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Main Authors: Lun, Jingsheng, Zheng, Peng, Liang, Xueji, Hu, Yihui, An, Lu, Xiao, Guiqian, Chen, Xinyi, Chen, Ying, Gong, Huisheng, Zhong, Mingqi, Zhang, Yueling, Hu, Zhong
Format: Artículo científico
Language:en
Published: Vaccine 2025
Subjects:
Online Access:https://pubmed.ncbi.nlm.nih.gov/40037129/
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author Lun, Jingsheng
Zheng, Peng
Liang, Xueji
Hu, Yihui
An, Lu
Xiao, Guiqian
Chen, Xinyi
Chen, Ying
Gong, Huisheng
Zhong, Mingqi
Zhang, Yueling
Hu, Zhong
author_facet Lun, Jingsheng
Zheng, Peng
Liang, Xueji
Hu, Yihui
An, Lu
Xiao, Guiqian
Chen, Xinyi
Chen, Ying
Gong, Huisheng
Zhong, Mingqi
Zhang, Yueling
Hu, Zhong
Lun, Jingsheng
Zheng, Peng
Liang, Xueji
Hu, Yihui
An, Lu
Xiao, Guiqian
Chen, Xinyi
Chen, Ying
Gong, Huisheng
Zhong, Mingqi
Zhang, Yueling
Hu, Zhong
collection PubMed - marine biology
contents Identification of a conserved cryptic epitope with cross-immunoreactivity in outer membrane protein K (OmpK) from Vibrio species. Lun, Jingsheng Zheng, Peng Liang, Xueji Hu, Yihui An, Lu Xiao, Guiqian Chen, Xinyi Chen, Ying Gong, Huisheng Zhong, Mingqi Zhang, Yueling Hu, Zhong Vibrio Cross Reactions Antibodies, Bacterial Epitopes Animals Bacterial Outer Membrane Proteins Bacterial Vaccines Vibrio Infections Mice Outer membrane protein K (OmpK) has been proven to be an ideal vaccine candidate for broad-spectrum cross-prevention against Vibriosis. However, due to the extensive biological and genetic diversity of Vibrio species, current OmpK subunit vaccines can only target different strains of the same bacterial species or closely related species and have difficulty providing promising cross-immunoprotection against more diverse Vibrio infections. In recent years, the development of epitope-focused vaccines has been described as the latest stage in the development of vaccine formulations, providing new ideas for the development of broad-spectrum Vibrio vaccines. Interestingly, a cryptic epitope (K7) was identified in OmpK from Vibrio species, which is itself immunogenic but is not involved in the immune response to intact OmpK. Epitope K7 is a 15-residue hairpin structure in OmpK predicted to contain a 6-residue extracellular turn region. Interestingly, unlike other highly variable extracellular long loops, epitope K7 is the only conserved extracellular short turn in OmpK, with a similarity of 33 % to 93 %. K7 homologous peptides stimulated the production of specific antibodies, confirming their high immunogenicity. Cross-immunoreactivity between K7 homologous and K7-induced antibodies was evaluated by peptide-based ELISA, western blot, and cell-based ELISA. Flow cytometry and immunofluorescence assay further confirmed that the native epitope K7 in OmpK is surface-exposed and therefore an extracellular target that binds to antibodies. Moreover, an antibody-dependent and complement-mediated serum bactericidal assay suggested that epitope K7-induced antibodies have vibriocidal activity. In conclusion, we identified a conserved cryptic epitope with cross-immunoreactivity in OmpK from Vibrio species. Our results suggest that epitope K7 could be an ideal candidate for the design of epitope-focused vaccines against diverse Vibrio infections.
format Artículo científico
id pubmed_40037129
institution PubMed
language en
publishDate 2025
publisher Vaccine
record_format pubmed
spellingShingle Identification of a conserved cryptic epitope with cross-immunoreactivity in outer membrane protein K (OmpK) from Vibrio species.
Lun, Jingsheng
Zheng, Peng
Liang, Xueji
Hu, Yihui
An, Lu
Xiao, Guiqian
Chen, Xinyi
Chen, Ying
Gong, Huisheng
Zhong, Mingqi
Zhang, Yueling
Hu, Zhong
Vibrio
Cross Reactions
Antibodies, Bacterial
Epitopes
Animals
Bacterial Outer Membrane Proteins
Bacterial Vaccines
Vibrio Infections
Mice
Identification of a conserved cryptic epitope with cross-immunoreactivity in outer membrane protein K (OmpK) from Vibrio species. Lun, Jingsheng Zheng, Peng Liang, Xueji Hu, Yihui An, Lu Xiao, Guiqian Chen, Xinyi Chen, Ying Gong, Huisheng Zhong, Mingqi Zhang, Yueling Hu, Zhong Vibrio Cross Reactions Antibodies, Bacterial Epitopes Animals Bacterial Outer Membrane Proteins Bacterial Vaccines Vibrio Infections Mice Outer membrane protein K (OmpK) has been proven to be an ideal vaccine candidate for broad-spectrum cross-prevention against Vibriosis. However, due to the extensive biological and genetic diversity of Vibrio species, current OmpK subunit vaccines can only target different strains of the same bacterial species or closely related species and have difficulty providing promising cross-immunoprotection against more diverse Vibrio infections. In recent years, the development of epitope-focused vaccines has been described as the latest stage in the development of vaccine formulations, providing new ideas for the development of broad-spectrum Vibrio vaccines. Interestingly, a cryptic epitope (K7) was identified in OmpK from Vibrio species, which is itself immunogenic but is not involved in the immune response to intact OmpK. Epitope K7 is a 15-residue hairpin structure in OmpK predicted to contain a 6-residue extracellular turn region. Interestingly, unlike other highly variable extracellular long loops, epitope K7 is the only conserved extracellular short turn in OmpK, with a similarity of 33 % to 93 %. K7 homologous peptides stimulated the production of specific antibodies, confirming their high immunogenicity. Cross-immunoreactivity between K7 homologous and K7-induced antibodies was evaluated by peptide-based ELISA, western blot, and cell-based ELISA. Flow cytometry and immunofluorescence assay further confirmed that the native epitope K7 in OmpK is surface-exposed and therefore an extracellular target that binds to antibodies. Moreover, an antibody-dependent and complement-mediated serum bactericidal assay suggested that epitope K7-induced antibodies have vibriocidal activity. In conclusion, we identified a conserved cryptic epitope with cross-immunoreactivity in OmpK from Vibrio species. Our results suggest that epitope K7 could be an ideal candidate for the design of epitope-focused vaccines against diverse Vibrio infections.
title Identification of a conserved cryptic epitope with cross-immunoreactivity in outer membrane protein K (OmpK) from Vibrio species.
topic Vibrio
Cross Reactions
Antibodies, Bacterial
Epitopes
Animals
Bacterial Outer Membrane Proteins
Bacterial Vaccines
Vibrio Infections
Mice
url https://pubmed.ncbi.nlm.nih.gov/40037129/