Výsledky vyhledávání - "Mitali Choudhury"

Iron uptake and transport by the carboxymycobactin-mycobactin siderophore machinery of Mycobacterium tuberculosis is dependent on the iron-regulated protein HupB

Autor: Manjula Sritharan, Mitali Choudhury, Naveen Kumar, Sasan Salimi, Nagu Prakash Prabhu, Kavya Desai, Tejaswi Naidu Koduru

Publikováno v: BioMetals. 34:511-528

Iron-starved Mycobacterium tuberculosis utilises the carboxymycobactin-mycobactin siderophore machinery to acquire iron. These two siderophores have high affinity for ferric iron and can withdraw the metal ion from insoluble iron hydroxides and iron-

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ad933c94a49927af3fd3e646cd8be099
https://doi.org/10.1007/s10534-021-00292-2

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Th2 immune response by the iron-regulated protein HupB of Mycobacterium tuberculosis

Autor: Jahnavi Virivinti, Manjula Sritharan, Subhakar Kandi, Mitali Choudhury, Venkataraman Sritharan

Publikováno v: The Indian journal of tuberculosis. 69(1)

Background HupB is an iron-regulated protein essential for the growth of Mycobacterium tuberculosis inside macrophages. To investigate if HupB induced a dominant Th2 type immune response, we studied the effect of rHupB on PBMCs from TB patients and b

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::433d7dae2a2c2b68706c10363301ce3c
https://pubmed.ncbi.nlm.nih.gov/35074158

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Histone methyltransferase SUV39H1 participates in host defense by methylating mycobacterial histone-like protein HupB

Autor: Imtiyaz Yaseen, Sanjeev Khosla, Mitali Choudhury, Manjula Sritharan

Publikováno v: The EMBO journal. 37(2)

Host cell defense against an invading pathogen depends upon various multifactorial mechanisms, several of which remain undiscovered. Here, we report a novel defense mechanism against mycobacterial infection that utilizes the histone methyltransferase

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d04fe6f3220157c77d7bf103cfd82126
https://pubmed.ncbi.nlm.nih.gov/29301860

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Highly immunoreactive antibodies against the rHup-F2 fragment (aa 63–161) of the iron-regulated HupB protein of Mycobacterium tuberculosis and its potential for the serodiagnosis of extrapulmonary and recurrent tuberculosis

Autor: Subha Sivakolundu, R. Chaurasia, N. Chouhan, Mitali Choudhury, N. Sritharan, Manjula Sritharan, P. P. Rao

Publikováno v: European Journal of Clinical Microbiology & Infectious Diseases. 34:33-40

HupB is an iron-regulated protein in Mycobacterium tuberculosis that functions as a positive regulator of mycobactin biosynthesis. It is essential for the growth and survival of the pathogen inside macrophages. Previously, using the full-length rHupB

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::32aebc932255bf1f50303ecfa8d237ff
https://doi.org/10.1007/s10096-014-2203-y

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Iron-Regulated Protein HupB of Mycobacterium tuberculosis Positively Regulates Siderophore Biosynthesis and Is Essential for Growth in Macrophages

Autor: Paul R. Wheeler, Suhail Yousuf, Satya Deo Pandey, Stephen V. Gordon, Mitali Choudhury, Manjula Sritharan, Akash Ranjan

Publikováno v: Journal of Bacteriology. 196:1853-1865

Mycobacterium tuberculosis expresses the 28-kDa protein HupB (Rv2986c) and the Fe 3+ -specific high-affinity siderophores mycobactin and carboxymycobactin upon iron limitation. The objective of this study was to understand the functional role of HupB

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff989f39b443315b30aed262b7b9f1d4
https://doi.org/10.1128/jb.01483-13

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