The sodium/proline transporter PutP of Helicobacter pylori.

Helicobacter pylori is cause of chronic gastritis, duodenal ulcer and gastric carcinoma in humans. L-proline is a preferred energy source of the microaerophilic bacterium. Previous analyses revealed that HpputP and HpputA, the genes that are predicted to play a central role in proline metabolism as...

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Autores principales:	Araceli Rivera-Ordaz, Susanne Bracher, Sannia Sarrach, Zheng Li, Lei Shi, Matthias Quick, Daniel Hilger, Rainer Haas, Heinrich Jung
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/ede29dcd634a40bb9e6398ae8f541793
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spelling	oai:doaj.org-article:ede29dcd634a40bb9e6398ae8f5417932021-11-18T08:41:34ZThe sodium/proline transporter PutP of Helicobacter pylori.1932-620310.1371/journal.pone.0083576https://doaj.org/article/ede29dcd634a40bb9e6398ae8f5417932013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24358297/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Helicobacter pylori is cause of chronic gastritis, duodenal ulcer and gastric carcinoma in humans. L-proline is a preferred energy source of the microaerophilic bacterium. Previous analyses revealed that HpputP and HpputA, the genes that are predicted to play a central role in proline metabolism as they encode for the proline transporter and proline dehydrogenase, respectively, are essential for stomach colonization. Here, the molecular basis of proline transport in H. pylori by HpPutP was investigated experimentally for the first time. Measuring radiolabeled substrate transport in H. pylori and E. coli heterologously expressing HpputP as well as in proteoliposomes reconstituted with HpPutP, we demonstrate that the observed proline transport in H. pylori is mediated by HpPutP. HpPutP is specific and exhibits a high affinity for L-proline. Notably, L-proline transport is exclusively dependent on Na(+) as coupling ion, i.e., Na(+)/L-proline symport, reminiscent to the properties of PutP of E. coli even though H. pylori lives in a more acidic environment. Homology model-based structural comparisons and substitution analyses identified amino acids crucial for function. HpPutP-catalyzed proline uptake was efficiently inhibited by the known proline analogs 3,4-dehydro-D,L-proline and L-azetidine-2-carboxylic acid.Araceli Rivera-OrdazSusanne BracherSannia SarrachZheng LiLei ShiMatthias QuickDaniel HilgerRainer HaasHeinrich JungPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 12, p e83576 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Araceli Rivera-Ordaz Susanne Bracher Sannia Sarrach Zheng Li Lei Shi Matthias Quick Daniel Hilger Rainer Haas Heinrich Jung The sodium/proline transporter PutP of Helicobacter pylori.
description	Helicobacter pylori is cause of chronic gastritis, duodenal ulcer and gastric carcinoma in humans. L-proline is a preferred energy source of the microaerophilic bacterium. Previous analyses revealed that HpputP and HpputA, the genes that are predicted to play a central role in proline metabolism as they encode for the proline transporter and proline dehydrogenase, respectively, are essential for stomach colonization. Here, the molecular basis of proline transport in H. pylori by HpPutP was investigated experimentally for the first time. Measuring radiolabeled substrate transport in H. pylori and E. coli heterologously expressing HpputP as well as in proteoliposomes reconstituted with HpPutP, we demonstrate that the observed proline transport in H. pylori is mediated by HpPutP. HpPutP is specific and exhibits a high affinity for L-proline. Notably, L-proline transport is exclusively dependent on Na(+) as coupling ion, i.e., Na(+)/L-proline symport, reminiscent to the properties of PutP of E. coli even though H. pylori lives in a more acidic environment. Homology model-based structural comparisons and substitution analyses identified amino acids crucial for function. HpPutP-catalyzed proline uptake was efficiently inhibited by the known proline analogs 3,4-dehydro-D,L-proline and L-azetidine-2-carboxylic acid.
format	article
author	Araceli Rivera-Ordaz Susanne Bracher Sannia Sarrach Zheng Li Lei Shi Matthias Quick Daniel Hilger Rainer Haas Heinrich Jung
author_facet	Araceli Rivera-Ordaz Susanne Bracher Sannia Sarrach Zheng Li Lei Shi Matthias Quick Daniel Hilger Rainer Haas Heinrich Jung
author_sort	Araceli Rivera-Ordaz
title	The sodium/proline transporter PutP of Helicobacter pylori.
title_short	The sodium/proline transporter PutP of Helicobacter pylori.
title_full	The sodium/proline transporter PutP of Helicobacter pylori.
title_fullStr	The sodium/proline transporter PutP of Helicobacter pylori.
title_full_unstemmed	The sodium/proline transporter PutP of Helicobacter pylori.
title_sort	sodium/proline transporter putp of helicobacter pylori.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/ede29dcd634a40bb9e6398ae8f541793
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The sodium/proline transporter PutP of Helicobacter pylori.

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