Structural and immunological characterization of an epitope within the PAN motif of ectodomain I in Babesia bovis apical membrane antigen 1 for vaccine development.

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Tytuł:: Structural and immunological characterization of an epitope within the PAN motif of ectodomain I in Babesia bovis apical membrane antigen 1 for vaccine development.
Autorzy:: Rittipornlertrak A; Graduate School of Veterinary Sciences, Chiang Mai University, Muang, Chiang Mai, Thailand.
Nambooppha B; Graduate School of Veterinary Sciences, Chiang Mai University, Muang, Chiang Mai, Thailand.
Muenthaisong A; Graduate School of Veterinary Sciences, Chiang Mai University, Muang, Chiang Mai, Thailand.
Punyapornwithaya V; Department of Food Animal Clinic, Faculty of Veterinary Medicine, Chiang Mai University, Muang, Chiang Mai, Thailand.
Tiwananthagorn S; Department of Veterinary Bioscience and Veterinary Public Health, Faculty of Veterinary Medicine, Chiang Mai University, Muang, Chiang Mai, Thailand.
Chung YT; Department of Veterinary Medicine, College of Veterinary Medicine, National Chung Hsing University, Taichung, Taichung, Taiwan.
Tuvshintulga B; National Research Center for Protozoan Diseases, Obihiro University of Agriculture and Veterinary Medicine, Obihiro, Hokkaido, Japan.
Sivakumar T; National Research Center for Protozoan Diseases, Obihiro University of Agriculture and Veterinary Medicine, Obihiro, Hokkaido, Japan.
Yokoyama N; National Research Center for Protozoan Diseases, Obihiro University of Agriculture and Veterinary Medicine, Obihiro, Hokkaido, Japan.
Sthitmatee N; Department of Veterinary Bioscience and Veterinary Public Health, Faculty of Veterinary Medicine, Chiang Mai University, Muang, Chiang Mai, Thailand.
Źródło:: PeerJ [PeerJ] 2021 Jul 16; Vol. 9, pp. e11765. Date of Electronic Publication: 2021 Jul 16 (Print Publication: 2021).
Typ publikacji:: Journal Article
Język:: English
Imprint Name(s):: Original Publication: Corte Madera, CA : PeerJ Inc.
References:: PLoS One. 2010 Feb 04;5(2):e9041. (PMID: 20140214)
BMC Genomics. 2019 Dec 24;20(Suppl 9):921. (PMID: 31874646)
PLoS One. 2012;7(12):e51023. (PMID: 23227229)
J Mol Biol. 2018 Jul 20;430(15):2244-2248. (PMID: 29391170)
Vaccine. 2017 Oct 27;35(45):6218-6227. (PMID: 28947345)
Mol Biochem Parasitol. 2001 Apr 6;113(2):279-87. (PMID: 11295182)
Int J Parasitol Drugs Drug Resist. 2019 Apr;9:87-92. (PMID: 30785049)
Infect Immun. 2009 Nov;77(11):4783-93. (PMID: 19720759)
Parasitology. 2004;129 Suppl:S247-69. (PMID: 15938514)
J Biol Chem. 2001 Aug 17;276(33):31311-20. (PMID: 11399764)
Infect Immun. 2015 Oct;83(10):3890-901. (PMID: 26195550)
Infect Immun. 2002 Jun;70(6):3101-10. (PMID: 12011004)
Infect Immun. 2006 May;74(5):2628-36. (PMID: 16622199)
Protein Sci. 2013 Jan;22(1):114-27. (PMID: 23169033)
Exp Parasitol. 2016 Jul;166:10-5. (PMID: 26965399)
Infect Immun. 2005 Jun;73(6):3677-85. (PMID: 15908397)
Vet Parasitol. 2006 May 31;138(1-2):88-96. (PMID: 16504404)
Mol Microbiol. 2000 Nov;38(4):706-18. (PMID: 11115107)
Nat Protoc. 2015 Jun;10(6):845-58. (PMID: 25950237)
Infect Immun. 2002 Oct;70(10):5822-6. (PMID: 12228313)
Exp Parasitol. 2015 Aug;155:40-5. (PMID: 25956948)
Science. 2005 Apr 15;308(5720):408-11. (PMID: 15731407)
Vet Parasitol. 2011 Jun 10;178(3-4):201-7. (PMID: 21324601)
Trends Parasitol. 2008 Feb;24(2):74-84. (PMID: 18226584)
Int J Parasitol. 2019 Feb;49(2):183-197. (PMID: 30690089)
Sci Rep. 2016 Dec 21;6:39462. (PMID: 28000709)
Infect Immun. 2005 Oct;73(10):6981-9. (PMID: 16177378)
Protein Eng. 2001 Sep;14(9):691-8. (PMID: 11707616)
Infect Immun. 2002 Dec;70(12):6961-7. (PMID: 12438375)
Cell Microbiol. 2014 May;16(5):642-56. (PMID: 24571085)
Int J Parasitol. 2013 Feb;43(2):125-32. (PMID: 23068911)
Ann N Y Acad Sci. 2000;916:540-5. (PMID: 11193669)
Transbound Emerg Dis. 2020 Jul;67 Suppl 2:60-68. (PMID: 31231975)
NPJ Vaccines. 2017;2:. (PMID: 28804644)
Nucleic Acids Res. 2015 Jul 1;43(W1):W174-81. (PMID: 25883148)
Infect Immun. 2001 May;69(5):3286-94. (PMID: 11292751)
Proc Natl Acad Sci U S A. 2003 Oct 14;100(21):12295-300. (PMID: 14526103)
BMC Bioinformatics. 2004 Aug 19;5:113. (PMID: 15318951)
Trends Parasitol. 2007 Sep;23(9):420-6. (PMID: 17656155)
Proc Natl Acad Sci U S A. 2005 Sep 6;102(36):12736-41. (PMID: 16129835)
PLoS Pathog. 2012;8(6):e1002755. (PMID: 22737069)
PLoS One. 2007 Oct 17;2(10):e1045. (PMID: 17940609)
Vet Parasitol. 2012 Jul 6;187(3-4):548-52. (PMID: 22309798)
Exp Parasitol. 2013 Nov;135(3):623-8. (PMID: 24090565)
OMICS. 2011 Sep;15(9):533-7. (PMID: 21815811)
Infect Immun. 2004 May;72(5):2947-55. (PMID: 15102807)
Infect Genet Evol. 2017 Oct;54:447-454. (PMID: 28807856)
Mol Biochem Parasitol. 1994 Sep;67(1):59-68. (PMID: 7838184)
Proc Natl Acad Sci U S A. 2011 Aug 9;108(32):13275-80. (PMID: 21788485)
Biochemistry. 2014 Nov 25;53(46):7310-20. (PMID: 25360546)
PLoS Pathog. 2007 Sep 7;3(9):1308-19. (PMID: 17907804)
Braz J Med Biol Res. 2012 May;45(5):376-85. (PMID: 22030866)
J Biol Chem. 2010 May 7;285(19):14815-22. (PMID: 20228060)
Contributed Indexing:: Keywords: Apical membrane antigen 1; Babesia bovis; Growth-inhibition; Invasion-inhibition; Synthetic peptide
Entry Date(s):: Date Created: 20210728 Latest Revision: 20220425
Update Code:: 20240105
PubMed Central ID:: PMC8288113
DOI:: 10.7717/peerj.11765
PMID:: 34316404
: Czasopismo naukowe

