the retroviral transmembrane envelope protein. DR1 (DRB1*0101)-restricted T lymphocytes were activated by the conserved peptide sequence in nanomolar concentrations. In contrast, this conserved sequence can also induce non-specific, cAMP-mediated immunosuppressive effects on T cells when added in micromolar concentrations to culture media, as shown by Haraguchi S, Good RA, James-Yarish M, Cianciolo GJ, Day NK, Proc Natl Acad Sci USA 1995; 92:5568-71. Hence, HTLV-1 env gp21 might exert either stimulating immunological or immunosuppressive effects in HTLV-1-infected individuals, depending on the level of its expression and the presence of HLA DRB1*0101.

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Analysis of antibody response to the measles virus using synthetic peptides of the fusion protein

Cited by 14 publications

References 31 publications

Bioinformatic and immunological analysis reveals lack of support for measles virus related mimicry in Crohn’s disease

Bioinformatic and immunological analysis reveals lack of support for measles virus related mimicry in Crohn’s disease

Hierarchic T‐Cell Help to Non‐Linked B‐Cell Epitopes

Human CD4+ T lymphocytes recognize a highly conserved epitope of human T lymphotropic virus type 1 (HTLV-1)envgp21 restricted by HLA DRB1*0101

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