<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>51(2)</volume><submitter>Cao L</submitter><pubmed_abstract>Porcine epidemic diarrhea virus (PEDV) is a pathogen of swine that causes severe diarrhea and dehydration resulting in substantial morbidity and mortality in newborn piglets. Phage display is a technique with wide application, in particular, the identification of key antigen epitopes for the development of therapeutic and diagnostic reagents and vaccines. To identify antigen epitopes with specificity for PEDV, a monoclonal antibody (MAb-5E12) against the immunodominant region of the PEDV Spike protein (S1) was used as the target for biopanning a 12-mer phage display, random peptide library. After multiple rounds of biopanning and stringent washing, three phage-displayed peptides, designated L, W and H, were identified that recognize MAb-5E12. Sequence analysis showed that the one or more of the peptides exhibited partial sequence similarity to the native S1 sequence 'MQYVYTPTYYML' (designated peptide M) at position 201-212. In combination with software analysis for the prediction of B cell epitopes, aa 201-212 exhibited characteristics of a linear epitope on the PEDV S1 protein. In contrast to peptide M, a consensus motif 'PxxY' was identified on both peptides L and W, and on the S1 protein, but not on peptide H. Peptide M and the MAb-5E12-recognizing peptides L and W significantly inhibited the adsorption of PEDV on the cell surface as monitored through plaque-reduction assays. Furthermore, data from real-time PCR and indirect immunofluorescence assays were consistent with the ability of peptides M, L and W to block viral protein expression and thereby function as antiviral agents for PEDV.</pubmed_abstract><journal>Virus genes</journal><pagination>217-24</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC7089464</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Putative phage-display epitopes of the porcine epidemic diarrhea virus S1 protein and their anti-viral activity.</pubmed_title><pmcid>PMC7089464</pmcid><pubmed_authors>Cao L</pubmed_authors><pubmed_authors>Ren X</pubmed_authors><pubmed_authors>Li G</pubmed_authors><pubmed_authors>Li X</pubmed_authors><pubmed_authors>Yin X</pubmed_authors><pubmed_authors>Liu J</pubmed_authors><pubmed_authors>Qin Z</pubmed_authors><pubmed_authors>Ge X</pubmed_authors><pubmed_authors>Gao Y</pubmed_authors><pubmed_authors>Zarlenga DS</pubmed_authors><pubmed_authors>Wang K</pubmed_authors></additional><is_claimable>false</is_claimable><name>Putative phage-display epitopes of the porcine epidemic diarrhea virus S1 protein and their anti-viral activity.</name><description>Porcine epidemic diarrhea virus (PEDV) is a pathogen of swine that causes severe diarrhea and dehydration resulting in substantial morbidity and mortality in newborn piglets. Phage display is a technique with wide application, in particular, the identification of key antigen epitopes for the development of therapeutic and diagnostic reagents and vaccines. To identify antigen epitopes with specificity for PEDV, a monoclonal antibody (MAb-5E12) against the immunodominant region of the PEDV Spike protein (S1) was used as the target for biopanning a 12-mer phage display, random peptide library. After multiple rounds of biopanning and stringent washing, three phage-displayed peptides, designated L, W and H, were identified that recognize MAb-5E12. Sequence analysis showed that the one or more of the peptides exhibited partial sequence similarity to the native S1 sequence 'MQYVYTPTYYML' (designated peptide M) at position 201-212. In combination with software analysis for the prediction of B cell epitopes, aa 201-212 exhibited characteristics of a linear epitope on the PEDV S1 protein. In contrast to peptide M, a consensus motif 'PxxY' was identified on both peptides L and W, and on the S1 protein, but not on peptide H. Peptide M and the MAb-5E12-recognizing peptides L and W significantly inhibited the adsorption of PEDV on the cell surface as monitored through plaque-reduction assays. Furthermore, data from real-time PCR and indirect immunofluorescence assays were consistent with the ability of peptides M, L and W to block viral protein expression and thereby function as antiviral agents for PEDV.</description><dates><release>2015-01-01T00:00:00Z</release><publication>2015 Oct</publication><modification>2021-02-21T04:59:12Z</modification><creation>2020-05-22T14:28:13Z</creation></dates><accession>S-EPMC7089464</accession><cross_references><pubmed>26292945</pubmed><doi>10.1007/s11262-015-1234-5</doi></cross_references></HashMap>