Kinome Analysis of Host Response to Mycobacterial Infection: a Novel Technique in Proteomics
AUTOR(ES)
Hestvik, Anne Lise K.
FONTE
American Society for Microbiology
RESUMO
An array of mammalian phospho-specific antibodies was used to screen for a host response upon mycobacterial infection, reflected as changes in host protein phosphorylation. Changes in the phosphorylation state of 31 known signaling molecules were tracked after infection with live or heat killed Mycobacterium bovis BCG or after incubation with the mycobacterial cell wall component lipoarabinomannan (LAM). Mycobacterial infection triggers a signaling cascade leading to activation of stress-activated protein kinase and its subsequent downstream target, c-Jun. Mycobacteria were also shown to inhibit the activation of protein kinase C ɛ and to induce phosphorylation of proteins not yet known to be involved in mycobacterial infection, such as the cytoskeletal protein α-adducin, glycogen synthase kinase 3β, and a receptor subunit involved in regulation of intracellular Ca2+ levels. The mycobacterial cell wall component LAM has been identified as a trigger for some of these modulation events.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=201077Documentos Relacionados
- Large-scale Proteomics Analysis of the Human Kinome
- Production of Matrix Metalloproteinases in Response to Mycobacterial Infection
- Immune response to persistent mycobacterial infection in mice.
- Genomic analysis of the host response to hepatitis C virus infection
- Genomic analysis of the host response to hepatitis B virus infection