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How a bacterial virulence factor promotes its own secretion

Date:
September 18, 2016
Source:
University of Oslo, Department of Biosciences
Summary:
Many bacteria depend on their ability to attach, or adhere, to our cells for the ability to cause disease. When their survival means disease for us, we often turn to antibiotics, but his miracle medicine is now under threat of becoming useless because of bacteria's increasing resistance. Therefore scientists have turned to look at other strategies.
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Many bacteria depend on their ability to attach, or adhere, to our cells for the ability to cause disease. When their survival means disease for us we often turn to antibiotics, but his miracle medicine is now under threat of becoming useless because of bacteria's increasing resistance. Therefore scientists have turned to look at other strategies.

"If we can block the bacteria's way of attaching to our cells we can disarm them instead of killing them," says Jack Leo, a post-doc at the Department of Biosciences at the University of Oslo.

He and his team have been studying the protein Intimin, which is an essential adhesin of certain diarrhea-causing bacteria such as enteropathogenic E. coli. Intimin is a so-called autotransporter, which means it mediates its own secretion to the bacterial surface. Once there, Intimin causes the bacteria to attach to the cells of our intestinal lining, which leads to disease symptoms. If you can block the function of Intimin, then you also block the bacterial adhesion.

Until now it has been a mystery how Intimin actually transports itself outside the cell. Intimin is found in Gram-negative bacteria, which, unlike our own cells, have two membranes covering the cell. This means that transporting something across these two barriers requires extra energy. Bernstein and co-workers have argued that protein folding alone cannot provide enough free energy in order to secrete a protein.

"In this study we prove that it is indeed the protein folding that provides energy for the secretion, at least in the case of Intimin and related proteins," concludes Leo.

However, the study has not found which energy source that initiates the transport. The way intimin works is that it is the folding of part of the protein already outside the cell literally pulls the rest of the protein across the outer membrane, but without initiation nothing happens. The figure shows how intimin folds domain by domain, pulling the rest of the protein through. A protein domain is defined as part of a protein chain that can fold independently to produce a stable 3-dimensional structure.

"When we introduced a "tag" at the first domain in Intimin, the protein folding was disrupted," says Leo.

More research is needed to fully understand the process, but it is one small step closer to target the weaknesses in the way bacteria attack us.


Story Source:

Materials provided by University of Oslo, Department of Biosciences. Note: Content may be edited for style and length.


Journal Reference:

  1. Jack C. Leo, Philipp Oberhettinger, Shogo Yoshimoto, D. B. R. K. Gupta Udatha, J. Preben Morth, Monika Schütz, Katsutoshi Hori, Dirk Linke. Secretion of the Intimin Passenger Domain Is Driven by Protein Folding. Journal of Biological Chemistry, 2016; 291 (38): 20096 DOI: 10.1074/jbc.M116.731497

Cite This Page:

University of Oslo, Department of Biosciences. "How a bacterial virulence factor promotes its own secretion." ScienceDaily. ScienceDaily, 18 September 2016. <www.sciencedaily.com/releases/2016/09/160918175959.htm>.
University of Oslo, Department of Biosciences. (2016, September 18). How a bacterial virulence factor promotes its own secretion. ScienceDaily. Retrieved May 23, 2017 from www.sciencedaily.com/releases/2016/09/160918175959.htm
University of Oslo, Department of Biosciences. "How a bacterial virulence factor promotes its own secretion." ScienceDaily. www.sciencedaily.com/releases/2016/09/160918175959.htm (accessed May 23, 2017).

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