NDLI: The unusual chaperonins of Mycobacterium tuberculosis.

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The unusual chaperonins of Mycobacterium tuberculosis.

Content Provider	Semantic Scholar
Author	Qamra, Rohini Mande, Shekhar C. Coates, Anthony R. M. Henderson, Brian
Copyright Year	2005
Abstract	Heat shock proteins (Hsps), also known as molecular chaperones, are a diverse set of proteins that mediate the correct folding, assembly, transport and degradation of other proteins. In addition, Hsps have been shown to play a variety of important roles in immunity, thereby representing prominent antigens in the humoral and cellular immune response. Chaperonins form a sub-group of molecular chaperones that are found in all domains of life. Chaperonins in all bacteria are encoded by the essential groEL and groES genes, also called cpn60 and cpn10 arranged on the bicistronic groESL operon. Interestingly, Mycobacterium tuberculosis contains two copies of the cpn60 genes. The existence of a duplicate set of cpn60 genes in M. tuberculosis, however, has been perplexing. Cpn10 and Cpn60s of M. tuberculosis have been shown to be highly antigenic in nature, eliciting strong B- and T-cell immune responses. Recent work has shown intriguing structural, biochemical and signaling properties of the M. tuberculosis chaperonins. This review details the recent developments in the study of the M. tuberculosis chaperonins.
Starting Page	1
Ending Page	3
Page Count	3
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://www.cdfd.org.in/images/Academicprojects/2005_Rohini_Tuberculosis-pro2.pdf
PubMed reference number	16253564v1
Volume Number	85
Issue Number	5-6
Journal	Tuberculosis
Language	English
Access Restriction	Open
Subject Keyword	Chronic Lymphocytic Leukemia Copy (object) Genus Mycobacterium HSPE1 gene Heat Shock Protein 27 Heat shock proteins Immunity Molecular Chaperones Mycobacterium tuberculosis complex genotype:Prid:Pt:Isolate:Nar Operon chaperonin varicella-zoster immune globulin
Content Type	Text
Resource Type	Article

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