Biochemical characterization of recombinant guaA-encoded guanosine monophosphate synthetase (EC 6.3.5.2) from Mycobacterium tuberculosis H37Rv strain

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Biochemical characterization of PE_PGRS61 family protein of Mycobacterium tuberculosis H37Rv reveals the binding ability to fibronectin

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biochemical characterization of pe_pgrs61 family protein of mycobacterium tuberculosis h37rv reveals the binding ability to fibronectin

objective(s): the periodic binding of protein expressed by mycobacterium tuberculosis h37rv with the host cell receptor molecules i.e. fibronectin (fn) is gaining significance because of its adhesive properties.  the genome sequencing of m. tuberculosis h37rv revealed that the proline-glutamic (pe) proteins contain polymorphic gc-rich repetitive sequences (pgrs) which have clinical importance i...

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Gene replacement and quantitative mass spectrometry approaches validate guanosine monophosphate synthetase as essential for Mycobacterium tuberculosis growth

Guanosine monophosphate synthetase (GMPS), encoded by guaA gene, is a key enzyme for guanine nucleotide biosynthesis in Mycobacterium tuberculosis. The guaA gene from several bacterial pathogens has been shown to be involved in virulence; however, no information about the physiological effect of direct guaA deletion in M. tuberculosis has been described so far. Here, we demonstrated that the gu...

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Biochemical characterization of PE_PGRS61 family protein of Mycobacterium tuberculosis H37Rv reveals the binding ability to fibronectin

OBJECTIVES The periodic binding of protein expressed by Mycobacterium tuberculosis H37Rv with the host cell receptor molecules i.e. fibronectin (Fn) is gaining significance because of its adhesive properties. The genome sequencing of M. tuberculosis H37Rv revealed that the proline-glutamic (PE) proteins contain polymorphic GC-rich repetitive sequences (PGRS) which have clinical importance in pa...

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ژورنال

عنوان ژورنال: Archives of Biochemistry and Biophysics

سال: 2012

ISSN: 0003-9861

DOI: 10.1016/j.abb.2011.11.013