Identification of a novel septin 4 protein binding to human herpesvirus 8 kaposin A protein using a phage display cDNA library

Cheng Wen Lin, Ping Feng Tu, Nai Wan Hsiao, Ching Yao Chang, Lei Wan, Yu Tsun Lin, Hsueh Wei Chang

Research output: Contribution to journalArticlepeer-review

13 Citations (Scopus)


Human herpesvirus 8 (HHV-8) is associated with the development of Kaposi's sarcoma and several other human malignancies. Kaposin A protein of HHV-8 has been demonstrated as inducing tumorigenic transformation, being responsible for nuclear receptor coactivators in the transforming activity. In this study, a kaposin A-interacting septin 4 variant that contained the unique GDR at the N-terminus and AAALE at the C-terminus was identified using affinity selection of a phage display library. Co-immunoprecipitation and confocal imaging revealed in vitro binding specificity and in vivo co-localization of HHV-8 kaposin A protein to the septin 4 variant. The kaposin A-interacting septin 4 variant induced cell rounding up, activated caspase-3, and up-regulated transcriptional factor NF-κB. By contrast, kaposin A protein showed an antagonistic effect on the biological functions of the septin 4 variant. Therefore, the interaction of kaposin A protein and the septin 4 variant was suggested as playing a possible role in the development of HHV-8-associated malignancies. This study provides insights into the mechanism of the kaposin A protein pathology, in which the interactions of kaposin A protein with cellular proteins might allow alteration of fundamental cellular processes.

Original languageEnglish
Pages (from-to)65-72
Number of pages8
JournalJournal of Virological Methods
Issue number1
Publication statusPublished - 2007 Jul 1

All Science Journal Classification (ASJC) codes

  • Virology

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