Recognition of host proteins by Helicobacter cysteine-rich protein C
Bernd Roschitzki1, Stefan Schauer, Peer R E Mittl
1Functional Genomics Center Zurich, UZH / ETH Zürich, Winterthurerstr. 190, 8057 Zürich, Switzerland. bernd.roschitzki@fgcz.uzh.ch
Abstract:
Tetratricopeptide- and sel1-like repeat (SLR) proteins modulate various cellular activities, ranging from transcription regulation to cell-fate control. Helicobacter cysteine-rich proteins (Hcp) consist of several SLRs that are cross-linked by disulfide bridges and have been implicated in host/pathogen interactions. Using pull-down proteomics, several human proteins including Nek9, Hsp90, and Hsc71 have been identified as putative human interaction partners for HcpC. The interaction between the NimA-like protein kinase Nek9 and HcpC has been validated by ELISA and surface plasmon resonance. Recombinant Nek9 is recognized by HcpC with a dissociation constant in the lower micromolar range. This interaction is formed either directly between Nek9 and HcpC or via the formation of a complex with Hsc71. The HcpC homologue HcpA possesses no affinity for Nek9, suggesting that the reported interaction is rather specific for HcpC. These results are consistent with previous observations where Nek9 was targeted upon bacterial or viral invasion. However, further experiments will be required to show that the reported interactions also occur in vivo.
Related Concept Videos
Antigens Involved in Adaptive Immunity
Complete Antigens
Complete antigens possess both immunogenicity and reactivity.
Export of Misfolded Proteins out of the ER
Gastritis II: Pathophysiology
Antigen Processing Pathways
MHC Class I: Presenting Endogenous...
The Antiviral System of Bacteria and Archaea: CRISPR
Cytoskeletal Proteins in Bacteria


