Secondary extended mannan side chains and attachment of the arabinan in mycobacterial lipoarabinomannan

Autor:	Michael R. McNeil, Claudia M. Boot, Shiva K. Angala, Wei Li, Mary Jackson
Jazyk:	angličtina
Rok vydání:	2020
Předmět:	Antigenicity Cell Biochemistry Article lcsh:Chemistry 03 medical and health sciences chemistry.chemical_compound Biosynthesis immune system diseases hemic and lymphatic diseases Materials Chemistry medicine Environmental Chemistry 030304 developmental biology Mannan 0303 health sciences Lipoarabinomannan 030306 microbiology Protein primary structure General Chemistry Periplasmic space bacterial infections and mycoses carbohydrates (lipids) medicine.anatomical_structure chemistry lcsh:QD1-999 lipids (amino acids peptides and proteins) Cell envelope
Zdroj:	Communications Chemistry, Vol 3, Iss 1, Pp 1-15 (2020) Commun Chem
ISSN:	2399-3669
DOI:	10.1038/s42004-020-00356-3
Popis:	Mycobacterial lipoarabinomannan (LAM) is in an essential cell envelope lipopolysaccharide anchored both to the plasma and outer membranes. To understand critical biological questions such as the biosynthesis, spatial organization of LAM within the cell envelope, structural remodeling during growth, and display or lack of display of LAM-based antigenicity requires a basic understanding of the primary structure of the mannan, arabinan and how they are attached to each other. Herein, using enzymatic digestions and high-resolution mass spectrometry, we show that the arabinan component of LAM is attached at the non-reducing end of the mannan rather than to internal regions. Further, we show the presence of secondary extended mannan side chains attached to the internal mannan region. Such findings lead to a significant revision of the structure of LAM and lead to guidance of biosynthetic studies and to hypotheses of the role of LAM both in the periplasm and outside the cell as a fundamental part of the dynamic mycobacterial cell envelope. Lipoarabinomannan is a carbohydrate expressed on mycobacterial cell surfaces and implicated in host-pathogen interactions, but its structure is not well-characterised. Here mass spectrometry studies of enzymatic digests reveal the presence of secondary extended mannan pendants and indicate a revised structure for the connectivity of the core domains.
Databáze:	OpenAIRE
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