scholarly journals Study on the secondary structure and B-cell epitopes of Mycoplasma suis ORF9 protein by Bioinformatics

Author(s):  
Si Shan ◽  
Nie Peng ◽  
Xiaojun Yan ◽  
Caifeng Ba
Biopolymers ◽  
2000 ◽  
Vol 58 (2) ◽  
pp. 117-128 ◽  
Author(s):  
M. J. G�mara ◽  
V. Girona ◽  
G. Ercilla ◽  
F. Reig ◽  
M. A. Alsina ◽  
...  

2017 ◽  
Vol 54 (4) ◽  
pp. 275-283 ◽  
Author(s):  
Y.-J. Lu ◽  
D.-Sh. Chen ◽  
W.-T. Hao ◽  
H.-W. Xu ◽  
Y.-W. Zhang ◽  
...  

Summary The paramyosin (Pmy) protein has been presented as a potential vaccine candidate against Schistosoma spp. However, it remains elusive whether it works in controlling cystic echinococcosis (CE), which is caused by the larval stages of Echinococcus granulosus (E. granulosus). This study investigated the characteristics of E. granulosus Pmy (EgPmy) using in silico analysis and evaluated its potential as an epitope vaccine. The secondary structure was predicted by SOPMA software and linear B-cell epitopes were screened by the Kolaskar and Tongaonkar’s method on IEBD while conformational B-cell epitopes were predicted by the Ellipro. Additionally, the epitopes of cytotoxic T lymphocyte (CTL) were analyzed by the NetCTL-1.2 server. The results showed that α-helices, extended strands, random coils and β-turns accounted for 84.82 %, 6.60 %, 5.56 % and 3.01 % in EgPmy’s secondary structure, respectively. A total of 29 linear B-cell epitopes and 6 conformational epitopes were identified together with 25 CTL epitopes. The CTL epitope 709KLEEAEAFA717 showed a high potential to elicit CTL response. These results suggested that EgPmy has a strong immunogenicity, which could serve as a reference for the development of EgPmy-based epitope vaccine against CE.


Vaccines ◽  
2021 ◽  
Vol 9 (1) ◽  
pp. 52
Author(s):  
Hassan Moeini ◽  
Suliman Qadir Afridi ◽  
Sainitin Donakonda ◽  
Percy A. Knolle ◽  
Ulrike Protzer ◽  
...  

Human norovirus (HuNoV) is the leading cause of nonbacterial gastroenteritis worldwide with the GII.4 genotype accounting for over 80% of infections. The major capsid protein of GII.4 variants is evolving rapidly, resulting in new epidemic variants with altered antigenic potentials that must be considered for the development of an effective vaccine. In this study, we identify and characterize linear blockade B-cell epitopes in HuNoV GII.4. Five unique linear B-cell epitopes, namely P2A, P2B, P2C, P2D, and P2E, were predicted on the surface-exposed regions of the capsid protein. Evolving of the surface-exposed epitopes over time was found to correlate with the emergence of new GII.4 outbreak variants. Molecular dynamic simulation (MD) analysis and molecular docking revealed that amino acid substitutions in the putative epitopes P2B, P2C, and P2D could be associated with immune escape and the appearance of new GII.4 variants by affecting solvent accessibility and flexibility of the antigenic sites and histo-blood group antigens (HBAG) binding. Testing the synthetic peptides in wild-type mice, epitopes P2B (336–355), P2C (367–384), and P2D (390–400) were recognized as GII.4-specific linear blockade epitopes with the blocking rate of 68, 55 and 28%, respectively. Blocking rate was found to increase to 80% using the pooled serum of epitopes P2B and P2C. These data provide a strategy for expanding the broad blockade potential of vaccines for prevention of NoV infection.


Cells ◽  
2021 ◽  
Vol 10 (2) ◽  
pp. 438
Author(s):  
Jean Harb ◽  
Nicolas Mennesson ◽  
Cassandra Lepetit ◽  
Maeva Fourny ◽  
Margaux Louvois ◽  
...  

Chronic stimulation by infectious pathogens or self-antigen glucosylsphingosine (GlcSph) can lead to monoclonal gammopathy of undetermined significance (MGUS) and multiple myeloma (MM). Novel assays such as the multiplex infectious antigen microarray (MIAA) and GlcSph assays, permit identification of targets for >60% purified monoclonal immunoglobulins (Igs). Searching for additional targets, we selected 28 purified monoclonal Igs whose antigen was not represented on the MIAA and GlcSph assays; their specificity of recognition was then analyzed using microarrays consisting of 3760 B-cell epitopes from 196 pathogens. The peptide sequences PALTAVETG and PALTAAETG of the VP1 coat proteins of human poliovirus 1/3 and coxsackievirus B1/B3, respectively, were specifically recognized by 6/28 monoclonal Igs. Re-analysis of patient cohorts showed that purified monoclonal Igs from 10/155 MGUS/SM (6.5%) and 3/147 MM (2.0%) bound to the PALTAVETG or PALTAAETG epitopes. Altogether, PALTAV/AETG-initiated MGUS are not rare and few seem to evolve toward myeloma.


Author(s):  
Xiaohui Wang ◽  
Joy-Yan Lam ◽  
Linlei Chen ◽  
Shannon Wing-Ngor Au ◽  
Kelvin K. W. To ◽  
...  
Keyword(s):  
B Cell ◽  

Author(s):  
Shahab Mahmoudvand ◽  
Somayeh Shokri ◽  
Manoochehr Makvandi ◽  
Reza Taherkhani ◽  
Mohammad Rashno ◽  
...  

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