Heparan sulfate 3-O-sulfotransferase isoform 5 generates both an antithrombin-binding site and an entry receptor for herpes simplex virus, type 1

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Fältnamn	Indikatorer	Metadata
000		03326naa a2200361 4500
001		oai:lup.lub.lu.se:785a61c6-854b-4ef3-bac3-790fd6dadb0b
003		SwePub
008		160401s2002 \| \|\|\|\|\|\|\|\|\|\|\|000 \|\|eng\|
024	7	a https://lup.lub.lu.se/record/3261362 URI
024	7	a https://doi.org/10.1074/jbc.M2042092002 DOI
040		a (SwePub)lu
041		a engb eng
042		9 SwePub
072	7	a art2 swepub-publicationtype
072	7	a ref2 swepub-contenttype
100	1	a Xia, Guoqing4 aut
245	1 0	a Heparan sulfate 3-O-sulfotransferase isoform 5 generates both an antithrombin-binding site and an entry receptor for herpes simplex virus, type 1
264	1	c 2002
520		a Heparan sulfate 3-O-sulfotransferase transfers sulfate to the 3-OH position of a glucosamine residue of heparan sulfate (HS) to form 3-O-sulfated HS. The 3-O-sulfated glucosamine residue contributes to two important biological functions of HS: binding to antithrombin and thereby carrying anticoagulant activity, and binding to herpes simplex viral envelope glycoprotein D to serve as an entry receptor for herpes simplex virus 1. A total of five HS 3-O-sulfotransferase isoforms were reported previously. Here we report the isolation and characterization of a novel HS 3-O-sulfotransferase isoform, designated as HS 3-O-sulfotransferase isoform 5 (3-OST-5). 3-OST-5 cDNA was isolated from a human placenta cDNA library and expressed in COS-7 cells. The disaccharide analysis of 3-OST-5-modified HS revealed that 3-OST-5 generated at least three 3-O-sulfated disaccharides as follows: IdoUA2S-AnMan3S, GlcUA-AnMan3S6S, and IdoUA2S-AnMan3S6S. Transfection of the plasmid expressing 3-OST-5 rendered wild type Chinese hamster ovary cells susceptible to the infection by herpes simplex virus 1, suggesting that 3-OST-5-modified HS serves as an entry receptor for herpes simplex virus 1. In addition, 3-OST-5-modified HS bound to herpes simplex viral envelope protein glycoprotein D. Furthermore, we found that 3-OST-5-modified HS also bound to antithrombin, suggesting that 3-OST-5 also produces anticoagulant HS. In summary, our results indicate that a new member of 3-OST family generates both anticoagulant HS and an entry receptor for herpes simplex virus 1. These results provide a new insight regarding the mechanism for the biosynthesis of biologically active HS.
650	7	a MEDICIN OCH HÄLSOVETENSKAPx Medicinska och farmaceutiska grundvetenskaperx Cell- och molekylärbiologi0 (SwePub)301082 hsv//swe
650	7	a MEDICAL AND HEALTH SCIENCESx Basic Medicinex Cell and Molecular Biology0 (SwePub)301082 hsv//eng
700	1	a Chen, JH4 aut
700	1	a Tiwari, V4 aut
700	1	a Ju, WJ4 aut
700	1	a Li, JP4 aut
700	1	a Malmström, Andersu Lund University,Lunds universitet,Matrixbiologi,Forskargrupper vid Lunds universitet,Matrix Biology,Lund University Research Groups4 aut0 (Swepub:lu)medk-ama
700	1	a Shukla, D4 aut
700	1	a Liu, J4 aut
710	2	a Matrixbiologib Forskargrupper vid Lunds universitet4 org
773	0	t Journal of Biological Chemistryg 277:40, s. 37912-37919q 277:40<37912-37919x 1083-351X
856	4	u http://dx.doi.org/10.1074/jbc.M204209200x freey FULLTEXT
856	4 8	u https://lup.lub.lu.se/record/326136
856	4 8	u https://doi.org/10.1074/jbc.M204209200

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Av författaren/redakt...: Xia, Guoqing; Chen, JH; Tiwari, V; Ju, WJ; Li, JP; Malmström, Ander ...; visa fler...; Shukla, D; Liu, J; visa färre...

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