ArticleThe Journal of biological chemistry2009
Complex N-linked glycans on Asn-89 of Kaposi sarcoma herpes virus-encoded interleukin-6 mediate optimal function by affecting cytokine protein conformation.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 13 citations in OpenAlex.
- The biology of interleukin-6 family cytokines is regulated by glycosylation.The Biochemical journal · 2025Review
- Review
- The Impact of Glycosylation on the Functional Activity of CD133 and the Accuracy of Its Immunodetection.Biology · 2024Review
- N-Linked Glycosylation and Expression of Duck Plague Virus pUL10 Promoted by pUL49.5.Microbiology spectrum · 2023Article
- Direct MALDI Glycotyping of Glycoproteins toward Practical Subtyping of Biological Samples.ACS omega · 2022Article
- Global aspects of viral glycosylation.Glycobiology · 2018Article
- Article
- Mutation of N-linked glycosylation at Asn548 in CD133 decreases its ability to promote hepatoma cell growth.Oncotarget · 2015Article
- Cytokine homologs of human gammaherpesviruses.Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research · 2012Review
- Viral interleukin-6: role in Kaposi's sarcoma-associated herpesvirus: associated malignancies.Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research · 2011Review
- Human herpesvirus 8-encoded cytokines.Future virology · 2010Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Kaposi sarcoma-associated herpesvirus-encoded interleukin-6 (vIL-6) and its human cellular homologue (huIL-6) share similar biological functions. Our previous work showed that N-linked glycosylation was required for optimal function of vIL6 but not huIL-6 (1). Here we describe heterogeneity in the composition of the glycans of the two N-linked sites of vIL-6. The Asn-89 site of vIL-6, found to be required for optimal cytokine function, is composed of complex glycans. The Asn-78 site is composed of high mannose glycans, which are dispensable for cytokine function. N-Linked glycosylation at the Asn-89 site was required for intracellular production of functional vIL-6, but endoglycosidase-mediated removal of N-linked glycans from secreted vIL-6 did not impair protein function. With the use of a conformation-specific antibody and tryptic digestion assays, we showed that glycosylation at the Asn-89 site of vIL-6 affected protein conformation. Human IL-6, but not vIL-6, requires IL-6Ralpha for binding to gp130. We tested the hypothesis that the Asn-89 complex glycan of vIL-6 alone was sufficient to confer binding to gp130 independently of IL-6Ralpha. Two mutants of huIL-6, made to contain additional complex N-linked glycans in the region that interacts with IL-6Ralpha, did not confer binding to gp130 independently of IL-6Ralpha. Our findings support the conclusion that complex glycans on Asn-89 of vIL-6 specifically promote a protein conformation that allows the viral cytokine to bind gp130 independently of IL-6Ralpha.
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Registered trials
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