PMID- 11991991
OWN - NLM
STAT- MEDLINE
DCOM- 20020610
LR  - 20190508
IS  - 0022-538X (Print)
IS  - 1098-5514 (Electronic)
IS  - 0022-538X (Linking)
VI  - 76
IP  - 11
DP  - 2002 Jun
TI  - Identification of amino acid residues of gp130 signal transducer and gp80 alpha 
      receptor subunit that are involved in ligand binding and signaling by human 
      herpesvirus 8-encoded interleukin-6.
PG  - 5627-36
AB  - Human herpesvirus 8-encoded interleukin-6 (vIL-6) signals through the gp130 
      signal transducer but is not dependent on the IL-6 receptor alpha subunit (IL-6R, 
      gp80) that is required for signaling by endogenous IL-6 proteins; however, IL-6R 
      can enhance vIL-6 activity and can enable signaling through a gp130 variant, 
      gp130.PM5, that is itself unable to support vIL-6 signaling. These findings 
      suggest that the vIL-6-gp130 interactions are qualitatively different from those 
      of human IL-6 (hIL-6) and that vIL-6 signaling may be more promiscuous than that 
      of hIL-6 but that IL-6R may play a role in vIL-6 signaling in vivo. To examine 
      the receptor binding requirements of vIL-6, we have undertaken mutational 
      analyses of regions of gp130 and IL-6R potentially involved in interactions with 
      ligand or in functional complex formation and used these variants in functional, 
      ligand-binding, and receptor dimerization assays. The data presented identify 
      positions within two interstrand loops of the gp130 cytokine-receptor homology 
      domain that are important for vIL-6 signaling and vIL-6-induced receptor 
      dimerization and show that vIL-6, like hIL-6, can form complexes with IL-6R and 
      gp130 but that the roles of putative cytokine-binding residues of IL-6R in 
      ligand-induced functional complex formation are qualitatively different in the 
      case of vIL-6 and hIL-6.
FAU - Li, Hong
AU  - Li H
AD  - Molecular Virology Laboratories, Department of Oncology, Johns Hopkins 
      University, Baltimore, Maryland 21231, USA.
FAU - Nicholas, John
AU  - Nicholas J
LA  - eng
GR  - R01 CA076445/CA/NCI NIH HHS/United States
GR  - R01 CA083519/CA/NCI NIH HHS/United States
GR  - CA-76445/CA/NCI NIH HHS/United States
GR  - CA-83519/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Virol
JT  - Journal of virology
JID - 0113724
RN  - 0 (Amino Acids)
RN  - 0 (Antigens, CD)
RN  - 0 (IL6ST protein, human)
RN  - 0 (Interleukin-6)
RN  - 0 (Ligands)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Receptors, Interleukin-6)
RN  - 0 (interleukin-6 receptor alpha)
RN  - 133483-10-0 (Cytokine Receptor gp130)
RN  - OF5P57N2ZX (Alanine)
SB  - IM
MH  - Alanine
MH  - Amino Acids
MH  - Antigens, CD/genetics/*metabolism
MH  - Binding Sites
MH  - Cell Line, Transformed
MH  - Cytokine Receptor gp130
MH  - Herpesvirus 8, Human/genetics/*metabolism
MH  - Humans
MH  - Interleukin-6/genetics/*metabolism
MH  - Ligands
MH  - Membrane Glycoproteins/genetics/*metabolism
MH  - Mutagenesis, Site-Directed
MH  - Receptors, Interleukin-6/genetics/*metabolism
MH  - *Signal Transduction
MH  - Tumor Cells, Cultured
PMC - PMC137051
EDAT- 2002/05/07 10:00
MHDA- 2002/06/11 10:01
PMCR- 2002/06/01
CRDT- 2002/05/07 10:00
PHST- 2002/05/07 10:00 [pubmed]
PHST- 2002/06/11 10:01 [medline]
PHST- 2002/05/07 10:00 [entrez]
PHST- 2002/06/01 00:00 [pmc-release]
AID - 2401 [pii]
AID - 10.1128/jvi.76.11.5627-5636.2002 [doi]
PST - ppublish
SO  - J Virol. 2002 Jun;76(11):5627-36. doi: 10.1128/jvi.76.11.5627-5636.2002.