LipL41, a hemin binding protein from Leptospira santarosai serovar Shermani.

Leptospirosis is one of the most widespread zoonotic diseases in the world. It is caused by the pathogen Leptospira that results in multiple-organ failure, in particular of the kidney. Outer membrane lipoprotein is the suspected virulence factor of Leptospira. In Leptospira spp LipL41 is one major l...

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Autores principales:	Ming-Hsing Lin, Yuan-Chih Chang, Chwan-Deng Hsiao, Shih-Hsun Huang, Min-Shi Wang, Yi-Ching Ko, Chih-Wei Yang, Yuh-Ju Sun
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/7391a2bc8f794378aac3da06b4db365b
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spelling	oai:doaj.org-article:7391a2bc8f794378aac3da06b4db365b2021-11-18T08:42:09ZLipL41, a hemin binding protein from Leptospira santarosai serovar Shermani.1932-620310.1371/journal.pone.0083246https://doaj.org/article/7391a2bc8f794378aac3da06b4db365b2013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24349474/?tool=EBIhttps://doaj.org/toc/1932-6203Leptospirosis is one of the most widespread zoonotic diseases in the world. It is caused by the pathogen Leptospira that results in multiple-organ failure, in particular of the kidney. Outer membrane lipoprotein is the suspected virulence factor of Leptospira. In Leptospira spp LipL41 is one major lipoprotein and is highly conserved. Previous study suggests that LipL41 bears hemin-binding ability and might play a possible role in iron regulation and storage. However, the characterization of hemin-binding ability of LipL41 is still unclear. Here the hemin-binding ability of LipL41 was examined, yielding a K d = 0.59 ± 0.14 μM. Two possible heme regulatory motifs (HRMs), C[P/S], were found in LipL41 at (140)Cys-Ser and (220)Cys-Pro. The mutation study indicates that Cys140 and Cys220 might be cooperatively involved in hemin binding. A supramolecular assembly of LipL41 was determined by transmission electron microscopy. The LipL41 oligomer consists of 36 molecules and folds as a double-layered particle. At the C-terminus of LipL41, there are two tetratricopeptide repeats (TPRs), which might be involved in the protein-protein interaction of the supramolecular assembly.Ming-Hsing LinYuan-Chih ChangChwan-Deng HsiaoShih-Hsun HuangMin-Shi WangYi-Ching KoChih-Wei YangYuh-Ju SunPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 12, p e83246 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Ming-Hsing Lin Yuan-Chih Chang Chwan-Deng Hsiao Shih-Hsun Huang Min-Shi Wang Yi-Ching Ko Chih-Wei Yang Yuh-Ju Sun LipL41, a hemin binding protein from Leptospira santarosai serovar Shermani.
description	Leptospirosis is one of the most widespread zoonotic diseases in the world. It is caused by the pathogen Leptospira that results in multiple-organ failure, in particular of the kidney. Outer membrane lipoprotein is the suspected virulence factor of Leptospira. In Leptospira spp LipL41 is one major lipoprotein and is highly conserved. Previous study suggests that LipL41 bears hemin-binding ability and might play a possible role in iron regulation and storage. However, the characterization of hemin-binding ability of LipL41 is still unclear. Here the hemin-binding ability of LipL41 was examined, yielding a K d = 0.59 ± 0.14 μM. Two possible heme regulatory motifs (HRMs), C[P/S], were found in LipL41 at (140)Cys-Ser and (220)Cys-Pro. The mutation study indicates that Cys140 and Cys220 might be cooperatively involved in hemin binding. A supramolecular assembly of LipL41 was determined by transmission electron microscopy. The LipL41 oligomer consists of 36 molecules and folds as a double-layered particle. At the C-terminus of LipL41, there are two tetratricopeptide repeats (TPRs), which might be involved in the protein-protein interaction of the supramolecular assembly.
format	article
author	Ming-Hsing Lin Yuan-Chih Chang Chwan-Deng Hsiao Shih-Hsun Huang Min-Shi Wang Yi-Ching Ko Chih-Wei Yang Yuh-Ju Sun
author_facet	Ming-Hsing Lin Yuan-Chih Chang Chwan-Deng Hsiao Shih-Hsun Huang Min-Shi Wang Yi-Ching Ko Chih-Wei Yang Yuh-Ju Sun
author_sort	Ming-Hsing Lin
title	LipL41, a hemin binding protein from Leptospira santarosai serovar Shermani.
title_short	LipL41, a hemin binding protein from Leptospira santarosai serovar Shermani.
title_full	LipL41, a hemin binding protein from Leptospira santarosai serovar Shermani.
title_fullStr	LipL41, a hemin binding protein from Leptospira santarosai serovar Shermani.
title_full_unstemmed	LipL41, a hemin binding protein from Leptospira santarosai serovar Shermani.
title_sort	lipl41, a hemin binding protein from leptospira santarosai serovar shermani.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/7391a2bc8f794378aac3da06b4db365b
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LipL41, a hemin binding protein from Leptospira santarosai serovar Shermani.

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