Functional and structural analysis of BPSS0140-BPSS0142 ABC transporter that mediates fructose import in Burkholderia pseudomallei

ATP-binding cassette (ABC) transporters mediate bacteria uptake or export of a variety of solutes across biological membranes. Bacterial uptake of the monosaccharides is important as a source of carbohydrate building blocks that contribute to the bacteria’s major structure. Burkholderia pseudomallei...

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Main Authors: Shu, Sian How, Su, Datt Lam, Sheila Nathan, Chieng, Sylvia
Format: Article
Language:English
Published: Penerbit Universiti Kebangsaan Malaysia 2022
Online Access:http://journalarticle.ukm.my/21690/
http://journalarticle.ukm.my/21690/1/ML%203.pdf
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author Shu, Sian How
Su, Datt Lam
Sheila Nathan,
Chieng, Sylvia
author_facet Shu, Sian How
Su, Datt Lam
Sheila Nathan,
Chieng, Sylvia
author_sort Shu, Sian How
building UKM Institutional Repository
collection Online Access
description ATP-binding cassette (ABC) transporters mediate bacteria uptake or export of a variety of solutes across biological membranes. Bacterial uptake of the monosaccharides is important as a source of carbohydrate building blocks that contribute to the bacteria’s major structure. Burkholderia pseudomallei is the etiological agent of melioidosis and within its genome, 33 genes related to monosaccharide ABC transporters have been predicted. The presence of these transporters is believed to assist in bacterial survival and adaptation in various environments. Despite a large number of genes in the genome, most of these systems have yet to be characterized, including the bpss0140-bpss0142 operon. Here, we predicted the 3D structure of each protein encoded by bpss0140-0142 and identified the specifically associated monosaccharides. In silico analyses of the structures demonstrated that BPSS0140 is a sugar-binding protein, BPSS0141 is a transmembrane permease and BPSS0142 is an ATPase. Through protein structure modeling and protein-ligand docking, several specific monosaccharide sugars were found to interact with the BPSS0140-BPSS0142 ABC transporter. To validate the in silico prediction, knock-out mutants for each of the genes were constructed. A growth profile between wild-type and mutants in an M9 medium supplemented with glucose, fructose, ribose, and galactose as predicted from the protein-ligand docking was then performed. The growth of mutants decreased significantly compared to the wild-type bacteria when grown in M9 supplemented with fructose as the sole carbon source indicating that this transporter is potentially the main fructose transporter in B. pseudomallei.
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spelling oai:generic.eprints.org:216902023-06-08T01:42:48Z http://journalarticle.ukm.my/21690/ Functional and structural analysis of BPSS0140-BPSS0142 ABC transporter that mediates fructose import in Burkholderia pseudomallei Shu, Sian How Su, Datt Lam Sheila Nathan, Chieng, Sylvia ATP-binding cassette (ABC) transporters mediate bacteria uptake or export of a variety of solutes across biological membranes. Bacterial uptake of the monosaccharides is important as a source of carbohydrate building blocks that contribute to the bacteria’s major structure. Burkholderia pseudomallei is the etiological agent of melioidosis and within its genome, 33 genes related to monosaccharide ABC transporters have been predicted. The presence of these transporters is believed to assist in bacterial survival and adaptation in various environments. Despite a large number of genes in the genome, most of these systems have yet to be characterized, including the bpss0140-bpss0142 operon. Here, we predicted the 3D structure of each protein encoded by bpss0140-0142 and identified the specifically associated monosaccharides. In silico analyses of the structures demonstrated that BPSS0140 is a sugar-binding protein, BPSS0141 is a transmembrane permease and BPSS0142 is an ATPase. Through protein structure modeling and protein-ligand docking, several specific monosaccharide sugars were found to interact with the BPSS0140-BPSS0142 ABC transporter. To validate the in silico prediction, knock-out mutants for each of the genes were constructed. A growth profile between wild-type and mutants in an M9 medium supplemented with glucose, fructose, ribose, and galactose as predicted from the protein-ligand docking was then performed. The growth of mutants decreased significantly compared to the wild-type bacteria when grown in M9 supplemented with fructose as the sole carbon source indicating that this transporter is potentially the main fructose transporter in B. pseudomallei. Penerbit Universiti Kebangsaan Malaysia 2022 Article PeerReviewed application/pdf en http://journalarticle.ukm.my/21690/1/ML%203.pdf Shu, Sian How and Su, Datt Lam and Sheila Nathan, and Chieng, Sylvia (2022) Functional and structural analysis of BPSS0140-BPSS0142 ABC transporter that mediates fructose import in Burkholderia pseudomallei. Malaysian Applied Biology, 51 (5). pp. 23-35. ISSN 0126-8643 https://jms.mabjournal.com/index.php/mab/index
spellingShingle Shu, Sian How
Su, Datt Lam
Sheila Nathan,
Chieng, Sylvia
Functional and structural analysis of BPSS0140-BPSS0142 ABC transporter that mediates fructose import in Burkholderia pseudomallei
title Functional and structural analysis of BPSS0140-BPSS0142 ABC transporter that mediates fructose import in Burkholderia pseudomallei
title_full Functional and structural analysis of BPSS0140-BPSS0142 ABC transporter that mediates fructose import in Burkholderia pseudomallei
title_fullStr Functional and structural analysis of BPSS0140-BPSS0142 ABC transporter that mediates fructose import in Burkholderia pseudomallei
title_full_unstemmed Functional and structural analysis of BPSS0140-BPSS0142 ABC transporter that mediates fructose import in Burkholderia pseudomallei
title_short Functional and structural analysis of BPSS0140-BPSS0142 ABC transporter that mediates fructose import in Burkholderia pseudomallei
title_sort functional and structural analysis of bpss0140-bpss0142 abc transporter that mediates fructose import in burkholderia pseudomallei
url http://journalarticle.ukm.my/21690/
http://journalarticle.ukm.my/21690/
http://journalarticle.ukm.my/21690/1/ML%203.pdf