Journal
ANNUAL REVIEW OF MICROBIOLOGY
Volume 62, Issue -, Pages 171-192Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev.micro.62.081307.163009
Keywords
caspase inhibition; serine protease; CrmA; p35; IAP; vFLIP
Categories
Funding
- National Institute of Allergy and Infections Diseases, National Institutes of Health.
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [Z01AI000940] Funding Source: NIH RePORTER
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To prolong cell viability and facilitate replication, viruses have evolved multiple mechanisms to inhibit the host apoptotic response. Cellular proteases such as caspases and serine proteases are instrumental in promoting apoptosis. Thus, these enzymes are logical targets for virus-mediated modulation to suppress cell death. Four major classes of viral inhibitors antagonize caspase function: serpins, p35 family members, inhibitor of apoptosis proteins, and viral FLICE-inhibitory proteins. Viruses also subvert activity of the serine proteases, granzyme B and HtrA2/Omi, to avoid cell death. The combined efforts of viruses to suppress apoptosis suggest that this response should be avoided at all costs. However, some viruses utilize caspases during replication to aid virus protein maturation, progeny release, or both. Hence, a multifaceted relationship exists between viruses and the apoptotic response they induce. Examination of these interactions contributes to our understanding of both virus pathogenesis and the regulation of apoptotic enzymes in normal cellular functions.
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