Prediction of Multiple Peptide Based Vaccine from E1, E2 and Capsid Proteins of Rubella Virus: An In-Silico Approach

Elgenaid, Shaima Nasr Eldeen Mohamed; Al-Hajj, Ebrahim Mohammed; Ibrahim, Abdullahi Ali; Essa, Mohammed Elmujtaba Adam; Abu-haraz, Ahmed Hamdi; Abd-elrahman, Khoubieb Ali; Hassan, Mohamed A.

doi:10.4172/1745-7580.1000146

Cited by 3 publications

(2 citation statements)

References 43 publications

(54 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Bepipred linear epitope calculation method used specific average binding score for glycoprotein E of 0.210. All values equal or above than score of default threshold were considered as potential B-cell binders [35]. Concerning Emini surface accessibility prediction, the binding score was 1.00.…”

Section: Prediction Of B Cell Epitopesmentioning

confidence: 99%

“…The epitopes sequences of glycoprotein E were subjected to MHC I in binding prediction tool of IEDP and T-cell epitope was predicted to interact with different MHC class I alleles using ANN (artificial natural network) as prediction method and a length of nine amino acids [35] using the same score for each peptide interacted with MHC I. The top three peptides which had highest affinity to interact with largest coverage of different alleles were "KAYDHNSPY" (HLA-B*35:01, HLA-B*15:01, HLA-B*15:02, HLA-*30:01), "MWNYHSHVF" with HLA-B*35:01, HLA-B*15:01, HLA-A*24:02, HLA-A*23:01 and "SSYTVYIDK" with HLA-A*11:01, HLA-A*03:01, HLA-A*68:01,HLA-A*30:01.…”

Section: Prediction Of T-cell Epitopes and Mhc Class I Interaction Anmentioning

confidence: 99%

See 1 more Smart Citation

Immunoinformatics Approach-Multiple Peptides Vaccine Design from Glycoprotein E of Herpes Simplex Virus-3

Albagi¹,

Ahmed²,

Mohamme³

et al. 2018

Immunome Res

View full text Add to dashboard Cite

Background: Herpes simplex virus (HSV) is a common human pathogen, causing infections of orofacial mucosal surfaces (HSV-1) and genital mucosal surfaces (HSV-2). Productive infection results in the formation of vesicular lesions in the mucosal epithelia, followed by spread of the virus to sensory neurons and establishment of a latent infection that may remain for the life of the host. Material and method: All sequences of glycoprotein E [Human herpes virus 3] were obtained from NCBI and these sequences were subjected to IEDB predicted tools, including B cell and T cell examination, with B cell having multiple tests such as epitopes prediction, surface accessibility and antigenicity prediction; T cell included MHC I and MHC II predicted tools. Finally we used population coverage to select a highest percent of peptides related with different alleles. Result: We obtained some candidate peptides as vaccine derived peptides from B cell test which had a highest score in Emini surface accessibility ("DEDKLDTNSVYEPYYHSDHAESSWVNRGESSRKAYDHNSPYIWPRNDYDGF") of 21.807, and "LKFVDTPESL" with score 1.061 for Kolaskar and Tongaonkar antigenicity test, in another hand we got a highest affinity of peptides that interacted with major coverage of different alleles in MHC I ("KAYDHNSPY") and in MHC II ("MWNYHSHVF"). Conclusion: The efficiency and safety degree in predicted candidate epitopes by computational examination methods are required to be estimated through studies of animal model, to check whether they are able to induce a good defending immune response or not with previous mentioned properties, and we considered this study as first promising peptide based vaccine of [Human herpes virus 3] glycoprotein E in comparison to the previous studies.

show abstract

Section: Prediction Of B Cell Epitopesmentioning

confidence: 99%

Section: Prediction Of T-cell Epitopes and Mhc Class I Interaction Anmentioning

confidence: 99%

Immunoinformatics Approach-Multiple Peptides Vaccine Design from Glycoprotein E of Herpes Simplex Virus-3

