J Immunol 2001, 166:7477–7485.PubMed 26. Pathak SK, Basu S, Bhattacharyya selleck screening library A, Kundu M, Basu J: Mycobacterium tuberculosis lipoarabinomannan-mediated IRAK-M

induction negatively regulates Toll-like receptor-dependent interleukin-12 p40 production in macrophages. J Biol Chem 2005, 280:42794–42800.PubMedCrossRef 27. Lowe DM, Redford PS, Wilkinson RJ, O’Garra A, Martineau AR: Neutrophils in tuberculosis: friend or foe? Trends Immunol 2012, 1:14–25.CrossRef 28. Weischenfeldt J, Porse B: Bone Marrow-Derived Macrophages (BMM): Isolation and Applications. Cold Spring Harb Protoc 2008. Competing interests The authors declare that they have no competing interests. Authors’ contributions MRMA performed the experiments and prepared the figures; EPA evaluated growth curves of mycobacteria in MΦ and broth; VL cultured and characterized the mycobacterial strains; TVP established the in vitro model of BMDM infection; EPA, SCMR and FMA carried out the immunoassays; EBL, MRIL and MRMA analyzed the data; EL and MRMA conceived of, designed the study and wrote the manuscript, MREL revised the manuscript critically. Entinostat price All authors read and approved the final manuscript.”
“Selleckchem PFT�� Background Mycobacterium tuberculosis is one of the leading causes of death due to a single infectious agent. Its success is based on perfect adaptation to the human host

and the conditions prevailing in infected cells and tissues such as hypoxia, nutrient starvation, low pH and the presence of antimicrobial substances. By adapting their gene expression, growth and metabolism to these environmental conditions, the bacteria are able to persist over long periods of time inside immune cells within granuloma in a latent Carbohydrate state until possible reactivation and outbreak of disease. To be able to combat the disease, it is necessary to understand the molecular mechanisms regulating mycobacterial intracellular persistence, latency

and reactivation. A class of proteins implicated in regulating latency are the mycobacterial histone-like proteins (Hlp) [1]. Hlp have been identified in pathogenic as well as environmental mycobacteria [2, 3]. Proteins belonging to this class have been given different designations in different mycobacterial species such as HLPMt or HupB in M. tuberculosis[3, 4], MDP1 (mycobacterial DNA-binding protein 1) in Mycobacterium bovis BCG [5], Hlp in Mycobacterium smegmatis[2] and ML-LBP21 in Mycobacterium leprae[6]. They are composed of an extremely basic C-terminal part homologous to eukaryotic histone H1 and an N-terminal region similar to HU from Escherichia coli[3, 5]. Hlp expression is developmentally regulated and up-regulation was observed in dormant M. smegmatis[2] and stationary cultures from M. bovis BCG [5]. It is an immunogenic protein detectable in tuberculosis patients [7].