alexa Abstract | Mutation in pncA and distortion in PZase model structure as a basis of pyrazinamide resistance in Mycobacterium tuberculosis

Journal of Chemical and Pharmaceutical Research
Open Access

OMICS International organises 3000+ Global Conferenceseries Events every year across USA, Europe & Asia with support from 1000 more scientific Societies and Publishes 700+ Open Access Journals which contains over 50000 eminent personalities, reputed scientists as editorial board members.

Open Access Journals gaining more Readers and Citations

700 Journals and 15,000,000 Readers Each Journal is getting 25,000+ Readers

This Readership is 10 times more when compared to other Subscription Journals (Source: Google Analytics)

Original Articles Open Access

Abstract

Basis of pyrazinamide (PZA) resistance in M. tuberculosis is commonly associated with mutations in the pncA gene encoding pyrazinamidase (PZase) enzyme. The complete pncA open reading frame of 0,6 kb from R2 and R6 clinical isolate of PZA-resistant Mycobacterium tuberculosis has been characterized. A group mutations of T40C, G419A and A535G which link to amino acid replacements of Cis14Arg, Arg140His, Ser179Gly was identifed in pncA gene from the R2 PZA-resistant Mycobacterium tuberculosis, meanwhile a G511A mutation which replace amino acid of Ala171Thr was found in pncA gene from the R6 PZA-resistant strain. The structure modelling study to determine the effect of amino acid substitutions in the R2 and R6 PZase was carried out. Superposition of the generated model for R2 and R6 PZase with the wild-type PZase structure gave root mean square deviations (RMSD) of 0.24 and 0.23°A respectively, suggesting highly similar structures. However, the mutant structures of R2 and R6 PZase amended several interactions in its wild-type structure, expecially in the regions that contain the catalytic residues. The physical-chemical changes around the active site may be unfavorable for R2 and R6 PZase activities, and in turn create PZA resistance in both M. bacterium strains.

To read the full article Peer-reviewed Article PDF image

Author(s): Purkana Mukhlisin JA Marufa Wiwin Retnowatib Afaf Baktira andNi Nyoman T Puspaningsiha

Keywords

pncA gene, PZA resistance, PZase, Mycobacterium tuberculosis, Mutation

 
Peer Reviewed Journals
 
Make the best use of Scientific Research and information from our 700 + peer reviewed, Open Access Journals
International Conferences 2017-18
 
Meet Inspiring Speakers and Experts at our 3000+ Global Annual Meetings

Contact Us

Agri, Food, Aqua and Veterinary Science Journals

Dr. Krish

[email protected]

1-702-714-7001 Extn: 9040

Clinical and Biochemistry Journals

Datta A

[email protected]

1-702-714-7001Extn: 9037

Business & Management Journals

Ronald

[email protected]

1-702-714-7001Extn: 9042

Chemical Engineering and Chemistry Journals

Gabriel Shaw

[email protected]

1-702-714-7001 Extn: 9040

Earth & Environmental Sciences

Katie Wilson

[email protected]

1-702-714-7001Extn: 9042

Engineering Journals

James Franklin

[email protected]

1-702-714-7001Extn: 9042

General Science and Health care Journals

Andrea Jason

[email protected]

1-702-714-7001Extn: 9043

Genetics and Molecular Biology Journals

Anna Melissa

[email protected]

1-702-714-7001 Extn: 9006

Immunology & Microbiology Journals

David Gorantl

[email protected]

1-702-714-7001Extn: 9014

Informatics Journals

Stephanie Skinner

[email protected]

1-702-714-7001Extn: 9039

Material Sciences Journals

Rachle Green

[email protected]

1-702-714-7001Extn: 9039

Mathematics and Physics Journals

Jim Willison

[email protected]

1-702-714-7001 Extn: 9042

Medical Journals

Nimmi Anna

[email protected]

1-702-714-7001 Extn: 9038

Neuroscience & Psychology Journals

Nathan T

[email protected]

1-702-714-7001Extn: 9041

Pharmaceutical Sciences Journals

John Behannon

[email protected]

1-702-714-7001Extn: 9007

Social & Political Science Journals

Steve Harry

[email protected]

1-702-714-7001 Extn: 9042

 
© 2008-2017 OMICS International - Open Access Publisher. Best viewed in Mozilla Firefox | Google Chrome | Above IE 7.0 version
adwords