![]() Moreover, other DGK isozymes, DGKη and ζ, as well as glucose uptake-related proteins, such as protein kinase C (PKC) α, PKCζ, Akt and glycogen synthase kinase 3β, failed to be stabilized by myristic acid. A cycloheximide chase assay demonstrated that myristic acid, but not palmitic acid, markedly stabilized DGKδ protein. In the present study, we characterized the myristic acid-dependent increase of DGKδ protein. However, it has been unclear how myristic acid regulates the level of DGKδ2 protein. ![]() ![]() We recently found that free myristic acid (14:0), but not free palmitic acid (16:0), increased the DGKδ protein levels and enhanced glucose uptake in C2C12 myotube cells. aureus infection in mice and raises the idea that the MBL gene may act as a disease susceptibility gene against staphylococci infections in humans.ĭecreased levels of the δ isozyme of diacylglycerol kinase (DGK) in skeletal muscle attenuate glucose uptake and, consequently, are critical for the pathogenesis of type 2 diabetes. Our study provides direct evidence that MBL plays a key role in restricting the complications associated with S. Furthermore, we demonstrated that neutrophils and MBL are required to limit intraperitoneal infection with S. aureus compared with 45% mortality in wild-type mice. We found that 100% of MBL-null mice died 48 h after exposure to an intravenous inoculation of S. We tested this contention directly in vivo by generating mice that were devoid of all MBL activity. Circumstantial evidence in vitro and in vivo suggests that MBL plays a key role in first line host defense. The mannose-binding lectin (MBL, also known as mannose-binding protein) is an oligomeric serum molecule that recognizes carbohydrates decorating a broad range of infectious agents including S. Humoral response molecules together with phagocytes play a role in host responses to S. Gram-positive organisms like Staphylococcus aureus are a major cause of morbidity and mortality worldwide. Our method provides an effi- cient and semiquantitative map of epitopes that are targeted in a polyclonal antibody response and should be of widespread utility in vaccine and infec- tion studies. We uncovered previously un- identified epitopes, including an epitope proximal to one recognized by human broadly neutralizing antibodies as well as potentially distracting non- neutralizing epitopes. We detected known epitopes within the polyclonal sera and revealed how antibody responses evolved during the prime- boosting strategy to ultimately result in a neutralizing antibody response. Here, we describe a method of characterizing polyclonal responses by using electron microscopy, and we applied this method to the immunization of rabbits with an HIV-1 envelope glycoprotein vaccine candidate, BG505 SOSIP.664. Mapping epitopes in an immune response is typically incomplete, which creates a barrier to fully understanding the humoral response to antigens and hinders rational vaccine design ef- forts. Characterizing polyclonal antibody responses via currently available methods is inherently complex and difficult.
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