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Article

Complex N-linked glycans on Asn-89 of Kaposi sarcoma herpes virus-encoded interleukin-6 mediate optimal function by affecting cytokine protein conformation.

The Journal of biological chemistry - 23 Oct 2009

Dela Cruz Charles S, Viswanathan Srinivas R, El-Guindy Ayman S, Shedd Duane, Miller George

Abstract excerpt

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...

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Share to Antibodies, Viral
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 19690161
DOI: 10.1074/jbc.M109.039115
PMCID: PMC2785557

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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