Immunodominance of LipL3293-272 peptides ... - Science Direct

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detection and acts as an antigen in IgM- and IgG-enzyme- .... wells were then blocked with 150 ml of blocking reagent (1%. BSA in PBS) at 37 C for 1 h. Serum ...
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Journal of Microbiology, Immunology and Infection (2018) xx, 1e12

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Original Article

Immunodominance of LipL3293e272 peptides revealed by leptospirosis sera and therapeutic monoclonal antibodies Tippawan Pissawong a, Santi Maneewatchararangsri b,*, Nonglucksanawan Ritthisunthorn b, Ngamphol Soonthornworasiri c, Onrapak Reamtong b, Poom Adisakwattana d, Thareerat Kalambaheti e, Urai Chaisri f, Galayanee Doungchawee g a

Chulabhorn International College of Medicine, Thammasat University, Pathumthani 12120, Thailand Department of Molecular Tropical Medicine and Genetics, Faculty of Tropical Medicine, Mahidol University, Bangkok 10400, Thailand c Department of Tropical Hygiene, Faculty of Tropical Medicine, Mahidol University, Bangkok 10400, Thailand d Department of Helminthology, Faculty of Tropical Medicine, Mahidol University, Bangkok 10400, Thailand e Department of Microbiology and Immunology, Faculty of Tropical Medicine, Mahidol University, Bangkok 10400, Thailand f Department of Tropical Pathology, Faculty of Tropical Medicine, Mahidol University, Bangkok 10400, Thailand g Department of Pathobiology, Faculty of Science, Mahidol University, Bangkok 10400, Thailand b

Received 18 May 2017; received in revised form 30 October 2017; accepted 12 December 2017

Available online - - -

KEYWORDS Leptospira spp.; LipL32; IgM-dominant LipL32 peptide; IgG-dominant LipL32 peptide; Therapeutic LipL32 epitopes

Abstract Background/Purpose: Leptospirosis is a neglected zoonosis, imposing significant human and veterinary public health burdens. In this study, recombinant LipL3293e147 and LipL32148e184 middle domain of LipL3293e184, and LipL32171e214, and LipL32215e272 of c-terminal LipL32171e272 truncations were defined for immunodominance of the molecule during Leptospira infections revealed by leptospirosis sera. Results: IgM-dominant was directed to highly surface accessible LipL32148e184 and Lipl32171e214. IgG dominance of LipL32148e184 revealed by rabbit anti-Leptospira sera and convalescent leptospirosis paired sera were mapped to highly accessible surface of middle LipL32148e184 truncation whereas two LipL32148e184 and LipL32215e272 truncations were IgG-dominant when revealed by single leptospirosis sera. The IgM-dominant of LipL32148e214 and IgG-dominant LipL32148e184

* Corresponding author. E-mail address: [email protected] (S. Maneewatchararangsri). https://doi.org/10.1016/j.jmii.2017.12.006 1684-1182/Copyright ª 2018, Taiwan Society of Microbiology. Published by Elsevier Taiwan LLC. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). Please cite this article in press as: Pissawong T, et al., Immunodominance of LipL3293e272 peptides revealed by leptospirosis sera and therapeutic monoclonal antibodies, Journal of Microbiology, Immunology and Infection (2018), https://doi.org/10.1016/ j.jmii.2017.12.006

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T. Pissawong et al. peptides have highly conserved amino acids of 70% identity among pathogenic and intermediate Leptospira species and were mapped to the highly surface accessible area of LipL32 molecule that mediated interaction of host components. IgG dominance of two therapeutic epitopes located at LipL32243e253 and LipL32122e130 of mAbLPF1 and mAbLPF2, respectively has been shown less IgG-dominant (