N-linked glycosylation is required for optimal function of Kaposi's sarcoma herpesvirus-encoded, but not cellular, interleukin 6.
N-linked glycosylation is required for optimal function of Kaposi's sarcoma herpesvirus-encoded, but not cellular, interleukin 6.
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DOI:
10.1084/jem.20031205
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发表时间:
2004-02-16
期刊:
影响因子:
--
通讯作者:
Miller G
中科院分区:
文献类型:
--
作者:
Dela Cruz CS;Lee Y;Viswanathan SR;El-Guindy AS;Gerlach J;Nikiforow S;Shedd D;Gradoville L;Miller G
Kaposi's sarcoma–associated herpesvirus interleukin-6 (vIL-6) is a structural and functional homologue of the human cytokine IL-6 (hIL-6). hIL-6 and vIL-6 exhibit similar biological functions and both act via the gp130 receptor subunit to activate the Janus tyrosine kinase (JAK)1 and signal transducer and activator of transcription (STAT)1/3 pathway. Here we show that vIL-6 is N-linked glycosylated at N78 and N89 and demonstrate that N-linked glycosylation at site N89 of vIL-6 markedly enhances binding to gp130, signaling through the JAK1-STAT1/3 pathway and functions in a cytokine-dependent cell proliferation bioassay. Although hIL-6 is also N-glycosylated at N73 and multiply O-glycosylated, neither N-linked nor O-linked glycosylation is necessary for IL-6 receptor α–dependent binding to gp130 or signaling through JAK1-STAT1/3. As distinct from vIL-6, unglycosylated hIL-6 is as potent as glycosylated hIL-6 in stimulating B cell proliferation. These findings highlight distinct functional roles of N-linked glycosylation in viral and cellular IL-6.
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影响因子:
3.8
作者:
BOCK, GH;LONG, CA;NELSON, DL
通讯作者:
NELSON, DL
影响因子:
82.9
作者:
Nicholas, J;Ruvolo, VR;Reitz, MS
通讯作者:
Reitz, MS
影响因子:
56.9
作者:
Chatterjee, M;Osborne, J;Moore, PS
通讯作者:
Moore, PS
影响因子:
2.9
作者:
Chow, DC;Ho, J;Garcia, KC
通讯作者:
Garcia, KC
DOI:
10.1111/j.1432-1033.1993.tb17624.x
发表时间:
1993-02-01
期刊:
EUROPEAN JOURNAL OF BIOCHEMISTRY
影响因子:
--
作者:
KODAMA, S;TSUJIMOTO, M;KOBATA, A
通讯作者:
KOBATA, A