Deciphering the function of YcbK lipoprotein-like hypo-thetical protein from Klebsiella pneumoniae MGH 78578.

Klebsiella pneumoniae is a Gram negative opportunistic pathogen which causes respiratory infection among immunocompromised patients. Recently more extended-spectrum beta-lactamase-producing K. pneumoniae strains are emerging worldwide making treatment for this bacterium more difficult. Approximately...

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Main Authors: Boon, Aun Teh, Choi, Sy Bing, Mohd Najimuddin, Mohd Nazalan, Salleh, Abu Bakar, A. Wahab, Habibah, Mohd Yahaya, Normi
Format: Conference or Workshop Item
Language:English
English
Published: 2012
Online Access:http://psasir.upm.edu.my/id/eprint/27345/
http://psasir.upm.edu.my/id/eprint/27345/1/ID%2027345.pdf
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author Boon, Aun Teh
Choi, Sy Bing
Mohd Najimuddin, Mohd Nazalan
Salleh, Abu Bakar
A. Wahab, Habibah
Mohd Yahaya, Normi
author_facet Boon, Aun Teh
Choi, Sy Bing
Mohd Najimuddin, Mohd Nazalan
Salleh, Abu Bakar
A. Wahab, Habibah
Mohd Yahaya, Normi
author_sort Boon, Aun Teh
building UPM Institutional Repository
collection Online Access
description Klebsiella pneumoniae is a Gram negative opportunistic pathogen which causes respiratory infection among immunocompromised patients. Recently more extended-spectrum beta-lactamase-producing K. pneumoniae strains are emerging worldwide making treatment for this bacterium more difficult. Approximately 20% of the genome of K. pneumoniae MGH 78578 encodes hypothetical proteins. Hypothetical proteins are proteins with unknown function where their sequences and structures are largely non-similar with other known proteins. Deciphering the functions of hypothetical proteins of this pathogen may give insight to possible new mechanisms leading to potential drug targets in the future. In this study, a particular lipoprotein-like hypothetical protein, YcbK, from K. pneumoniae MGH 78578 was cloned and characterized. Expression of YcbK in Escherichia coli JE5505 lipoprotein- deficient strain interestingly showed the presence of film-like material on the surface of the cells. In addition, the colonies on agar plates appeared to be smoother and more opaque than the negative control. Bioinformatics analysis on YcbK revealed it contains a putative conserved domain belonging to the Peptidase M15_3 superfamily. In silico homology modeling of the protein utilizing this conserved domain revealed that it preserves a Zn binding motif with two conserved His and Asp residues important for chelation of the metal ion. All the results obtained point to the possibility of YcbK adopting the function as a metallopeptidase with an important role in cell wall architecture similar with a few other peptidases in the family.
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institution Universiti Putra Malaysia
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language English
English
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publishDate 2012
recordtype eprints
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spelling upm-273452014-04-08T09:19:35Z http://psasir.upm.edu.my/id/eprint/27345/ Deciphering the function of YcbK lipoprotein-like hypo-thetical protein from Klebsiella pneumoniae MGH 78578. Boon, Aun Teh Choi, Sy Bing Mohd Najimuddin, Mohd Nazalan Salleh, Abu Bakar A. Wahab, Habibah Mohd Yahaya, Normi Klebsiella pneumoniae is a Gram negative opportunistic pathogen which causes respiratory infection among immunocompromised patients. Recently more extended-spectrum beta-lactamase-producing K. pneumoniae strains are emerging worldwide making treatment for this bacterium more difficult. Approximately 20% of the genome of K. pneumoniae MGH 78578 encodes hypothetical proteins. Hypothetical proteins are proteins with unknown function where their sequences and structures are largely non-similar with other known proteins. Deciphering the functions of hypothetical proteins of this pathogen may give insight to possible new mechanisms leading to potential drug targets in the future. In this study, a particular lipoprotein-like hypothetical protein, YcbK, from K. pneumoniae MGH 78578 was cloned and characterized. Expression of YcbK in Escherichia coli JE5505 lipoprotein- deficient strain interestingly showed the presence of film-like material on the surface of the cells. In addition, the colonies on agar plates appeared to be smoother and more opaque than the negative control. Bioinformatics analysis on YcbK revealed it contains a putative conserved domain belonging to the Peptidase M15_3 superfamily. In silico homology modeling of the protein utilizing this conserved domain revealed that it preserves a Zn binding motif with two conserved His and Asp residues important for chelation of the metal ion. All the results obtained point to the possibility of YcbK adopting the function as a metallopeptidase with an important role in cell wall architecture similar with a few other peptidases in the family. 2012 Conference or Workshop Item NonPeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/27345/1/ID%2027345.pdf Boon, Aun Teh and Choi, Sy Bing and Mohd Najimuddin, Mohd Nazalan and Salleh, Abu Bakar and A. Wahab, Habibah and Mohd Yahaya, Normi (2012) Deciphering the function of YcbK lipoprotein-like hypo-thetical protein from Klebsiella pneumoniae MGH 78578. In: Annual Symposium Frontiers in Biological Catalysis, 10-12 Jan. 2012, United Kingdom. . English
spellingShingle Boon, Aun Teh
Choi, Sy Bing
Mohd Najimuddin, Mohd Nazalan
Salleh, Abu Bakar
A. Wahab, Habibah
Mohd Yahaya, Normi
Deciphering the function of YcbK lipoprotein-like hypo-thetical protein from Klebsiella pneumoniae MGH 78578.
title Deciphering the function of YcbK lipoprotein-like hypo-thetical protein from Klebsiella pneumoniae MGH 78578.
title_full Deciphering the function of YcbK lipoprotein-like hypo-thetical protein from Klebsiella pneumoniae MGH 78578.
title_fullStr Deciphering the function of YcbK lipoprotein-like hypo-thetical protein from Klebsiella pneumoniae MGH 78578.
title_full_unstemmed Deciphering the function of YcbK lipoprotein-like hypo-thetical protein from Klebsiella pneumoniae MGH 78578.
title_short Deciphering the function of YcbK lipoprotein-like hypo-thetical protein from Klebsiella pneumoniae MGH 78578.
title_sort deciphering the function of ycbk lipoprotein-like hypo-thetical protein from klebsiella pneumoniae mgh 78578.
url http://psasir.upm.edu.my/id/eprint/27345/
http://psasir.upm.edu.my/id/eprint/27345/1/ID%2027345.pdf