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Background: Bovine babesiosis caused by Babesia bovis (B. bovi s) has had a significant effect on the mobility and mortality rates of the cattle industry worldwide. Live-attenuated vaccines are currently being used in many endemic countries, but their wide use has been limited for a number of reasons. Although recombinant vaccines have been proposed as an alternative to live vaccines, such vaccines are not commercially available to date. Apical membrane antigen-1 (AMA-1) is one of the leading candidates in the development of a vaccine against diseases caused by apicomplexan parasite species. In Plasmodium falciparum ( P. falciparum ) AMA-1 (PfAMA-1), several antibodies against epitopes in the plasminogen, apple, and nematode (PAN) motif of PfAMA-1 domain I significantly inhibited parasite growth. Therefore, the purpose of this study was to predict an epitope from the PAN motif of domain I in the B. bovis AMA-1 (BbAMA-1) using a combination of linear and conformational B-cell epitope prediction software. The selected epitope was then bioinformatically analyzed, synthesized as a peptide (sBbAMA-1), and then used to immunize a rabbit. Subsequently, in vitro growth- and the invasion-inhibitory effects of the rabbit antiserum were immunologically characterized.
Results: Our results demonstrated that the predicted BbAMA-1 epitope was located on the surface-exposed α-helix of the PAN motif in domain I at the apex area between residues 181 and 230 with six polymorphic sites. Subsequently, sBbAMA-1 elicited antibodies capable of recognizing the native BbAMA-1 in immunoassays. Furthermore, anti-serum against sBbAMA-1 was immunologically evaluated for its growth- and invasion-inhibitory effects on B. bovis merozoites in vitro . Our results demonstrated that the rabbit anti-sBbAMA-1 serum at a dilution of 1:5 significantly inhibited ( p < 0.05) the growth of B. bovis merozoites by approximately 50-70% on days 3 and 4 of cultivation, along with the invasion of merozoites by approximately 60% within 4 h of incubation when compared to the control groups.
Conclusion: Our results indicate that the epitope predicted from the PAN motif of BbAMA-1 domain I is neutralization-sensitive and may serve as a target antigen for vaccine development against bovine babesiosis caused by B. bovis .
Competing Interests: The authors declare that they have no competing interests.
(© 2021 Rittipornlertrak et al.)

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