Discovery and structural characterization of newcastle disease virus mimetic peptides identified through phage display

Recent advances in precision medicine and virotherapy have expanded the search for novel biomolecules with therapeutic potential. In this study, we employed a phage display-based platform to identify and characterize mimetic peptides of the Newcastle Disease Virus (NDV), a promising agent in oncolytic virotherapy and veterinary vaccinology. Following the immunization of gallus domesticus (White Leghorn) and the high-performance liquid chromatography (HPLC) purification of specific IgY antibodies, a Ph.D.-7™ phage library was screened against anti-NDV targets. We identified three high-affinity mimotopes (NDV-1, NDV-2, and NDV-3) that were further characterized through an integrated in silico workflow involving AlphaFold2 and PEP-FOLD3. Structural analysis revealed that NDV-3 exhibits a stable helical conformation, which correlates with its superior binding affinity observed in Phage-ELISA assays. Furthermore, B-cell epitope predictions (BepPred-3.0) highlighted the immunogenic potential of NDV-1. Our findings demonstrate a robust proof-of-concept for the identification of NDV-mimetic leads, providing a structural basis for the future development of targeted oncolytic strategies and next-generation avian vaccines. Further functional assays are required to validate the translational efficacy of these candidates in clinical and veterinary settings.

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Publication Details

Journal
Virus Research
Published
2026-04-14
DOI
https://doi.org/10.1016/j.virusres.2026.199728
Primary Topic
Monoclonal and Polyclonal Antibodies Research
Type
article
Field-Weighted Citation Impact
0.00

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article

Discovery and structural characterization of newcastle disease virus mimetic peptides identified through phage display

Vivian Alonso‐Goulart, E. Resende Vaz, T. Velikkakam, B. Beatriz Fonseca et al.
Virus Research
Monoclonal and Polyclonal Antibodies Research
article

Discovery and structural characterization of newcastle disease virus mimetic peptides identified through phage display

Vivian Alonso‐Goulart, E. Resende Vaz, T. Velikkakam, B. Beatriz Fonseca, S. Lorenti, H. Oliveira Almeida Souza, D. Caixeta Moreira
article en

Abstract

Recent advances in precision medicine and virotherapy have expanded the search for novel biomolecules with therapeutic potential. In this study, we employed a phage display-based platform to identify and characterize mimetic peptides of the Newcastle Disease Virus (NDV), a promising agent in oncolytic virotherapy and veterinary vaccinology. Following the immunization of gallus domesticus (White Leghorn) and the high-performance liquid chromatography (HPLC) purification of specific IgY antibodies, a Ph.D.-7™ phage library was screened against anti-NDV targets. We identified three high-affinity mimotopes (NDV-1, NDV-2, and NDV-3) that were further characterized through an integrated in silico workflow involving AlphaFold2 and PEP-FOLD3. Structural analysis revealed that NDV-3 exhibits a stable helical conformation, which correlates with its superior binding affinity observed in Phage-ELISA assays. Furthermore, B-cell epitope predictions (BepPred-3.0) highlighted the immunogenic potential of NDV-1. Our findings demonstrate a robust proof-of-concept for the identification of NDV-mimetic leads, providing a structural basis for the future development of targeted oncolytic strategies and next-generation avian vaccines. Further functional assays are required to validate the translational efficacy of these candidates in clinical and veterinary settings.

Virus ResearchVol. 368
Universidade Federal de Uberlândia (BR)
Coordenação de Aperfeiçoamento de Pessoal de Nível Superior, Conselho Nacional de Desenvolvimento Científico e Tecnológico, Fundação de Amparo à Pesquisa do Estado de Minas Gerais, Ministério da Ciência, Tecnologia, Inovações e Comunicações, Sistema de Laboratórios em Nanotecnologias, Universidade Federal de Viçosa
Affordable and clean energy
Openalex Percentile: Top 23%
Monoclonal and Polyclonal Antibodies Research
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