Abstract
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 language | English |
|---|---|
| Pages (from-to) | 65-72 |
| Number of pages | 8 |
| Journal | Journal of Virological Methods |
| Volume | 143 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 2007 Jul 1 |
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All Science Journal Classification (ASJC) codes
- Virology
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Identification of a novel septin 4 protein binding to human herpesvirus 8 kaposin A protein using a phage display cDNA library. / Lin, Cheng Wen; Tu, Ping Feng; Hsiao, Nai-Wan; Chang, Ching Yao; Wan, Lei; Lin, Yu Tsun; Chang, Hsueh Wei.
In: Journal of Virological Methods, Vol. 143, No. 1, 01.07.2007, p. 65-72.Research output: Contribution to journal › Article
TY - JOUR
T1 - Identification of a novel septin 4 protein binding to human herpesvirus 8 kaposin A protein using a phage display cDNA library
AU - Lin, Cheng Wen
AU - Tu, Ping Feng
AU - Hsiao, Nai-Wan
AU - Chang, Ching Yao
AU - Wan, Lei
AU - Lin, Yu Tsun
AU - Chang, Hsueh Wei
PY - 2007/7/1
Y1 - 2007/7/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=34249093635&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=34249093635&partnerID=8YFLogxK
U2 - 10.1016/j.jviromet.2007.02.010
DO - 10.1016/j.jviromet.2007.02.010
M3 - Article
C2 - 17383018
AN - SCOPUS:34249093635
VL - 143
SP - 65
EP - 72
JO - Journal of Virological Methods
JF - Journal of Virological Methods
SN - 0166-0934
IS - 1
ER -