HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Deszcz, L. Articles by Seipelt, J. Search for Related Content PubMed PubMed Citation Articles by Deszcz, L. Articles by Seipelt, J. Agricola Articles by Deszcz, L. Articles by Seipelt, J.

Apoptotic events induced by human rhinovirus infection

Ernst Kuechler

Max F. Perutz Laboratories, University Departments at the Vienna Biocenter, Department of Medical Biochemistry, Medical University of Vienna, Dr Bohr Gasse 9/3, A-1030 Vienna, Austria

Correspondence
Joachim Seipelt
joachim.seipelt{at}meduniwien.ac.at

HeLa and 16HBE14o^– bronchial epithelium cells infected with human rhinovirus serotype 14 (HRV14) were found to exhibit typical apoptotic morphological alterations, such as cell contraction and nuclear condensation. These events coincided with high-molecular-weight DNA fragmentation, activation of caspase-9 and caspase-3 and poly(ADP–ribose) polymerase cleavage. Caspase activation was preceded by cytochrome c translocation from the mitochondria to the cytoplasm, indicating that apoptosis caused by HRV14 infection was triggered predominantly via the mitochondrial pathway. Apoptosis did not affect HRV14 replication per se, but it facilitated the release of newly formed virus from cells. As apoptosis was fully induced at the time of maximal accumulation of progeny HRV14, it is postulated that apoptosis contributed to the destabilization of the cell and facilitated viral progeny release.

Deceased 5 March 2005; this paper is dedicated to his memory.

This article has been cited by other articles:

				J. Drahos and V. R. Racaniello Cleavage of IPS-1 in Cells Infected with Human Rhinovirus J. Virol., November 15, 2009; 83(22): 11581 - 11587. [Abstract] [Full Text] [PDF]

				L. I. Romanova, P. V. Lidsky, M. S. Kolesnikova, K. V. Fominykh, A. P. Gmyl, E. V. Sheval, S. V. Hato, F. J. M. van Kuppeveld, and V. I. Agol Antiapoptotic Activity of the Cardiovirus Leader Protein, a Viral "Security" Protein J. Virol., July 15, 2009; 83(14): 7273 - 7284. [Abstract] [Full Text] [PDF]

				U. Sajjan, Q. Wang, Y. Zhao, D. C. Gruenert, and M. B. Hershenson Rhinovirus Disrupts the Barrier Function of Polarized Airway Epithelial Cells Am. J. Respir. Crit. Care Med., December 15, 2008; 178(12): 1271 - 1281. [Abstract] [Full Text] [PDF]

				D. Proud, R. B. Turner, B. Winther, S. Wiehler, J. P. Tiesman, T. D. Reichling, K. D. Juhlin, A. W. Fulmer, B. Y. Ho, A. A. Walanski, et al. Gene Expression Profiles during In Vivo Human Rhinovirus Infection: Insights into the Host Response Am. J. Respir. Crit. Care Med., November 1, 2008; 178(9): 962 - 968. [Abstract] [Full Text] [PDF]

				C.-H. Tsao, H.-L. Su, Y.-L. Lin, H.-P. Yu, S.-M. Kuo, C.-I Shen, C.-W. Chen, and C.-L. Liao Japanese encephalitis virus infection activates caspase-8 and -9 in a FADD-independent and mitochondrion-dependent manner J. Gen. Virol., August 1, 2008; 89(8): 1930 - 1941. [Abstract] [Full Text] [PDF]

				L. Deszcz, R. Cencic, C. Sousa, E. Kuechler, and T. Skern An Antiviral Peptide Inhibitor That Is Active against Picornavirus 2A Proteinases but Not Cellular Caspases J. Virol., October 1, 2006; 80(19): 9619 - 9627. [Abstract] [Full Text] [PDF]