scholarly journals Replication of cowpox virus in macrophages is dependent on the host range factor p28/N1R

2021 ◽  
Vol 18 (1) ◽  
Author(s):  
Daniel Bourquain ◽  
Livia Schrick ◽  
Bernd Karsten Tischer ◽  
Klaus Osterrieder ◽  
Lars Schaade ◽  
...  
Keyword(s):  
Immune Response ◽  
Host Range ◽  
Human Health ◽  
Ring Finger ◽  
Cowpox Virus ◽  
Ring Finger Domain ◽  
Cellular Machinery ◽  
Truncated Variants

AbstractZoonotic orthopoxvirus infections continue to represent a threat to human health. The disease caused by distinct orthopoxviruses differs in terms of symptoms and severity, which may be explained by the unique repertoire of virus factors that modulate the host’s immune response and cellular machinery. We report here on the construction of recombinant cowpox viruses (CPXV) which either lack the host range factor p28 completely or express truncated variants of p28. We show that p28 is essential for CPXV replication in macrophages of human or mouse origin and that the C-terminal RING finger domain of p28 is necessary to allow CPXV replication in macrophages.

scholarly journals Normal Immune System Development in Mice Lacking the Deltex-1 RING Finger Domain

2005 ◽  
Vol 25 (4) ◽  
pp. 1437-1445 ◽  
Author(s):  
Sébastien Storck ◽  
Frédéric Delbos ◽  
Nicolas Stadler ◽  
Catherine Thirion-Delalande ◽  
Florence Bernex ◽  
...  
Keyword(s):  
B Cell ◽  
Notch Signaling ◽  
Ubiquitin Ligase ◽  
Cell Lineage ◽  
Ring Finger ◽  
Mouse Development ◽  
Ring Finger Domain ◽  
Ubiquitin Ligase Activity ◽  
Immune System Development ◽  
Cell Commitment

ABSTRACT The Notch signaling pathway controls several cell fate decisions during lymphocyte development, from T-cell lineage commitment to the peripheral differentiation of B and T lymphocytes. Deltex-1 is a RING finger ubiquitin ligase which is conserved from Drosophila to humans and has been proposed to be a regulator of Notch signaling. Its pattern of lymphoid expression as well as gain-of-function experiments suggest that Deltex-1 regulates both B-cell lineage and splenic marginal-zone B-cell commitment. Deltex-1 was also found to be highly expressed in germinal-center B cells. To investigate the physiological function of Deltex-1, we generated a mouse strain lacking the Deltex-1 RING finger domain, which is essential for its ubiquitin ligase activity. Deltex-1Δ/Δ mice were viable and fertile. A detailed histological analysis did not reveal any defects in major organs. T- and B-cell development was normal, as were humoral responses against T-dependent and T-independent antigens. These data indicate that the Deltex-1 ubiquitin ligase activity is dispensable for mouse development and immune function. Possible compensatory mechanisms, in particular those from a fourth Deltex gene identified during the course of this study, are also discussed.

Special Issue on "Immunomodulatory and therapeutic approaches against infectious diseases"

2011 ◽  
Vol 1 (5) ◽  
pp. 1-2
Author(s):  
Lavkush Dwivedi
Keyword(s):  
Immune Response ◽  
Infectious Diseases ◽  
Human Health ◽  
Immune Stimulation ◽  
Defense System ◽  
Special Issue ◽  
Therapeutic Approaches ◽  
Major Constraint ◽  
The World ◽  
Insight Into

Infectious diseases and consequent immune imbalancesare major constraint in human health managementthroughout the world. However, in recentdecades enormous efforts have been made to elucidatethe immunomodulatory approaches againstinfectious diseases. Immunomodulation is a therapeuticapproach in which we try to intervene inauto regulating processes of the defense system toadjust the immune response at a desired level.The present special issue on cutting edge issues inImmunomodulation like Immune stimulation, Immunesuppression, Immune potentiating and immunereinforcement summarizes our current understandingof this complex mosaic. The accompanyingselection of recent articles from across theworld provides further insight into this topic. 

The MDM2 RING-finger domain is required to promote p53 nuclear export

2000 ◽  
Vol 2 (9) ◽  
pp. 569-573 ◽  
Author(s):  
Rory K. Geyer ◽  
Zhong K. Yu ◽  
Carl G. Maki
Keyword(s):  
Nuclear Export ◽  
Ring Finger ◽  
Ring Finger Domain

scholarly journals Scaling in the Immune System: PhD Thesis

2019 ◽  
Author(s):  
soumya banerjee
Keyword(s):  
Immune Response ◽  
Immune System ◽  
Body Size ◽  
Human Health ◽  
Response Rates ◽  
System Response ◽  
Metabolic Rates ◽  
Viral Dynamics ◽  
Immune System Response ◽  
Phd Thesis

How different is the immune system in a human from that of a mouse? Do pathogens replicate at the same rate in different species? Answers to these questions have impact on human health since multi-host pathogens that jump from animals to humans affect millions worldwide.It is not known how rates of immune response and viral dynamics vary from species to species and how they depend on species body size. Metabolic scalingtheory predicts that intracellular processes will be slower in larger animals since cellular metabolic rates are slower. We test how rates of pathogenesis and immune system response rates depend on species body size.

scholarly journals MdmX Protects p53 from Mdm2-Mediated Degradation

2000 ◽  
Vol 20 (3) ◽  
pp. 1001-1007 ◽  
Author(s):  
Mark W. Jackson ◽  
Steven J. Berberich
Keyword(s):  
Cell Cycle ◽  
Cell Cycle Arrest ◽  
Nuclear Export ◽  
P53 Protein ◽  
Ring Finger ◽  
Ring Finger Domain ◽  
Cycle Arrest ◽  
Dependent Cell ◽  
Potential Basis ◽  
P53 Tumor Suppressor Protein

ABSTRACT The p53 tumor suppressor protein is stabilized in response to cellular stress, resulting in activation of genes responsible for either cell cycle arrest or apoptosis. The cellular pathway for releasing normal cells from p53-dependent cell cycle arrest involves the Mdm2 protein. Recently, a p53-binding protein with homology to Mdm2 was identified and called MdmX. Like Mdm2, MdmX is able to bind p53 and inhibit p53 transactivation; however, the ability of MdmX to degrade p53 has yet to be examined. We report here that MdmX is capable of associating with p53 yet is unable to facilitate nuclear export or induce p53 degradation. In addition, expression of MdmX can reverse Mdm2-targeted degradation of p53 while maintaining suppression of p53 transactivation. Using a series of MdmX deletions, we have determined that there are two distinct domains of the MdmX protein that can stabilize p53 in the presence of Mdm2. One domain requires MdmX interaction with p53 and results in the retention of both proteins within the nucleus and repression of p53 transactivation. The second domain involves the MdmX ring finger and results in stabilization of p53 and an increase in p53 transactivation. The potential basis for stabilization and increased p53 transactivation by the MdmX ring finger domain is discussed. Based on these observations, we propose that the MdmX protein may function to maintain a nuclear pool of p53 protein in undamaged cells.

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