期刊
TUBERCULOSIS
卷 95, 期 4, 页码 476-489出版社
CHURCHILL LIVINGSTONE
DOI: 10.1016/j.tube.2015.04.002
关键词
Mycobacterium tuberculosis; Dendritic cell; Innate immunity; Host response; Cell wall; Galactosamine; GalN; IL-10; DC-SIGN; Mycobacterium; Arabinogalactan; Human PBMC; PAMP; PRR; GalN-AG
资金
- National Institutes of Health/National Institute of Allergy and Infectious Diseases [AI064798]
- MRC [MR/J006874/1] Funding Source: UKRI
Slow-growing and pathogenic Mycobacterium spp. are characterized by the presence of galactosamine (GalN) that modifies the interior branched arabinosyl residues of the arabinogalactan (AG) that is a major heteropolysaccharide cell wall component. The availability of null mutants of the polyprenyl-phospho-Nacetylgalactosaminyl synthase (Rv3631, PpgS) and the (N-acetyl-) galactosaminyl transferase (Rv3779) of Mycobacterium tuberculosis (Mtb) has provided a means to elucidate the role of the GalN substituent of AG in terms of hostepathogen interactions. Comparisons of treating human peripheral blood monocytederived dendritic cells (hPMC-DCs) with wild-type, Rv3631 and Rv3779 mutant strains of Mtb revealed increased expression of DC maturation markers, decreased affinity for a soluble DC-SIGN probe, reduced IL-10 secretion and increased TLR-2-mediated NF-kB activation among GalN-deficient Mtb strains compared to GalN-producing strains. Analysis of surface expression of a panel of defined or putative DCSIGN ligands on both WT strains or either Rv3631 or Rv3779 mutant did not show significant differences suggesting that the role of the GalN substituent of AG may be to modulate access of the bacilli to immunologically-relevant receptor domains on DCs or contribute to higher ordered pathogen associated molecular pattern (PAMP)/pattern recognition receptor (PRR) interactions rather than the GalN-AG components having a direct immunological effect per se. (C) 2015 Elsevier Ltd. All rights reserved.
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