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Vol. 16, No. 19, pp. 2465-2478, October 1, 2002
1 Howard Hughes Medical Institute, Center for Advanced Biotechnology and Medicine, 2 Department of Molecular Biology and Biochemistry, Rutgers University, and 3 Cancer Institute of New Jersey, Piscataway, New Jersey 08854, USA
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Introduction |
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Cellular BCL-2-related proteins (cBCL-2s) function as regulators of
programmed cell death (apoptosis), in part by
modulating the release of proapoptotic signaling molecules from
mitochondria. These factors act to promote activation of cysteine
proteases of the caspase family and thereby propagate signaling of
apoptotic cell death. DNA viruses are known to encode homologs of
cellular antiapoptotic BCL-2 proteins (vBCL-2s), and the role of
vBCL-2s in various aspects of viral infection and the mechanism by
which they function have been gradually emerging. It is now apparent that inhibition of apoptosis by vBCL-2s in infected cells can prevent
premature death of the host
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