有哪些信誉好的足球投注网站an oligopeptide transporter of mycobacterium tuberculosis regulates cytokine release and apoptosis of infected macrophages结核分枝杆菌的寡肽转运体调节细胞因子释放和被感染的巨噬细胞的凋亡.pdfVIP
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an oligopeptide transporter of mycobacterium tuberculosis regulates cytokine release and apoptosis of infected macrophages结核分枝杆菌的寡肽转运体调节细胞因子释放和被感染的巨噬细胞的凋亡
An Oligopeptide Transporter of Mycobacterium
tuberculosis Regulates Cytokine Release and Apoptosis
of Infected Macrophages
1¤a. 2. 3 3 2
Arunava Dasgupta , Kamakshi Sureka , Devrani Mitra , Baisakhee Saha , Sourav Sanyal , Amit K.
3 2¤b 1¤c 1 2 2
Das , Parul Chakrabarti , Mary Jackson , Brigitte Gicquel , Manikuntala Kundu , Joyoti Basu *
´ ´ ´ ´
1 Unite de Genetique Mycobacterienne, Institut Pasteur, Paris, France, 2 Department of Chemistry, Bose Institute, Kolkata, India, 3 Department of Biotechnology, Indian
Institute of Technology, Kharagpur, India
Abstract
Background: The Mycobacterium tuberculosis genome encodes two peptide transporters encoded by Rv3665c-Rv3662c and
Rv1280c-Rv1283c. Both belong to the family of ABC transporters containing two nucleotide-binding subunits, two integral
membrane proteins and one substrate-binding polypeptide. However, little is known about their functions in M. tuberculosis. Here
we report functional characterization of the Rv1280c-Rv1283c-encoded transporter and its substrate-binding polypeptide OppAMTB.
Methodology/Principal Findings: OppAMTB was capable of binding the tripeptide glutathione and the nonapeptide
bradykinin, indicative of a somewhat broad substrate specificity. Amino acid residues G109, N110, N230, D494 and F496,
situated at the interface between domains I and III of OppA, were required for optimal peptide binding. Complementaton of
an oppA knockout mutant of M. smegmatis with OppAMTB confirmed the role of this trans
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