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Viral inhibition of inflammation: Cowpox virus encodes an inhibitor of the interleukin-1β converting enzyme
Cowpox virus encodes several cytokine response modifiers that act together to inhibit the release of pro-inflammatory cytokines in response to infection, which may contribute significantly to the pathology associated with poxvirus infections. Expand
Vaccinia and cowpox viruses encode a novel secreted interleukin-1-binding protein
Intracranial inoculation of mice with vB15RKO suggests that this ORF is involved in VV virulence, and the possible role of a virus-encoded IL-1-binding protein in the pathology of a poxvirus infection and its relationship to other poXvirus-encoding immune modulators is discussed. Expand
A third distinct tumor necrosis factor receptor of orthopoxviruses.
Possessing up to three TNFRs, including CrmD, which is secreted as disulfide-linked complexes in varied amounts by CPV and ECT, likely enhances the dynamics of the immune modulating mechanisms of orthopoxviruses. Expand
Cowpox virus genome encodes a second soluble homologue of cellular TNF receptors, distinct from CrmB, that binds TNF but not LT alpha.
The cowpox genome contains a single copy gene, crmC, encoding a soluble, secreted protein whose sequence marks it as a new member of the TNF receptor family, presumed function of CrmC is viral inhibition of host-elicited TNF. Expand
Cowpox virus and other members of the orthopoxvirus genus interfere with the regulation of NF-kappaB activation.
The results suggest that cowpox virus is capable of inhibiting the activation of NF-kappaB at a point where multiple signal transduction pathways converge, and that orthopoxviruses may affect a broad range of virus-host interactions through their effects upon NF- kappaB activation. Expand
Identification of the Orthopoxvirus p4c Gene, Which Encodes a Structural Protein That Directs Intracellular Mature Virus Particles into A-Type Inclusions
A model in which the P4c protein may play a role in the retrograde movement of IMV particles, thereby contributing to the retention ofIMV particles within the cytoplasm and within ATIs when they are present is suggested. Expand
Hemorrhage in lesions caused by cowpox virus is induced by a viral protein that is related to plasma protein inhibitors of serine proteases.
There is extensive similarity between the predicted amino acid sequence of the 38-kDa protein and the amino acid sequences of several plasma proteins that are inhibitors of various serine proteases involved in blood coagulation pathways, which suggests that the viral protein may possess a similar biological activity, which may enable it to effect hemorrhage by inhibiting one or more of the serine proteins involved in the host's normal processes of bloodCoagulation and wound containment. Expand
Inhibition of interleukin-1 beta converting enzyme by the cowpox virus serpin CrmA. An example of cross-class inhibition.
The mechanism and kinetics of this unusual inhibition of a cysteine proteinase by a member of the serpin superfamily previously thought to inhibit serineproteinase only are reported. Expand
Cowpox virus contains two copies of an early gene encoding a soluble secreted form of the type II TNF receptor.
The results show that orthopoxiviruses such as cowpox virus encode secreted forms of TNF receptors that can contribute to the modification of T NF-mediated antiviral processes. Expand
Granzyme B Is Inhibited by the Cowpox Virus Serpin Cytokine Response Modifier A(*)
The ability of cytolytic cells to cause apoptosis in target cells is in part due to the action of the serine proteinase granzyme B. We demonstrate that granzyme B is inhibited, with an associationExpand