BPoD

Jul 29

29 July 2014
It’s a Wrap
Our nerve endings (axons) rely on a protective outer layer called myelin to insulate their lively signals, a bit like the plastic coating on electrical wires. The little round blobs pictured are microscopic myelin makers, known as oligodendrocytes, migrating towards tiny conical mounds of silicon, each 1000-times smaller than a sand castle. Each mound, or ‘micropillar’, acts like an exposed axon, prompting the oligodendrocytes to transform into stringy myelin-forming cells (top left), which coil protectively around the silicon cones. This is actually a chemical test site – drugs can be flooded in around the micropillars to discover those which encourage myelin growth, their effects measured from above by counting the rings of myelin wrapped around the cones. Finding chemicals which boost myelin growth could help to reverse degenerative nervous diseases like multiple sclerosis, were myelin is worn away leaving nerves fragile and exposed.
Written by John Ankers
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Adapted from image by Jonah Chan and colleaguesUniversity of California, USACopyright held by Nature Publishing GroupResearch published by Nature Medicine, July 2014
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29 July 2014

It’s a Wrap

Our nerve endings (axons) rely on a protective outer layer called myelin to insulate their lively signals, a bit like the plastic coating on electrical wires. The little round blobs pictured are microscopic myelin makers, known as oligodendrocytes, migrating towards tiny conical mounds of silicon, each 1000-times smaller than a sand castle. Each mound, or ‘micropillar’, acts like an exposed axon, prompting the oligodendrocytes to transform into stringy myelin-forming cells (top left), which coil protectively around the silicon cones. This is actually a chemical test site – drugs can be flooded in around the micropillars to discover those which encourage myelin growth, their effects measured from above by counting the rings of myelin wrapped around the cones. Finding chemicals which boost myelin growth could help to reverse degenerative nervous diseases like multiple sclerosis, were myelin is worn away leaving nerves fragile and exposed.

Written by John Ankers

Adapted from image by Jonah Chan and colleagues
University of California, USA
Copyright held by Nature Publishing Group
Research published by Nature Medicine, July 2014

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Jul 28

28 July 2014
Blocking Malaria
Plasmodium falciparum – one of the five Plasmodium parasites that cause malaria – spend the majority of their lives in human red blood cells (where they are seen pictured here in green/purple). During this time, they produce over 450 proteins, allowing them to rebuild the surface of the host cell and avoid being discovered by our immune cells. These proteins also help the parasites take in nutrients and increase their virulence. But transporting these building blocks within the host cell relies on an enzyme called plasmepsin V (PMV) and now researchers have developed a compound called WEHI-916, which prevents PMV from working properly. As soon as PMV is no longer active, the malaria parasites die. As PMV is such an important enzyme, targeting it with antimalarial drugs could prevent infections from the outset, by stopping the development and release of Plasmodium ’s crucial proteins.
Written by Katie Panteli
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Image by Eric Hanssen and Megan Dearnley courtesy of Cell Picture ShowUniversity of Melbourne, AustraliaCopyright Elsevier 2014Research published in PLOS Biology, July 2014
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28 July 2014

Blocking Malaria

Plasmodium falciparum – one of the five Plasmodium parasites that cause malaria – spend the majority of their lives in human red blood cells (where they are seen pictured here in green/purple). During this time, they produce over 450 proteins, allowing them to rebuild the surface of the host cell and avoid being discovered by our immune cells. These proteins also help the parasites take in nutrients and increase their virulence. But transporting these building blocks within the host cell relies on an enzyme called plasmepsin V (PMV) and now researchers have developed a compound called WEHI-916, which prevents PMV from working properly. As soon as PMV is no longer active, the malaria parasites die. As PMV is such an important enzyme, targeting it with antimalarial drugs could prevent infections from the outset, by stopping the development and release of Plasmodium ’s crucial proteins.

Written by Katie Panteli

Image by Eric Hanssen and Megan Dearnley courtesy of Cell Picture Show
University of Melbourne, Australia
Copyright Elsevier 2014
Research published in PLOS Biology, July 2014

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Jul 27

27 July 2014
Kettling Proteins
Prions are infectious proteins that can cause deadly diseases like bovine spongiform encephalopathy, or mad cow disease. They also infect yeast cells and this simple fungus has been found to produce a protein, Btn2, that targets prions and kettles them into a small area inside the cell, rather like the way riot police control an unruly crowd. When the cell divides, one of the two offspring is free from prions and can thrive. Intriguingly, Btn2 has similarities to human hook proteins, which play an important role in positioning components inside human cells so they can divide correctly. Pictured are three yeast colonies, the top right producing Btn2 and with mainly healthy cells (stained red) and some infected by prions (white). The lower colony is producing Cur1, a protein allied to Btn2 and has some healthy cells, while the top left colony is producing neither protein and is heavily infected.
Written by Mick Warwicker
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Image by Reed Wickner and colleaguesNational Institutes of Health, USAOriginally published under a Creative Commons Licence (BY 4.0)Research published in PNAS, June 2014
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27 July 2014

Kettling Proteins

Prions are infectious proteins that can cause deadly diseases like bovine spongiform encephalopathy, or mad cow disease. They also infect yeast cells and this simple fungus has been found to produce a protein, Btn2, that targets prions and kettles them into a small area inside the cell, rather like the way riot police control an unruly crowd. When the cell divides, one of the two offspring is free from prions and can thrive. Intriguingly, Btn2 has similarities to human hook proteins, which play an important role in positioning components inside human cells so they can divide correctly. Pictured are three yeast colonies, the top right producing Btn2 and with mainly healthy cells (stained red) and some infected by prions (white). The lower colony is producing Cur1, a protein allied to Btn2 and has some healthy cells, while the top left colony is producing neither protein and is heavily infected.

