In silico prediction of B cell epitopes of the hemolysis-associated protein 1 for vaccine design against leptospirosis

Sakineh Poorhosein Fookolaee, Somayyeh Talebishelimaki, Mohammad Taha Saadati Rad, Mostafa Akbarian Rokni

Abstract


Leptospirosis is known as a zoonotic disease of global importance originated from infection with the spirochete bacterium Leptospira. Although several leptospirosis vaccines have been tested, the vaccination is relatively unsuccessful in clinical application despite decades of research. Therefore, this study was conducted to predict B cell epitopes of the hemolysis-associated protein 1 (Hap1) for vaccine design against leptospirosis. For prediction of linear epitopes, the sequence of extracellular region of Hap1 was submitted to ABCpred, BCPREDs, Bcepred, Bepipred and Ellipro servers. DiscoTope 2.0 and B-pred servers were used for prediction of conformational epitopes from the entire PDB structure of Hap1 that obtained from the homology modeling method. Further analysis for solvent accessible areas and relative solvent accessibility of all the residues on the PDB structures using Naccess program and NetSurfP server defined that predicted conformational B cell epitopes had higher solvent accessible and their residues were exposed on the surface therefore, immunoinformatics analysis showed that hemolysis-associated protein 1 can properly stimulate the B cells immune responses.

Keywords


Leptospirosis; Hemolysis-associated protein 1; B cell epitope; in silico

References


Lane AB, Dore MM. Leptospirosis A clinical review of evidence based diagnosis, treatment and prevention. World J Clin Infect Dis. 2016; 6(4):61-66.

Palaniappan RU, Ramanujam S, Chang Y-F. Leptospirosis: pathogenesis, immunity, and diagnosis. Curr Opin Infect Dis. 2007; 20(3):284-92.

Adler B, de la Peña Moctezuma A. Leptospira and leptospirosis. Vet Microbiol. 2010; 140(3-4):287-96.

Wang Z, Jin L, Węgrzyn A. Leptospirosis vaccines. Microb Cell Fact. 2007; 6:39.

Hoke DE, Egan S, Cullen PA, Adler B. LipL32 is an extracellular matrix-interacting protein of Leptospira spp. and Pseudoalteromonas tunicata. Infect Immun. 2008; 76(5):2063-9.

Branger C, Sonrier C, Chatrenet B, Klonjkowski B, Ruvoen-Clouet N, Aubert A, et al. Identification of the hemolysis-associated protein 1 as a cross-protective immunogen of Leptospira interrogans by adenovirus-mediated vaccination. Infect Immun. 2001; 69(11):6831-8.

Powell, Michael F., Newman, Mark J. (Eds.). Vaccine design: The subunit and adjuvant approach: Springer; 2012.

Blythe MJ, Flower DR. Benchmarking B cell epitope prediction: underperformance of existing methods. Protein Sci. 2005; 14(1):246-8.

Saha S, Raghava GP. Prediction of continuous B-cell epitopes in an antigen using recurrent neural network. Proteins. 2006; 65(1):40-8.

Ahmad TA, Eweida AE, Sheweita SA. B-cell epitope mapping for the design of vaccines and effective diagnostics. Trials Vaccinol. 2016; 5:71-83.

El-Manzalawy Y, Honavar V. Recent advances in B-cell epitope prediction methods. Immunome Res. 2010; 6 Suppl 2(Suppl 2):S2.

Saha S., Raghava G.P.S. BcePred: Prediction of Continuous B-Cell Epitopes in Antigenic Sequences Using Physico-chemical Properties. In: Nicosia G., Cutello V., Bentley P.J., Timmis J. (eds) Artificial Immune Systems. ICARIS 2004. Lecture Notes in Computer Science, vol 3239. Springer, Berlin, Heidelberg.

Kringelum JV, Lundegaard C, Lund O, Nielsen M. Reliable B cell epitope predictions: impacts of method development and improved benchmarking. PLoS Comput Biol. 2012; 8(12):e1002829.

Branger C, Chatrenet B, Gauvrit A, Aviat F, Aubert A, Bach JM, et al. Protection against Leptospira interrogans sensu lato challenge by DNA immunization with the gene encoding hemolysin-associated protein 1. Infect Immun. 2005; 73(7):4062-9.

Maneewatch S, Tapchaisri P, Sakolvaree Y, Klaysing B, Tongtawe P, Chaisri U, et al. OmpL1 DNA vaccine cross-protects against heterologous Leptospira spp. challenge. Asian Pac J Allergy Immunol. 2007; 25(1):75-82.

Nascimento IP, Leite LC. Recombinant vaccines and the development of new vaccine strategies. Braz J Med Biol Res. 2012; 45(12):1102-11.

He HJ, Wang WY, Wu ZD, Lv ZY, Li J, Tan LZ. Protection of guinea pigs against Leptospira interrogans serovar Lai by LipL21 DNA vaccine. Cell Mol Immunol. 2008; 5(5):385-91.

Feng CY, Li QT, Zhang XY, Dong K, Hu BY, Guo XK. Immune strategies using single-component LipL32 and multi-component recombinant LipL32-41-OmpL1 vaccines against leptospira. Braz J Med Biol Res. 2009; 42(9):796-803.

Hartwig DD, Forster KM, Oliveira TL, Amaral M, McBride AJ, Dellagostin OA. A prime-boost strategy using the novel vaccine candidate, LemA, protects hamsters against leptospirosis. Clin Vaccine Immunol. 2013; 20(5):747-52.

Buaklin A, Palaga T, Hannaman D, Kerdkaew R, Patarakul K, Jacquet A. Optimization of the immunogenicity of a DNA vaccine encoding a bacterial outer membrane lipoprotein. Mol Biotechnol. 2014; 56(10):903-10.

Oliveira TL, Grassmann AA, Schuch RA, Seixas Neto AC, Mendonça M, Hartwig DD, et al. Evaluation of the Leptospira interrogans Outer Membrane Protein OmpL37 as a Vaccine Candidate. PLoS One. 2015; 10(11):e0142821.

Forster KM, Hartwig DD, Oliveira TL, Bacelo KL, Schuch R, Amaral MG, et al. DNA prime-protein boost based vaccination with a conserved region of leptospiral immunoglobulin-like A and B proteins enhances protection against leptospirosis. Mem Inst Oswaldo Cruz. 2015; 110(8):989-95.

Larsen JE, Lund O, Nielsen M. Improved method for predicting linear B-cell epitopes. Immunome Res. 2006; 2:2.

Haste Andersen P, Nielsen M, Lund O. Prediction of residues in discontinuous B-cell epitopes using protein 3D structures. Protein Sci. 2006; 15(11):2558-67.




DOI: https://doi.org/10.52547/jcbior.1.1.32

Refbacks

  • There are currently no refbacks.


Copyright (c) 2020 © The Author(s)

Creative Commons License
This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.