Albagi¹,

Ahmed²,

Mohamme³

et al. 2018

Immunome Res

View full text Add to dashboard Cite

show abstract

Design of Epitope-Based Peptide Vaccine against Pseudomonas aeruginosa Fructose Bisphosphate Aldolase Protein Using Immunoinformatics

Elhag

Alaagib²,

Ahmed

et al. 2020

Journal of Immunology Research

View full text Add to dashboard Cite

Pseudomonas aeruginosa is a common pathogen that is responsible for serious hospital-acquired infections, ventilator-associated pneumonia, and various sepsis syndromes. Also, it is a multidrug-resistant pathogen recognized for its ubiquity and its intrinsically advanced antibiotic-resistant mechanisms. It usually affects immunocompromised individuals but can also infect immunocompetent individuals. There is no vaccine against it available till now. This study predicts an effective epitope-based vaccine against fructose bisphosphate aldolase (FBA) of Pseudomonas aeruginosa using immunoinformatics tools. The protein sequences were obtained from NCBI, and prediction tests were undertaken to analyze possible epitopes for B and T cells. Three B cell epitopes passed the antigenicity, accessibility, and hydrophilicity tests. Six MHC I epitopes were found to be promising, while four MHC II epitopes were found promising from the result set. Nineteen epitopes were shared between MHC I and II results. For the population coverage, the epitopes covered 95.62% worldwide excluding certain MHC II alleles. We recommend in vivo and in vitro studies to prove its effectiveness.

show abstract

High Affinity Peptides in Processes of IgG Purification, Chromatographic Column Virus Inactivation/Elimination and Titer of Anti-Rubella IgG Enrichment

Havryliuk¹,

Krasnobryzha²,

Havryliuk³

et al. 2022

J Biomed Res Environ Sci

View full text Add to dashboard Cite

According to "The Proteome Code" concept introduced by J. Biro and our early development of affinity peptide calculation method it was studied the possibility of high affinity peptide chromatographic gels development for IgG1-4 separation from the donor plasma. Given the next step of virus inactivation of IgG directly in the chromatographic column, the affinity gel had bind IgG at several spatially spaced points in order to limit the degree of freedom of the protein for retention IgG at high buffer flow rate or elevated buffer temperatures without denaturation. In addition, the possibility of creating highly specific affinity sense-antisense peptides against Rubella virus in order to increase the titer of aRIgG in plasma or even its isolation in highly purified form was studied. Based on previous experiments, an affinity multi-peptide chromatographic gel with the following properties was developed: the DBC with enough residence time 10 min was around 50-54 mg × mL-1 of total 98.0% purity of IgG with natural proportion of the 1-4 subclasses, any other immunoglobulins were not found. The virus inactivation/elimination on this gel directly in chromatographic column shown a highly effective virus elimination (log10>9) for both nonenveloped and lipid enveloped viruses. Using RV sequence from UniProt_KB and dates from more than 20 literature sources on the virus proteins interaction, affinity peptides were calculated against virus proteins C and E1,2. Then these peptides were modified to reach more affinity enhancement and affinity-peptide chromatographic gel was synthetized. By this gel from total mass IgG1-4 contained 6644 IU anti-Rubella IgG with specificity 6.64 IU × mg-1 were isolated 5382 IU aRIgG (> 80%) with a specificity of 791 IU × mg-1.

show abstract

Prediction of Multiple Peptide Based Vaccine from E1, E2 and Capsid Proteins of Rubella Virus: An In-Silico Approach

Cited by 3 publications

References 43 publications

Immunoinformatics Approach-Multiple Peptides Vaccine Design from Glycoprotein E of Herpes Simplex Virus-3

Immunoinformatics Approach-Multiple Peptides Vaccine Design from Glycoprotein E of Herpes Simplex Virus-3

Design of Epitope-Based Peptide Vaccine against Pseudomonas aeruginosa Fructose Bisphosphate Aldolase Protein Using Immunoinformatics

High Affinity Peptides in Processes of IgG Purification, Chromatographic Column Virus Inactivation/Elimination and Titer of Anti-Rubella IgG Enrichment

Contact Info

Product

Resources

About