Mapping the laminin-binding and adhesive domain of the cell surface-associated Hlp/LBP protein from Mycobacterium leprae

Lima, Cristiana Soares de; Zulianello, Laurence; Marques, Maria Angela M.; Kim, Heejin; Portugal, Michelle Iespa; Antunes, Sérgio Luiz Gomes; Menozzi, Franco D.; Ottenhoff, Tom; Brennan, Patrick J.; Pessolani, Maria Cristina Vidal

doi:10.1016/j.micinf.2005.02.013

Cited by 42 publications

(46 citation statements)

References 37 publications

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“…Hlp and HBHA are well known as extracellular matrixbinding proteins. While HBHA binds heparan sulfate (13,20), Hlp has been described as a multifunctional adhesin able to interact with laminin, hyaluronic acid, heparan sulfate, and collagen (14,53,(71)(72)(73). Previous studies have shown the in vivo expression of both proteins by M. leprae (62,71).…”

Section: Discussionmentioning

confidence: 99%

Interaction of Mycobacterium leprae with Human Airway Epithelial Cells: Adherence, Entry, Survival, and Identification of Potential Adhesins by Surface Proteome Analysis

et al. 2013

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f This study examined the in vitro interaction between Mycobacterium leprae, the causative agent of leprosy, and human alveolar and nasal epithelial cells, demonstrating that M. leprae can enter both cell types and that both are capable of sustaining bacterial survival. Moreover, delivery of M. leprae to the nasal septum of mice resulted in macrophage and epithelial cell infection in the lung tissue, sustaining the idea that the airways constitute an important M. leprae entry route into the human body. Since critical aspects in understanding the mechanisms of infection are the identification and characterization of the adhesins involved in pathogen-host cell interaction, the nude mouse-derived M. leprae cell surface-exposed proteome was studied to uncover potentially relevant adhesin candidates. A total of 279 cell surface-exposed proteins were identified based on selective biotinylation, streptavidin-affinity purification, and shotgun mass spectrometry; 11 of those proteins have been previously described as potential adhesins. In vitro assays with the recombinant forms of the histone-like protein (Hlp) and the heparin-binding hemagglutinin (HBHA), considered to be major mycobacterial adhesins, confirmed their capacity to promote bacterial attachment to epithelial cells. Taking our data together, they suggest that the airway epithelium may act as a reservoir and/or portal of entry for M. leprae in humans. Moreover, our report sheds light on the potentially critical adhesins involved in M. leprae-epithelial cell interaction that may be useful in designing more effective tools for leprosy control.

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Section: Discussionmentioning

confidence: 99%

Interaction of Mycobacterium leprae with Human Airway Epithelial Cells: Adherence, Entry, Survival, and Identification of Potential Adhesins by Surface Proteome Analysis

et al. 2013

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“…In the former case, the binding of surfaceassociated histone-like protein (HlpA) from Streptococcus gallolyticus to colon adenocarcinoma cells 29) and the binding of Hlp/LBP from Mycobacterium leprae to the extracellular matrix, 30) and in the latter case, the adhesion of 987P fimbriae from enterotoxigenic E. coli to histone H1 receptor 23) were reported. This indicates that histone proteins may be important factors in establishing infections by pathogenic bacteria in the human gastrointestinal tract.…”

Section: Discussionmentioning

confidence: 99%

An Adhesin-Like Protein, Lam29, fromLactobacillus mucosaeME-340 Binds to Histone H3 and Blood Group Antigens in Human Colonic Mucus

Watanabe

Kinoshita

Huang

et al. 2012

Bioscience, Biotechnology, and Biochemistry

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“…HupB, which has also been named HLPMt (histone-like protein in M. tuberculosis), mycobacterial DNA-binding protein 1 (MDP1), and laminin-binding protein (LBP) have been implicated in several biological functions, including immunoproliferation (39), adhesion (40), assembly of the cell wall (41), and recombination (42). The association of HupB with iron metabolism in M. tuberculosis was first demonstrated by Yeruva and coworkers, who identified the protein as a 28-kDa cell wall-associated protein in organisms (14) grown in iron-limiting medium (0.02 g Fe ml Ϫ1 ; 0.36 M Fe).…”

Section: Transcriptional Regulation Of Mycobactin Biosynthesis: Role mentioning

confidence: 99%

Iron Homeostasis in Mycobacterium tuberculosis: Mechanistic Insights into Siderophore-Mediated Iron Uptake

2016

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Mycobacterium tuberculosis requires iron for normal growth but faces a limitation of the metal ion due to its low solubility at biological pH and the withholding of iron by the mammalian host. The pathogen expresses the Fe 3؉ -specific siderophores mycobactin and carboxymycobactin to chelate the metal ion from insoluble iron and the host proteins transferrin, lactoferrin, and ferritin. Siderophore-mediated iron uptake is essential for the survival of M. tuberculosis, as knockout mutants, which were defective in siderophore synthesis or uptake, failed to survive in low-iron medium and inside macrophages. But as excess iron is toxic due to its catalytic role in the generation of free radicals, regulation of iron uptake is necessary to maintain optimal levels of intracellular iron. The focus of this review is to present a comprehensive overview of iron homeostasis in M. tuberculosis that is discussed in the context of mycobactin biosynthesis, transport of iron across the mycobacterial cell envelope, and storage of excess iron. The clinical significance of the serum iron status and the expression of the iron-regulated protein HupB in tuberculosis (TB) patients is presented here, highlighting the potential of HupB as a marker, notably in extrapulmonary TB cases.

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Mapping the laminin-binding and adhesive domain of the cell surface-associated Hlp/LBP protein from Mycobacterium leprae

Cited by 42 publications

References 37 publications

Interaction of Mycobacterium leprae with Human Airway Epithelial Cells: Adherence, Entry, Survival, and Identification of Potential Adhesins by Surface Proteome Analysis

Interaction of Mycobacterium leprae with Human Airway Epithelial Cells: Adherence, Entry, Survival, and Identification of Potential Adhesins by Surface Proteome Analysis

An Adhesin-Like Protein, Lam29, fromLactobacillus mucosaeME-340 Binds to Histone H3 and Blood Group Antigens in Human Colonic Mucus

Iron Homeostasis in Mycobacterium tuberculosis: Mechanistic Insights into Siderophore-Mediated Iron Uptake

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