Open AccessSignal Transduction by Human Herpesvirus 8 Viral Interleukin-6 (vIL-6) IsModulated by the Nonsignaling gp80 Subunit of the IL-6 Receptor Complex and Is Distinct from Signaling Induced by Human IL-6
Author(s) -
Fang Hu,
John Nicholas
Publication year - 2006
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.00767-06
Subject(s) - biology , glycoprotein 130 , signal transduction , phosphorylation , tyrosine phosphorylation , interleukin 6 receptor , hek 293 cells , microbiology and biotechnology , interleukin 12 receptor, beta 1 subunit , stat3 , receptor , protein subunit , biochemistry , interleukin , cytokine , genetics , gene
Humanherpesvirus 8 (HHV-8) viral interleukin-6 (vIL-6) mediates signalingthrough the gp130 signal transducer but unlike human IL-6 (hIL-6) doesnot require the nonsignaling gp80 α subunit of the IL-6receptor complex. By utilizing a gp80-refractory vIL-6 variant,vIL-6(R189L), we found that signal transduction, as measured by STAT1and STAT3 activation and gp130 tyrosine phosphorylation ingp80+ /gp130+ HEK293T cells, wasmodulated by gp80. Furthermore, the signaling and BAF-130 cellgrowth-promoting activities of vIL-6 and hIL-6 could be distinguished,and exogenous addition of soluble gp80 enhanced cell growth supportedby vIL-6. Our findings demonstrate that gp80 can modulate vIL-6activity and that vIL-6 and hIL-6 signaling are not directlyequivalent.