The BPS Art of Science Image Contest took place again this year, during the 61st Annual Meeting in New Orleans. The image that won third place was submitted by Ryan Littlefield, assistant professor, Department of Biology, University of South Alabama. Littlefield took some time to provide information about the image and the science it represents.
How did you compose this image?
Usually these C. elegans worms move around quite vigorously. I added muscimol to prevent muscle contraction. I picked three different types of worms that appear red only, green only, and red and green (which appear mostly yellow) and mixed them together on a thin pad of agarose. The worms in the image all happened to clump together, resulting in a nice demonstration of the different color patterns. I collected Z-stacks for each of the fields of view on an Andor spinning disk confocal microscope. Using ImageJ software, I then made projections for the images that included the body wall muscle of the worms and pair-wise stitching of about six different projections.
What do you love about this image?
The juxtaposition of all three types of transgenic worms being next to each other was very striking. The image includes all the different regions of the worms in various orientations, shows many of the different muscle types in these worms, and shows how the muscle cells fit together.
What do you want viewers to see or think about when they view this image?
The striated myofibrils in these worms are beautifully organized along their lengths, and it naturally raises the question of how this organization is achieved. In addition, the different muscle types show the viewer that there is a lot of diversity along the length of these 1mm worms.
How does this image reflect your scientific research?
I am interested in how actin and myosin become organized into functional, contractile bundles. In particular, I am interested in how actin filament lengths are specified in striated muscle. In these worms, I modified an isoform of muscle myosin and tropomodulin with fluorescent proteins (mCherry and GFP, respectively) to determine how thin filaments are organized within these muscles.
What are some real-world applications of your research?
Both the uniformity of and specific lengths of actin filaments are important components of muscle physiology. Misregulation of actin filament lengths may be important factor in diseases including cardio- and skeletal and myopathies. In addition, muscle damage from extended spaceflight, sarcopenia from aging, and acute muscle injuries may be slowed or prevented by interventions that prevent actin filament lengths from changing.
How does your research apply to those who are not working in your specific field?
Striated myofibrils are a dramatic example of a dynamic, self-organizing biological system that is attuned to a specific function (contraction). Similar mechanisms for functional self-organization may also be used for other contractile actomyosin bundles, such as stress fibers and contractile fibers in smooth muscle, and for other dynamic cytoskeletal systems, such as flagella and microtubules in the mitotic spindle.