In silico analysis of epitope-based CadF vaccine design against Campylobacter jejuni

Abstract Objective: Vaccination is an important strategy for the eradication of infectious diseases. CadF protein of Campylobacter jejuni is one of the important factors in the pathogenesis of this bacterium. The purpose of this work was to perform a bioinformatics study to identify an epitope-based CadF vaccine, as a subunit vaccine. Full protein sequences of CadF were extracted from the NCBI and UniProt databases and subjected to in silico evaluations, including sequence analysis, allergenicity, antigenicity, epitope conservancy, and molecular docking assessments done by different servers. Results: The results showed that CadF was a highly conserved protein belonging to the outer member proteins superfamily. Among the evaluated epitopes, LSDSLALRL was identified as an antigenic and non-allergenic peptide with a suitable structure for vaccine development. It was also able to stimulate both T and B cells. This 9-mer peptide was located in 136-144 segment of CadF protein and interacted with both HLA-A 0101 and HLA-DRB1 0101 alleles. Overall, the obtained theoretical results showed that CadF protein could be used for designing and evaluating a new effective vaccine against C. jejuni.

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In silico analysis of epitope-based CadF vaccine design against Campylobacter jejuni

10.21203/rs.3.rs-45952/v3 ◽

2020 ◽

Author(s):

Mona Moballegh Naseri ◽

Saeed Shams ◽

Mohammad Moballegh Naseri ◽

Bita Bakhshi

Keyword(s):

In Silico ◽

Vaccine Development ◽

In Silico Analysis ◽

Effective Vaccine ◽

T And B Cells ◽

Suitable Structure ◽

A Subunit ◽

Bioinformatics Study ◽

Theoretical Results ◽

Silico Analysis

Abstract Objective: Vaccination is an important strategy for the eradication of infectious diseases. CadF protein of Campylobacter jejuni is one of the important factors in the pathogenesis of this bacterium. The purpose of this work was to perform a bioinformatics study to identify an epitope-based CadF vaccine, as a subunit vaccine. Full protein sequences of CadF were extracted from the NCBI and UniProt databases and subjected to in silico evaluations, including sequence analysis, allergenicity, antigenicity, epitope conservancy, and molecular docking assessments done by different servers. Results: The results showed that CadF was a highly conserved protein belonging to the outer member proteins superfamily. Among the evaluated epitopes, LSDSLALRL was identified as an antigenic and non-allergenic peptide with a suitable structure for vaccine development. It was also able to stimulate both T and B cells. This 9-mer peptide was located in 136-144 segment of CadF protein and interacted with both HLA-A 0101 and HLA-DRB1 0101 alleles. Overall, the obtained theoretical results showed that CadF protein could be used for designing and evaluating a new effective vaccine against C. jejuni.

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In Silico Analysis of CadF Epitope-based Vaccine Design Against Campylobacter Jejuni

10.21203/rs.3.rs-45952/v1 ◽

2020 ◽

Author(s):

Mona Moballegh Naseri ◽

Saeed Shams ◽

Mohammad Moballegh Naseri ◽

Bita Bakhshi

Keyword(s):

In Silico ◽

In Silico Analysis ◽

Vaccine Design ◽

Allergenic Protein ◽

Epitope Structure ◽

Suitable Structure ◽

A Subunit ◽

Bioinformatics Study ◽

Theoretical Results ◽

Silico Analysis

Abstract Objective: To eradicate infectious diseases, vaccination is an important strategy. CadF protein of Campylo bacter jejuni is one of the important factors in the process of the pathogenesis of the bacterium. So, the purpose of the work was to perform a bioinformatics study for identifying an epitope-based CadF vaccine, as a subunit vaccine. CadF sequences were extracted from the NCBI database. In silico analysis including all ergeni city, antigenicity, epitope conservancy assessment, molecular docking, etc.was done by different servers. Results:The results showed that CadF is an antigenic and non-allergenic protein and provides a suitable structure for vaccine design. Among epitopes, LSDSLALRL has been confirmed to stimulate both B and T cells. This 9-mers peptide is located in 135-143 segment of the CadF protein and interacted with HLA-A0101 and HLA-DRB1 0101 with energies of docking -26.18kcal/mol and -109.89kcal/mol. The peptide is not an allergen and as an antigen, it has the ability for motivating the immune system. Hence, the analyses are performed on that the epitope structure could verify the design of a vaccine against C. jejuni. The obtained theoretical results showed that CadF protein could be used for designing and evaluating a new vaccine in humans.

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In silico Analysis of CadF epitope- based vaccine design against Campylobacter jejuni

10.21203/rs.2.14511/v1 ◽

2019 ◽

Author(s):

Mona Mobalegh Naseri ◽

Saeed Shams ◽

Mohammad Moballegh Naseri ◽

Bita Bakhshi

Keyword(s):

Campylobacter Jejuni ◽

Chemical Properties ◽

In Silico Analysis ◽

Main Body ◽

Allergenic Protein ◽

Epitope Structure ◽

A Subunit ◽

Bioinformatics Study ◽

Silico Analysis ◽

Pathogenic Process

Abstract Background To eradicate infectious diseases caused by microorganisms, vaccination is a popular strategy against them and can be an effective approach. Among vaccines, subunit vaccines have been used to be more effective against diseases. CadF protein of Campylobacter jejuni is one of the important antigens in the pathogenic process of the bacterium. So, the aim of this work was to do a bioinformatics study for the identification of epitope-based CadF vaccine, as a subunit vaccine. Main body CadF gene sequences were extracted from the NCBI database and suitable physic-chemical properties of CadF were evaluated by Protprom server. Some epitopes of the CadF protein with high affinity were detected by different servers, which were predicted based on MHC-peptide complex and B-cell epitopes. The results indicated that CadF is an antigenic and non-allergenic protein and provided a desirable structure for design vaccine. Among epitopes, LSDSLALRL was confirmed for the simulation of both of B and T cells. This 9-mers peptide was located in 135-143 sequences of CadF protein and interacted with HLA-A0101. The peptide isn’t allergen and has the ability to be an antigen for motivating immune system. Besides, the analysis implied that the epitope structure could allow designing a vaccine against C. jejuni.

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