Home > Research > Publications & Outputs > Synthetic phosphooligosaccharide fragments of l...

Research

Links

Text available via DOI:

Keywords

View graph of relations

Synthetic phosphooligosaccharide fragments of lipophosphoglycan as acceptors for Leishmania-major alpha-Dmannosylphosphate transferase.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Published

Standard

Synthetic phosphooligosaccharide fragments of lipophosphoglycan as acceptors for Leishmania-major alpha-Dmannosylphosphate transferase. / Brown, Gavin M.; Millar, Alan R.; Masterson, Claire et al.
In: European Journal of Biochemistry, Vol. 242, No. 2, 12.1996, p. 410-416.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Brown, GM, Millar, AR, Masterson, C, Brimacombe, JS, Nikolaev, AV & Ferguson, MA 1996, 'Synthetic phosphooligosaccharide fragments of lipophosphoglycan as acceptors for Leishmania-major alpha-Dmannosylphosphate transferase.', European Journal of Biochemistry, vol. 242, no. 2, pp. 410-416. https://doi.org/10.1111/j.1432-1033.1996.0410r.x

APA

Brown, G. M., Millar, A. R., Masterson, C., Brimacombe, J. S., Nikolaev, A. V., & Ferguson, M. A. (1996). Synthetic phosphooligosaccharide fragments of lipophosphoglycan as acceptors for Leishmania-major alpha-Dmannosylphosphate transferase. European Journal of Biochemistry, 242(2), 410-416. https://doi.org/10.1111/j.1432-1033.1996.0410r.x

Vancouver

Brown GM, Millar AR, Masterson C, Brimacombe JS, Nikolaev AV, Ferguson MA. Synthetic phosphooligosaccharide fragments of lipophosphoglycan as acceptors for Leishmania-major alpha-Dmannosylphosphate transferase. European Journal of Biochemistry. 1996 Dec;242(2):410-416. doi: 10.1111/j.1432-1033.1996.0410r.x

Author

Brown, Gavin M. ; Millar, Alan R. ; Masterson, Claire et al. / Synthetic phosphooligosaccharide fragments of lipophosphoglycan as acceptors for Leishmania-major alpha-Dmannosylphosphate transferase. In: European Journal of Biochemistry. 1996 ; Vol. 242, No. 2. pp. 410-416.

Bibtex

@article{1d1a211f9965410cb41a58e5c61e7e2b,
title = "Synthetic phosphooligosaccharide fragments of lipophosphoglycan as acceptors for Leishmania-major alpha-Dmannosylphosphate transferase.",
abstract = "Protozoan parasites of the genus Leishmania synthesise lipophosphoglycans, phosphoglycans and proteophosphoglycans that contain phosphosaccharide-repeat units of [-6Galβ1-4Manα1-P-]. In this study, a GDP-Man-dependent α-mannosylphosphate-transferase activity was detected in washed Leishmania major membranes using synthetic phospho-oligosaccharide fragments of lipophosphoglycan as acceptor substrates. The divalent-cation-dependent α-mannosylphosphate-transferase activity had an apparent Km for GDP-Man of about 15–20 μM and a pH optimum of 7.0. The activity showed a requirement for a non-reducing terminal βGal residue and for one or more phosphodiester units preceding the acceptor site. Based on these results, the activity may be defined as a GDP-Man:Galβ1-4Manα1-P-R α-mannosylphosphate-transferase. This acceptor specificity is consistent with a role for the α-mannosylphosphate transferase in the elongation of phosphosaccharide-repeat domains of Leishmania glycoconjugates rather than in the priming of these domains. An identical or similar activity must exist in the amastigote forms of the Leishmania that produce and secrete proteophosphoglycan material and the activity therefore represents a feasible target for the development of chemotherapeutics.",
keywords = "lipophosphoglycan • proteophosphoglycan • Leishmania • phospho-oligosaccharide biosynthesis",
author = "Brown, {Gavin M.} and Millar, {Alan R.} and Claire Masterson and Brimacombe, {John S.} and Nikolaev, {Andrei V.} and Ferguson, {Michael A.}",
year = "1996",
month = dec,
doi = "10.1111/j.1432-1033.1996.0410r.x",
language = "English",
volume = "242",
pages = "410--416",
journal = "European Journal of Biochemistry",
issn = "0014-2956",
publisher = "Wiley-Blackwell",
number = "2",

}

RIS

TY - JOUR

T1 - Synthetic phosphooligosaccharide fragments of lipophosphoglycan as acceptors for Leishmania-major alpha-Dmannosylphosphate transferase.

AU - Brown, Gavin M.

AU - Millar, Alan R.

AU - Masterson, Claire

AU - Brimacombe, John S.

AU - Nikolaev, Andrei V.

AU - Ferguson, Michael A.

PY - 1996/12

Y1 - 1996/12

N2 - Protozoan parasites of the genus Leishmania synthesise lipophosphoglycans, phosphoglycans and proteophosphoglycans that contain phosphosaccharide-repeat units of [-6Galβ1-4Manα1-P-]. In this study, a GDP-Man-dependent α-mannosylphosphate-transferase activity was detected in washed Leishmania major membranes using synthetic phospho-oligosaccharide fragments of lipophosphoglycan as acceptor substrates. The divalent-cation-dependent α-mannosylphosphate-transferase activity had an apparent Km for GDP-Man of about 15–20 μM and a pH optimum of 7.0. The activity showed a requirement for a non-reducing terminal βGal residue and for one or more phosphodiester units preceding the acceptor site. Based on these results, the activity may be defined as a GDP-Man:Galβ1-4Manα1-P-R α-mannosylphosphate-transferase. This acceptor specificity is consistent with a role for the α-mannosylphosphate transferase in the elongation of phosphosaccharide-repeat domains of Leishmania glycoconjugates rather than in the priming of these domains. An identical or similar activity must exist in the amastigote forms of the Leishmania that produce and secrete proteophosphoglycan material and the activity therefore represents a feasible target for the development of chemotherapeutics.

AB - Protozoan parasites of the genus Leishmania synthesise lipophosphoglycans, phosphoglycans and proteophosphoglycans that contain phosphosaccharide-repeat units of [-6Galβ1-4Manα1-P-]. In this study, a GDP-Man-dependent α-mannosylphosphate-transferase activity was detected in washed Leishmania major membranes using synthetic phospho-oligosaccharide fragments of lipophosphoglycan as acceptor substrates. The divalent-cation-dependent α-mannosylphosphate-transferase activity had an apparent Km for GDP-Man of about 15–20 μM and a pH optimum of 7.0. The activity showed a requirement for a non-reducing terminal βGal residue and for one or more phosphodiester units preceding the acceptor site. Based on these results, the activity may be defined as a GDP-Man:Galβ1-4Manα1-P-R α-mannosylphosphate-transferase. This acceptor specificity is consistent with a role for the α-mannosylphosphate transferase in the elongation of phosphosaccharide-repeat domains of Leishmania glycoconjugates rather than in the priming of these domains. An identical or similar activity must exist in the amastigote forms of the Leishmania that produce and secrete proteophosphoglycan material and the activity therefore represents a feasible target for the development of chemotherapeutics.

KW - lipophosphoglycan • proteophosphoglycan • Leishmania • phospho-oligosaccharide biosynthesis

U2 - 10.1111/j.1432-1033.1996.0410r.x

DO - 10.1111/j.1432-1033.1996.0410r.x

M3 - Journal article

VL - 242

SP - 410

EP - 416

JO - European Journal of Biochemistry

JF - European Journal of Biochemistry

SN - 0014-2956

IS - 2

ER -