High-resolution epitope mapping for monoclonal antibodies to the structural protein Erns of classical swine fever virus using peptide array and random peptide phage display approaches

Lin, Min; McRae, Heather; Dan, Hanhong; Tangorra, Erin; Laverdiere, Amanda; Pasick, John

doi:10.1099/vir.0.023259-0

Cited by 16 publications

(10 citation statements)

References 51 publications

(48 reference statements)

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“…In this context, epitope prediction programs have been widely used in malaria research ( 4 , 79 – 81 ). Nevertheless, the use of chemically prepared arrays of short peptides is a more powerful tool to identify and characterize epitopes recognized by antibodies ( 46 , 82 , 83 ). It is also important to mention that in order to raise antibodies for a peptide, a minimum length of six amino acids is required, and peptides of >10 amino acids are generally required for the induction of antibodies that may bind to the native protein ( 84 ).…”

Section: Discussionmentioning

confidence: 99%

Plasmodium vivax Cell-Traversal Protein for Ookinetes and Sporozoites: Naturally Acquired Humoral Immune Response and B-Cell Epitope Mapping in Brazilian Amazon Inhabitants

et al. 2017

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The cell-traversal protein for ookinetes and sporozoites (CelTOS), a highly conserved antigen involved in sporozoite motility, plays an important role in the traversal of host cells during the preerythrocytic stage of Plasmodium species. Recently, it has been considered an alternative target when designing novel antimalarial vaccines against Plasmodium falciparum. However, the potential of Plasmodium vivax CelTOS as a vaccine target is yet to be explored. This study evaluated the naturally acquired immune response against a recombinant P. vivax CelTOS (PvCelTOS) (IgG and IgG subclass) in 528 individuals from Brazilian Amazon, as well as the screening of B-cell epitopes in silico and peptide assays to associate the breadth of antibody responses of those individuals with exposition and/or protection correlates. We show that PvCelTOS is naturally immunogenic in Amazon inhabitants with 94 individuals (17.8%) showing specific IgG antibodies against the recombinant protein. Among responders, the IgG reactivity indexes (RIs) presented a direct correlation with the number of previous malaria episodes (p = 0.003; r = 0.315) and inverse correlation with the time elapsed from the last malaria episode (p = 0.031; r = −0.258). Interestingly, high responders to PvCelTOS (RI > 2) presented higher number of previous malaria episodes, frequency of recent malaria episodes, and ratio of cytophilic/non-cytophilic antibodies than low responders (RI < 2) and non-responders (RI < 1). Moreover, a high prevalence of the cytophilic antibody IgG1 over all other IgG subclasses (p < 0.0001) was observed. B-cell epitope mapping revealed five immunogenic regions in PvCelTOS, but no associations between the specific IgG response to peptides and exposure/protection parameters were found. However, the epitope (PvCelTOSI136-E143) was validated as a main linear B-cell epitope, as 92% of IgG responders to PvCelTOS were also responders to this peptide sequence. This study describes for the first time the natural immunogenicity of PvCelTOS in Amazon individuals and identifies immunogenic regions in a full-length protein. The IgG magnitude was mainly composed of cytophilic antibodies (IgG1) and associated with recent malaria episodes. The data presented in this paper add further evidence to consider PvCelTOS as a vaccine candidate.

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Section: Discussionmentioning

confidence: 99%

Plasmodium vivax Cell-Traversal Protein for Ookinetes and Sporozoites: Naturally Acquired Humoral Immune Response and B-Cell Epitope Mapping in Brazilian Amazon Inhabitants

et al. 2017

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“…The epitope of D29 was mapped using a random-peptide phage display library, an approach which has been widely used for the identification of both linear and conformational epitopes [26,[31][32][33][34]. Two peptide phage clones, P3 (Cluster 1) and P9 (Cluster 2), displayed significant inhibition of D29 Fab-IgG binding to immobilized DENV2 by ELISA; P9 was also able to significantly block the binding of D29 Fab-IgG in a nonreducing Western blot analysis.…”

Section: Discussionmentioning

confidence: 99%

A Human PrM Antibody That Recognizes a Novel Cryptic Epitope on Dengue E Glycoprotein

et al. 2012

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Dengue virus (DENV) is a major mosquito-borne pathogen infecting up to 100 million people each year; so far no effective treatment or vaccines are available. Recently, highly cross-reactive and infection-enhancing pre-membrane (prM)-specific antibodies were found to dominate the anti-DENV immune response in humans, raising concern over vaccine candidates that contain native dengue prM sequences. In this study, we have isolated a broadly cross-reactive prM-specific antibody, D29, during a screen with a non-immunized human Fab-phage library against the four serotypes of DENV. The antibody is capable of restoring the infectivity of virtually non-infectious immature DENV (imDENV) in FcγR-bearing K562 cells. Remarkably, D29 also cross-reacted with a cryptic epitope on the envelope (E) protein located to the DI/DII junction as evidenced by site-directed mutagenesis. This cryptic epitope, while inaccessible to antibody binding in a native virus particle, may become exposed if E is not properly folded. These findings suggest that generation of anti-prM antibodies that enhance DENV infection may not be completely avoided even with immunization strategies employing E protein alone or subunits of E proteins.

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“…Phage was performed according to the instructions of the manufacturer of the 12‐mer peptide phage display library, with modifications 12 . The 96‐well plates were coated with antibody PR8‐23 (10 μg/ml) overnight at 4°C.…”

Section: Methodsmentioning

confidence: 99%

Neutralizing antibody PR8‐23 targets the footprint of the sialoglycan receptor binding site of H1N1 hemagglutinin

Yan

Sun

Guo

et al. 2021

Journal of Medical Virology

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Influenza virus cause seasonal influenza epidemic and seriously sporadic influenza pandemic outbreaks. Hemagglutinin (HA) is an important target in the therapeutic treatment and diagnostic detection of the influenza virus. Variation in the sialic acid receptor binding site leads to strain‐specific binding and results in different binding modes to the host receptors. Here, we evaluated the neutralizing activity and hemagglutination inhibition activity of a prepared murine anti‐H1N1 monoclonal antibody PR8‐23. Then we identified the epitope peptide of antibody PR8‐23 by phage display technique from phage display peptide libraries. The identified epitope, 63‐IAPLQLGKCNIA‐74, containing two α‐helix and two β‐fold located at the footprint of the sialoglycan receptor on the RBS in the globular head domain of HA. It broads the growing arsenal of motifs for the amino acids on the globular head domain of HA in sialic acid receptor binding site and neutralizing antibody production.

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High-resolution epitope mapping for monoclonal antibodies to the structural protein Erns of classical swine fever virus using peptide array and random peptide phage display approaches

Cited by 16 publications

References 51 publications

Plasmodium vivax Cell-Traversal Protein for Ookinetes and Sporozoites: Naturally Acquired Humoral Immune Response and B-Cell Epitope Mapping in Brazilian Amazon Inhabitants

Plasmodium vivax Cell-Traversal Protein for Ookinetes and Sporozoites: Naturally Acquired Humoral Immune Response and B-Cell Epitope Mapping in Brazilian Amazon Inhabitants

A Human PrM Antibody That Recognizes a Novel Cryptic Epitope on Dengue E Glycoprotein

Neutralizing antibody PR8‐23 targets the footprint of the sialoglycan receptor binding site of H1N1 hemagglutinin

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