scholarly journals Prediction of B-Cell Epitopes in Listeriolysin O, a Cholesterol Dependent Cytolysin Secreted by Listeria monocytogenes

2014 ◽  
Vol 2014 ◽  
pp. 1-9 ◽  
Author(s):  
Morris S. Jones ◽  
J. Mark Carter
Keyword(s):  
Monoclonal Antibodies ◽  
Listeria Monocytogenes ◽  
B Cell ◽  
Three Dimensional ◽  
Listeriolysin O ◽  
Molecular Models ◽  
B Cell Epitopes ◽  
Discontinuous Epitopes ◽  
Pathogenic Effects ◽  
Domain 4

Listeria monocytogenes is a gram-positive, foodborne bacterium responsible for disease in humans and animals. Listeriolysin O (LLO) is a required virulence factor for the pathogenic effects of L. monocytogenes. Bioinformatics revealed conserved putative epitopes of LLO that could be used to develop monoclonal antibodies against LLO. Continuous and discontinuous epitopes were located by using four different B-cell prediction algorithms. Three-dimensional molecular models were generated to more precisely characterize the predicted antigenicity of LLO. Domain 4 was predicted to contain five of eleven continuous epitopes. A large portion of domain 4 was also predicted to comprise discontinuous immunogenic epitopes. Domain 4 of LLO may serve as an immunogen for eliciting monoclonal antibodies that can be used to study the pathogenesis of L. monocytogenes as well as develop an inexpensive assay.

Identification of three linear B cell epitopes against non-structural protein 3ABC of FMDV using monoclonal antibodies

2019 ◽  
Vol 103 (19) ◽  
pp. 8075-8086
Author(s):  
Wei Liu ◽  
Junjun Shao ◽  
Danian Chen ◽  
Yanyan Chang ◽  
Huiyun Chang ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
B Cell ◽  
Structural Protein ◽  
B Cell Epitopes ◽  
Linear B

Identification of two novel fowl adenovirus C-specific B cell epitopes using monoclonal antibodies against the capsid hexon protein

2018 ◽  
Vol 102 (21) ◽  
pp. 9243-9253 ◽  
Author(s):  
Qing Pan ◽  
Jing Wang ◽  
Yulong Gao ◽  
Hongyu Cui ◽  
Changjun Liu ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
B Cell ◽  
B Cell Epitopes ◽  
Hexon Protein ◽  
Fowl Adenovirus

scholarly journals Quantitative Computational Prediction of the Consensus B-cell Epitopes of 2019-nCoV

2020 ◽  
Vol 1 (1) ◽  
pp. 42-47
Author(s):  
Raúl Isea
Keyword(s):  
B Cell ◽  
Three Dimensional ◽  
Similarity Index ◽  
Computational Prediction ◽  
Dimensional Structure ◽  
Spike Glycoprotein ◽  
B Cell Epitopes ◽  
Three Dimensional Structure ◽  
Mathematical Algorithms

The goal of this paper is to obtain the numerical consensus of B cell epitopes from the three-dimensional structure of the prefusion spike glycoprotein of the new betacoronavirus that could lead to the development of a vaccine to 2019-nCoV. In order to do that, we first calculated the B-cell epitopes that are predicted using fourteen different mathematical algorithms. Later, we obtained the consensus of B-cell epitopes according to the Similarity Index, and finally selecting the best candidates according to the results of a function called <F> which is evaluated for the glycoprotein. The best candidates that we obtained in order to design a vaccine are SSANNCT, PLQSYGFQPT, TESNKKFLP, NNSYEC, AENS, LPDPSK and YDPLQPE.

Identification of linear B cell epitopes on VP1 and VP2 proteins of Senecavirus A (SVA) using monoclonal antibodies

2020 ◽  
Vol 247 ◽  
pp. 108753 ◽  
Author(s):  
Hui Fan ◽  
Huixin Zhu ◽  
Shihai Li ◽  
Mengyu Shi ◽  
Erxuan Zhou ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
B Cell ◽  
B Cell Epitopes ◽  
Linear B

scholarly journals Dissociated Linkage of Cytokine-Inducing Activity and Cytotoxicity to Different Domains of Listeriolysin O from Listeria monocytogenes

2002 ◽  
Vol 70 (3) ◽  
pp. 1334-1341 ◽  
Author(s):  
Chikara Kohda ◽  
Ikuo Kawamura ◽  
Hisashi Baba ◽  
Takamasa Nomura ◽  
Yutaka Ito ◽  
...  
Keyword(s):  
Listeria Monocytogenes ◽  
Binding Activity ◽  
Cytolytic Activity ◽  
Listeriolysin O ◽  
Spleen Cells ◽  
Normal Spleen ◽  
Cholesterol Treatment ◽  
Ifn Γ ◽  
Cholesterol Binding ◽  
Domain 4

ABSTRACT Listeriolysin O (LLO), a cholesterol-binding cytolysin of Listeria monocytogenes, exhibits cytokine-inducing and cytolytic activities. Because the cytolytic activity was abolished by cholesterol treatment but the cytokine-inducing activity was not, these activities appeared to be linked to different domains of the LLO molecule. In this study, we constructed recombinant full-length LLO (rLLO529) and various truncated derivatives and examined their cytolytic, cholesterol-binding, and gamma interferon (IFN-γ)-inducing activities. rLLO529 exhibited both IFN-γ-inducing and cytolytic activities. Four truncated rLLOs possessing different C termini, which did not exert either cytolytic or cholesterol-binding activity, stimulated IFN-γ production in normal spleen cells. However, a truncated rLLO corresponding to domain 4 (rLLO416-529) did not exhibit IFN-γ-inducing activity, whereas it did bind to immobilized cholesterol. In addition, though the hemolysis induced by rLLO529 was inhibited by rLLO416-529, such inhibition was not detected upon rLLO529-induced IFN-γ production. These data indicated that domain 4 was responsible for binding of LLO to membrane cholesterol followed by oligomerization and pore formation by the entire LLO molecule. In contrast, the other part of LLO, corresponding to domain 1-3, was essential for IFN-γ-inducing activity. These findings implied a novel aspect of the function of LLO as a bacterial modulin.

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