Abstract
The Type III Secretion System (T3SS) is a multimeric protein complex composed of over 20 different proteins, utilized by Gram-negative bacteria to infect eukaryotic host cells. The T3SS has been implicated as a virulence factor by which pathogens cause infection and has recently been characterized as a communication tool between bacteria and plant cells in the rhizosphere. The T3SS has been repurposed to be used as a tool for the delivery of non-native or heterologous proteins to eukaryotic cells or the extracellular space for a variety of purposes, including drug discovery and drug delivery. This review covers the methodology of heterologous protein secretion as well as multiple cases of utilizing the T3SS to deliver heterologous proteins or artificial materials. The research covered in this review will serve to outline the scope and limitations of utilizing the T3SS as a tool for protein delivery.
Highlights
The bacterial Type III Secretion System (T3SS) injectisome is a multimeric protein complex composed of more than 20 different proteins to form a needle-like structure to transverse the space between an interacting bacterial cell and eukaryotic cell (Figure 1) [1,2,3]
These results show the potential power of using T3SS-encoding bacteria to deliver antigens as a vaccination method
Issues related to proper folding and efficient delivery of protein via the T3SS will need to be overcome to broaden the application of this method
Summary
The bacterial Type III Secretion System (T3SS) injectisome is a multimeric protein complex composed of more than 20 different proteins to form a needle-like structure to transverse the space between an interacting bacterial cell and eukaryotic cell (Figure 1) [1,2,3]. The tip of the needle, or the translocon, forms a pore in the eukaryotic cell membrane through which effector proteins may travel [3,9]. Strategies for the Secretion of Heterologous Proteins. The differences in secretion tags between effectors are important for translocation efficiency. CyaA increases cAMP levels in eukaryotic cells when secreted via the T3SS, which can be readily quantified. In strains lacking the SseA chaperone, SseB was not secreted and cAMP levels were unchanged in the host cell. These results highlight the importance of chaperones and validates the use of existing effectors for secretion of heterologous proteins
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