| Literature DB >> 12676996 |
Craig R Brunetti1, Mini Paulose-Murphy, Rajkumari Singh, Jing Qin, John W Barrett, Aubry Tardivel, Pascal Schneider, Karim Essani, Grant McFadden.
Abstract
A class of secreted poxvirus tumor necrosis factor (TNF)-binding proteins has been isolated from Tanapox-infected cell supernatants. The inhibitor bound to a TNF-affinity column and was identified as the product of the 2L gene. Sequence analysis of 2L family members from other yatapoxviruses and swinepox virus yielded no sequence homology to any known cellular gene. The expressed Tanapox virus 2L protein bound to human TNF with high affinity (K(d) = 43 pM) and exhibits an unusually slow off-rate. However, 2L is unable to bind to a wide range of human TNF family members. The 2L protein can inhibit human TNF from binding to TNF receptors I and II as well as block TNF-induced cytolysis. Thus, Tanapox virus 2L represents an inhibitor of human TNF and offers a unique strategy with which to modulate TNF activity.Entities:
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Year: 2003 PMID： 12676996 PMCID： PMC153641 DOI： 10.1073/pnas.0737244100
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205