Sporozoite glycoprotein antigen (SGA) of Cryptosporidium parvum is a promising vaccine target for prevention of cryptosporidiosis In silico analysis of C. parvum SGA protein

Bibliographic Details
Title: Sporozoite glycoprotein antigen (SGA) of Cryptosporidium parvum is a promising vaccine target for prevention of cryptosporidiosis In silico analysis of C. parvum SGA protein
Authors: Bahareh Kordi, Amir Fotovati, Hamidreza Majidiani, Hadi Fazel, Esfandiar Azizi, Morteza Shams, Amir Abaszadeh
Source: Informatics in Medicine Unlocked, Vol 42, Iss , Pp 101333- (2023)
Publisher Information: Elsevier, 2023.
Publication Year: 2023
Collection: LCC:Computer applications to medicine. Medical informatics
Subject Terms: Cryptosporidium parvum, SGA, Multi-epitope vaccine, Computer applications to medicine. Medical informatics, R858-859.7
More Details: Cryptosporidiosis is a zoonotic parasitic infection causing diarrhea in humans and farm animals. The present study was done to computationally analyze the Cryptosporidium parvum sporozoite glycoprotein antigen (SGA) regarding immunogenic epitopes, as a potential vaccine candidate. Physico-chemical properties, solubility, antigenicity, allergenicity, signal peptide, transmembrane domain and post-translational modifications (PTMs) along with secondary and tertiary structure analyses were predicted. Also, linear B-cell epitopes, cytotoxic T-lymphocyte (CTL; human, cattle) and helper T-lymphocyte (HTL; human) epitopes were forecasted. The molecular weight of this 265-residue protein was 27.14 kDa, with hydrophilicity (GRAVY: 0.700), high solubility (0.892), and aliphatic index (46.83). No signal peptide and transmembrane domain was predicted, and the most abundant PTMs were phosphorylation (n = 68) and O-glycosylation (n = 53). Coils were dominant in secondary structure analysis, and the tertiary model refinement showed enhancement in the refined than crude model. Only 4 shared B-cell epitopes among three web servers (ABCpred, BepiPred 2.0, and SVMTriP) were shown to be antigenic, non-allergenic, with good water solubility. Also, five potent CTL epitopes in humans and two in cattle were predicted. Notably, four HTL epitopes were found as inducers of IFN-γ, IL-4 or both. In conclusion, our results demonstrated several immunogenic epitopes in this protein, which could be directed towards multi-epitope vaccine design.
Document Type: article
File Description: electronic resource
Language: English
ISSN: 2352-9148
Relation: http://www.sciencedirect.com/science/article/pii/S235291482300179X; https://doaj.org/toc/2352-9148
DOI: 10.1016/j.imu.2023.101333
Access URL: https://doaj.org/article/9d631861a5404693b3bed2df4728cca7
Accession Number: edsdoj.9d631861a5404693b3bed2df4728cca7
Database: Directory of Open Access Journals
More Details
ISSN:23529148
DOI:10.1016/j.imu.2023.101333
Published in:Informatics in Medicine Unlocked
Language:English