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Surface proteomics and label-free quantification of Leptospira interrogans serovar Pomona

Leptospirosis is a re-emerging zoonosis with a global distribution. Surface-exposed outer membrane proteins (SE-OMPs) are crucial for bacterial–host interactions. SE-OMPs locate and expose their epitope on cell surface where is easily accessed by host molecules. This study aimed to screen for surfac...

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Autores principales: Techawiwattanaboon, Teerasit, Thaibankluay, Praparat, Kreangkaiwal, Chahya, Sathean-Anan-Kun, Suwitra, Khaenam, Prasong, Makjaroen, Jiradej, Pisitkun, Trairak, Patarakul, Kanitha
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8659334/
https://www.ncbi.nlm.nih.gov/pubmed/34843470
http://dx.doi.org/10.1371/journal.pntd.0009983
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author Techawiwattanaboon, Teerasit
Thaibankluay, Praparat
Kreangkaiwal, Chahya
Sathean-Anan-Kun, Suwitra
Khaenam, Prasong
Makjaroen, Jiradej
Pisitkun, Trairak
Patarakul, Kanitha
author_facet Techawiwattanaboon, Teerasit
Thaibankluay, Praparat
Kreangkaiwal, Chahya
Sathean-Anan-Kun, Suwitra
Khaenam, Prasong
Makjaroen, Jiradej
Pisitkun, Trairak
Patarakul, Kanitha
author_sort Techawiwattanaboon, Teerasit
collection PubMed
description Leptospirosis is a re-emerging zoonosis with a global distribution. Surface-exposed outer membrane proteins (SE-OMPs) are crucial for bacterial–host interactions. SE-OMPs locate and expose their epitope on cell surface where is easily accessed by host molecules. This study aimed to screen for surface-exposed proteins and their abundance profile of pathogenic Leptospira interrogans serovar Pomona. Two complementary approaches, surface biotinylation and surface proteolytic shaving, followed by liquid chromatography tandem-mass spectrometry (LC-MS/MS) were employed to identify SE-OMPs of intact leptospires. For quantitative comparison, in-depth label-free analysis of SE-OMPs obtained from each method was performed using MaxQuant. The total number of proteins identified was 1,001 and 238 for surface biotinylation and proteinase K shaving, respectively. Among these, 39 were previously known SE-OMPs and 68 were predicted to be localized on the leptospiral surface. Based on MaxQuant analysis for relative quantification, six known SE-OMPs including EF- Tu, LipL21, LipL41, LipL46, Loa22, and OmpL36, and one predicted SE-OMPs, LipL71 were found in the 20 most abundant proteins, in which LipL41 was the highest abundant SE-OMP. Moreover, uncharacterized LIC14011 protein (LIP3228 ortholog in serovar Pomona) was identified as a novel predicted surface βb-OMP. High-abundance leptospiral SE-OMPs identified in this study may play roles in virulence and infection and are potential targets for development of vaccine or diagnostic tests for leptospirosis.
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spelling pubmed-86593342021-12-10 Surface proteomics and label-free quantification of Leptospira interrogans serovar Pomona Techawiwattanaboon, Teerasit Thaibankluay, Praparat Kreangkaiwal, Chahya Sathean-Anan-Kun, Suwitra Khaenam, Prasong Makjaroen, Jiradej Pisitkun, Trairak Patarakul, Kanitha PLoS Negl Trop Dis Research Article Leptospirosis is a re-emerging zoonosis with a global distribution. Surface-exposed outer membrane proteins (SE-OMPs) are crucial for bacterial–host interactions. SE-OMPs locate and expose their epitope on cell surface where is easily accessed by host molecules. This study aimed to screen for surface-exposed proteins and their abundance profile of pathogenic Leptospira interrogans serovar Pomona. Two complementary approaches, surface biotinylation and surface proteolytic shaving, followed by liquid chromatography tandem-mass spectrometry (LC-MS/MS) were employed to identify SE-OMPs of intact leptospires. For quantitative comparison, in-depth label-free analysis of SE-OMPs obtained from each method was performed using MaxQuant. The total number of proteins identified was 1,001 and 238 for surface biotinylation and proteinase K shaving, respectively. Among these, 39 were previously known SE-OMPs and 68 were predicted to be localized on the leptospiral surface. Based on MaxQuant analysis for relative quantification, six known SE-OMPs including EF- Tu, LipL21, LipL41, LipL46, Loa22, and OmpL36, and one predicted SE-OMPs, LipL71 were found in the 20 most abundant proteins, in which LipL41 was the highest abundant SE-OMP. Moreover, uncharacterized LIC14011 protein (LIP3228 ortholog in serovar Pomona) was identified as a novel predicted surface βb-OMP. High-abundance leptospiral SE-OMPs identified in this study may play roles in virulence and infection and are potential targets for development of vaccine or diagnostic tests for leptospirosis. Public Library of Science 2021-11-29 /pmc/articles/PMC8659334/ /pubmed/34843470 http://dx.doi.org/10.1371/journal.pntd.0009983 Text en © 2021 Techawiwattanaboon et al https://creativecommons.org/licenses/by/4.0/This is an open access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Techawiwattanaboon, Teerasit
Thaibankluay, Praparat
Kreangkaiwal, Chahya
Sathean-Anan-Kun, Suwitra
Khaenam, Prasong
Makjaroen, Jiradej
Pisitkun, Trairak
Patarakul, Kanitha
Surface proteomics and label-free quantification of Leptospira interrogans serovar Pomona
title Surface proteomics and label-free quantification of Leptospira interrogans serovar Pomona
title_full Surface proteomics and label-free quantification of Leptospira interrogans serovar Pomona
title_fullStr Surface proteomics and label-free quantification of Leptospira interrogans serovar Pomona
title_full_unstemmed Surface proteomics and label-free quantification of Leptospira interrogans serovar Pomona
title_short Surface proteomics and label-free quantification of Leptospira interrogans serovar Pomona
title_sort surface proteomics and label-free quantification of leptospira interrogans serovar pomona
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8659334/
https://www.ncbi.nlm.nih.gov/pubmed/34843470
http://dx.doi.org/10.1371/journal.pntd.0009983
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