BcePred: Prediction of Continuous B-Cell Epitopes in Antigenic Sequences Using Physico-chemical Properties

Saha, Sudipto; Raghava, G. P. S.

doi:10.1007/978-3-540-30220-9_16

Cited by 336 publications

(257 citation statements)

References 15 publications

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“…In the middle of each figure, the amino acid sequence in a single letter amino acid code is given for related orthopoxviruses. On the bottom, B cell-predicted epitopes obtained from the BcePred software (35).…”

Section: Discussionmentioning

confidence: 99%

Subunit Recombinant Vaccine Protects against Monkeypox

Heraud

Edghill-Smith

Ayala

et al. 2006

The Journal of Immunology

159

137

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The smallpox vaccine Dryvax, a live vaccinia virus (VACV), protects against smallpox and monkeypox, but is contraindicated in immunocompromised individuals. Because Abs to VACV mediate protection, a live virus vaccine could be substituted by a safe subunit protein-based vaccine able to induce a protective Ab response. We immunized rhesus macaques with plasmid DNA encoding the monkeypox orthologs of the VACV L1R, A27L, A33R, and B5R proteins by the intradermal and i.m. routes, either alone or in combination with the equivalent recombinant proteins produced in Escherichia coli. Animals that received only DNA failed to produce high titer Abs, developed innumerable skin lesions after challenge, and died in a manner similar to placebo controls. By contrast, the animals vaccinated with proteins developed moderate to severe disease (20–155 skin lesions) but survived. Importantly, those immunized with DNA and boosted with proteins had mild disease with 15 or fewer lesions that resolved within days. DNA/protein immunization elicited Th responses and binding Ab titers to all four proteins that correlated negatively with the total lesion number. The sera of the immunized macaques recognized a limited number of linear B cell epitopes that are highly conserved among orthopoxviruses. Their identification may guide future efforts to develop simpler, safer, and more effective vaccines for monkeypox and smallpox.

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Section: Discussionmentioning

confidence: 99%

Subunit Recombinant Vaccine Protects against Monkeypox

Heraud

Edghill-Smith

Ayala

et al. 2006

The Journal of Immunology

159

137

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“…There is close homology between the linear sequence in ␣-actinin, HMGB1 and HMGB3, with hsp70 showing slightly less homology. Furthermore, all the common peptide sequences from each respective Ag were in B cell epitope regions as determined by Bcepred, a B cell epitope prediction program (22). Importantly, the common peptide sequence from ␣-actinin is found in its actin binding domain, a region recently determined to be targeted by the anti-␣-actinin response in human lupus nephritis (5).…”

Section: Ags Bound By Sera From ␣-Actinin-immunized Mice Share a Commmentioning

confidence: 99%

α-Actinin Immunization Elicits Anti-Chromatin Autoimmunity in Nonautoimmune Mice

Deocharan¹,

Zhou

Antar

et al. 2007

The Journal of Immunology

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Anti-dsDNA Abs are characteristic of lupus and can be found deposited in the kidneys of lupus mice. Previously, we have shown that pathogenic anti-dsDNA Abs as well as Ig eluted from the kidneys of nephritic lupus mice cross-react with α-actinin. Moreover, cross-reactivity with α-actinin characterizes nephritogenic anti-dsDNA Abs in humans with lupus as well. To determine whether Abs generated against α-actinin in vivo cross-react with nuclear Ags, we s.c. immunized 10-wk-old female BALB/c mice (and several other nonautoimmune mice strains) with α-actinin in adjuvant. Immunized but not control mice displayed high titers of anti-nuclear Abs and IgG anti-chromatin autoantibodies, hypergammaglobulinemia, renal Ig deposition, and proteinuria. The specificity of the anti-chromatin response was determined by Western blotting of purified chromatin with serum from α-actinin immunized mice. By proteomic analysis, a 25-kDa doublet band was conclusively identified as high mobility group box (HMGB) proteins 1 and 3, and a 70-kDa band was identified as heat shock protein 70 (hsp70), both of which are known antigenic targets in murine lupus. Binding to purified HMGB1 and hsp70 by immunized mice sera was confirmed by ELISA and Western blot. Immunized mice sera binding to both 25- and 70-kDa bands were significantly inhibited by α-actinin and chromatin. Importantly, a panel of nephritogenic mAbs had significantly higher affinity for α-actinin, chromatin, HMGB, and hsp70 as compared with nonpathogenic Abs, suggesting a common motif in these Ags that is targeted by pathogenic autoantibodies.

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“…Classical methods of identifying potential linear B-cell epitopes from antigenic sequences typically rely on the use of amino acid propensity scales [23,21,15,11,24,22,1,20,29]. However, as shown by Blythe and Flower [5], the performance of such methods is only marginally better than that of random guessing.…”

Section: Introductionmentioning

confidence: 99%