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1. (CSDB ID: 12806) | report error |
| b-D-Araf-(1-2)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-a-D-Araf | Show graphically |
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Mycobacterium tuberculosis
(NCBI TaxID 1773,
species name lookup)
]
txbiomed.orgMannose-capped lipoarabinomannan (ManLAM), present in all members of the Mycobacterium tuberculosis complex and in other pathogenic Mycobacterium spp, is a high molecular mass amphipathic lipoglycan with a defined critical role in mycobacterial survival during infection. In particular, ManLAM is well-characterized for its importance in providing M. tuberculosis a safe portal of entry to phagocytes, regulating the intracellular trafficking network, as well as immune responses of infected host cells. These ManLAM immunological characteristics are thought to be linked to the subtle but unique and well-defined structural characteristics of this molecule, including but not limited to the degree of acylation, the length of the D-mannan and D-arabinan cores, the length of the mannose caps, as well as the presence of other acidic constituents such as succinates, lactates and/or malates, and also the presence of 5-methylthioxylosyl. The impact of all these structural features on ManLAM spatial conformation and biological functions during M. tuberculosis infection is still uncertain. In this review, we dissect the relationship between ManLAM structure and biological function addressing how this relationship determines M. tuberculosis interactions with host cells, and how it aids this exceptional pathogen during the course of infection.
Mycobacterium tuberculosis, tuberculosis, biological functions, host cell response, mannose-capped lipoarabinomannan
Structure type: structural motif or average structure|
2. (CSDB ID: 12989) | report error |
| b-D-Araf-(1-2)-a-D-Araf-(1-5)-+ | b-D-Araf-(1-2)-a-D-Araf-(1-3)-a-D-Araf-(1-5)-a-D-Araf | Show graphically |
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Mycobacterium tuberculosis
(NCBI TaxID 1773,
species name lookup)
]txbiomed.orgMannose-capped lipoarabinomannan (ManLAM), present in all members of the Mycobacterium tuberculosis complex and in other pathogenic Mycobacterium spp, is a high molecular mass amphipathic lipoglycan with a defined critical role in mycobacterial survival during infection. In particular, ManLAM is well-characterized for its importance in providing M. tuberculosis a safe portal of entry to phagocytes, regulating the intracellular trafficking network, as well as immune responses of infected host cells. These ManLAM immunological characteristics are thought to be linked to the subtle but unique and well-defined structural characteristics of this molecule, including but not limited to the degree of acylation, the length of the D-mannan and D-arabinan cores, the length of the mannose caps, as well as the presence of other acidic constituents such as succinates, lactates and/or malates, and also the presence of 5-methylthioxylosyl. The impact of all these structural features on ManLAM spatial conformation and biological functions during M. tuberculosis infection is still uncertain. In this review, we dissect the relationship between ManLAM structure and biological function addressing how this relationship determines M. tuberculosis interactions with host cells, and how it aids this exceptional pathogen during the course of infection.
Mycobacterium tuberculosis, tuberculosis, biological functions, host cell response, mannose-capped lipoarabinomannan
Structure type: structural motif or average structure|
3. (CSDB ID: 22329) | report error |
| b-D-Araf-(1-2)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-a-D-Araf | Show graphically |
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Mycobacterium tuberculosis
(NCBI TaxID 1773,
species name lookup)
]txbiomed.org>; D. Chatterjee <delphi.chatterjeecolostate.edu>The presence of lipoarabinomannan (LAM) in the Mycobacterium tuberculosis (Mtb) cell envelope was first reported close to 100 years ago. Since then, numerous studies have been dedicated to the isolation, purification, structural definition, and elucidation of the biological properties of Mtb LAM. In this review, we present a brief historical perspective on the discovery of Mtb LAM and the herculean efforts devoted to structurally characterizing the molecule because of its unique structural and biological features. The significance of LAM remains high to this date, mainly due to its distinct immunological properties in conjunction with its role as a biomarker for diagnostic tests due to its identification in urine, and thus can serve as a point-of-care diagnostic test for tuberculosis (TB). In recent decades, LAM has been thoroughly studied and massive amounts of information on this intriguing molecule are now available. In this review, we give the readers a historical perspective and an update on the current knowledge of LAM with information on the inherent carbohydrate composition, which is unique due to the often puzzling sugar residues that are specifically found on LAM. We then guide the readers through the complex and myriad immunological outcomes, which are strictly dependent on LAM's chemical structure. Furthermore, we present issues that remain unresolved and represent the immediate future of LAM research. Addressing the chemistry, functions, and roles of LAM will lead to innovative ways to manipulate the processes that involve this controversial and fascinating biomolecule.
Mycobacteria, lipoarabinomannan, Mycobacterium tuberculosis, lipoglycan, tuberculosis
Structure type: structural motif or average structure|
4. (CSDB ID: 27051) | report error |
| b-D-Araf-(1-2)-a-D-Araf-(1-5)-+ | b-D-Araf-(1-2)-a-D-Araf-(1-3)-a-D-Araf-(1-5)-a-D-Araf | Show graphically |
|
Show legend Show as text |
Mycobacterium tuberculosis
(NCBI TaxID 1773,
species name lookup)
]txbiomed.org>; D. Chatterjee <delphi.chatterjeecolostate.edu>The presence of lipoarabinomannan (LAM) in the Mycobacterium tuberculosis (Mtb) cell envelope was first reported close to 100 years ago. Since then, numerous studies have been dedicated to the isolation, purification, structural definition, and elucidation of the biological properties of Mtb LAM. In this review, we present a brief historical perspective on the discovery of Mtb LAM and the herculean efforts devoted to structurally characterizing the molecule because of its unique structural and biological features. The significance of LAM remains high to this date, mainly due to its distinct immunological properties in conjunction with its role as a biomarker for diagnostic tests due to its identification in urine, and thus can serve as a point-of-care diagnostic test for tuberculosis (TB). In recent decades, LAM has been thoroughly studied and massive amounts of information on this intriguing molecule are now available. In this review, we give the readers a historical perspective and an update on the current knowledge of LAM with information on the inherent carbohydrate composition, which is unique due to the often puzzling sugar residues that are specifically found on LAM. We then guide the readers through the complex and myriad immunological outcomes, which are strictly dependent on LAM's chemical structure. Furthermore, we present issues that remain unresolved and represent the immediate future of LAM research. Addressing the chemistry, functions, and roles of LAM will lead to innovative ways to manipulate the processes that involve this controversial and fascinating biomolecule.
Mycobacteria, lipoarabinomannan, Mycobacterium tuberculosis, lipoglycan, tuberculosis
Structure type: structural motif or average structure| New query | Export IDs | Home | Help |
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