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Expression and purification of human papillomavirus 18 L1 virus-like particle from Saccharomyces cerevisiae

Expression and purification of human papillomavirus 18 L1 virus-like particle from Saccharomyces... Cervical cancer caused by human papillomavirus (HPV) might be successfully prevented by HPV vaccination and screening. HPV vaccination and HPV serology assays have been investigated using HPV virus-like particles (VLPs). In this study we produced HPV18 L1 VLPs in Saccharomyces cerevisiae and purified them. The HPV18 L1 gene was cloned into the yeast expression vector YEGα-HIR525, and transformed into Saccharomyces cerevisiae . Expression of HPV18 L1 protein was demonstrated by Western blotting. The HPV18 L1 protein was purified by ultracentrifugation, size-exclusion chromatography and cation-exchange chromatography, and was up to 95% pure. We showed by transmission electron microscopy that the purified protein self-assembled into VLPs. These findings should be useful for establishing vaccine efficacy as well as characterizing vaccine candidates, and may provide an international reference standard for HPV serology assays. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Pharmacal Research Springer Journals

Expression and purification of human papillomavirus 18 L1 virus-like particle from Saccharomyces cerevisiae

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References (26)

Publisher
Springer Journals
Copyright
Copyright © 2008 by The Pharmaceutical Society of Korea
Subject
Pharmacy; Pharmacology/Toxicology ; Pharmacy
ISSN
0253-6269
eISSN
1976-3786
DOI
10.1007/s12272-001-1142-1
Publisher site
See Article on Publisher Site

Abstract

Cervical cancer caused by human papillomavirus (HPV) might be successfully prevented by HPV vaccination and screening. HPV vaccination and HPV serology assays have been investigated using HPV virus-like particles (VLPs). In this study we produced HPV18 L1 VLPs in Saccharomyces cerevisiae and purified them. The HPV18 L1 gene was cloned into the yeast expression vector YEGα-HIR525, and transformed into Saccharomyces cerevisiae . Expression of HPV18 L1 protein was demonstrated by Western blotting. The HPV18 L1 protein was purified by ultracentrifugation, size-exclusion chromatography and cation-exchange chromatography, and was up to 95% pure. We showed by transmission electron microscopy that the purified protein self-assembled into VLPs. These findings should be useful for establishing vaccine efficacy as well as characterizing vaccine candidates, and may provide an international reference standard for HPV serology assays.

Journal

Archives of Pharmacal ResearchSpringer Journals

Published: Feb 1, 2008

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