Written by Mick Warwicker

Image by Reed Wickner and colleagues
National Institutes of Health, USA
Originally published under a Creative Commons Licence (BY 4.0)
Research published in PNAS, June 2014

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Jul 26

26 July 2014
Lighting Up AID
The protein AID (here stained green) is crucial for fighting off unwanted germs. Without it, our immune system wouldn’t be able to make specific antibodies against individual invaders. Until recently, science was reaching in the dark to grasp how exactly AID comes to aid in the fight against disease: no one had been able to image the protein inside cells. Now, researchers have successfully lit up AID using a technique called immunofluorescence, creating a picture of AID molecules placed both in and outside the cells’ nuclei (red). This special microscopy method is by no means new, but getting it to work here was a real challenge. Interestingly, when the protein is active in the wrong places, it can contribute to a range of diseases including cancer. So being able to image AID has potential far beyond furthering our understanding of the immune system.
Written by Emma Bornebroek
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Image courtesy of David Rueda, Sheila Quingchun Xie and colleaguesMRC Clinical Sciences Centre Copyright held by original authorsResearch by Single Molecule Imaging Group, MRC Clinical Sciences Centre
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26 July 2014

Lighting Up AID

The protein AID (here stained green) is crucial for fighting off unwanted germs. Without it, our immune system wouldn’t be able to make specific antibodies against individual invaders. Until recently, science was reaching in the dark to grasp how exactly AID comes to aid in the fight against disease: no one had been able to image the protein inside cells. Now, researchers have successfully lit up AID using a technique called immunofluorescence, creating a picture of AID molecules placed both in and outside the cells’ nuclei (red). This special microscopy method is by no means new, but getting it to work here was a real challenge. Interestingly, when the protein is active in the wrong places, it can contribute to a range of diseases including cancer. So being able to image AID has potential far beyond furthering our understanding of the immune system.

Written by Emma Bornebroek

Image courtesy of David Rueda, Sheila Quingchun Xie and colleagues
MRC Clinical Sciences Centre
Copyright held by original authors
Research by Single Molecule Imaging Group, MRC Clinical Sciences Centre

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Jul 25

25 July 2014
The X File
This deceptively simple image revolutionised molecular biology. It also represents one of the most notorious controversies in science. ‘Photo 51’ was taken by Rosalind Franklin, who was born on this day in 1920. It is an x-ray crystallography image of DNA, created by bombarding a tiny DNA sample with x-rays for more than 60 hours. To most of us, this striped cross might not mean much, but to a few scientists in 1953 it held the secret to the structure of DNA. The controversy surrounds the instant Maurice Wilkins, who worked in Franklin’s lab, showed the photo to Francis Crick, a molecular biologist at Cambridge University, without Franklin’s knowledge. Crick published a paper with his colleague James Watson describing DNA’s double-helix structure. Wilkins, Crick and Watson shared the Nobel Prize in 1962. Franklin, whose peers never accepted her, died of cancer four years earlier, and couldn’t receive the prize posthumously.
Written by Nick Kennedy
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Image by Rosalind Franklin and Raymond GoslinCopyright held by Oregon State University Libraries
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25 July 2014

The X File

This deceptively simple image revolutionised molecular biology. It also represents one of the most notorious controversies in science. ‘Photo 51’ was taken by Rosalind Franklin, who was born on this day in 1920. It is an x-ray crystallography image of DNA, created by bombarding a tiny DNA sample with x-rays for more than 60 hours. To most of us, this striped cross might not mean much, but to a few scientists in 1953 it held the secret to the structure of DNA. The controversy surrounds the instant Maurice Wilkins, who worked in Franklin’s lab, showed the photo to Francis Crick, a molecular biologist at Cambridge University, without Franklin’s knowledge. Crick published a paper with his colleague James Watson describing DNA’s double-helix structure. Wilkins, Crick and Watson shared the Nobel Prize in 1962. Franklin, whose peers never accepted her, died of cancer four years earlier, and couldn’t receive the prize posthumously.

Written by Nick Kennedy

Image by Rosalind Franklin and Raymond Goslin
Copyright held by Oregon State University Libraries

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Jul 24

24 July 2014
Library of Fungus
The fungus Candida glabrata is an increasingly common cause of an infection called candidiasis, which is usually superficial and unpleasant – oral thrush, for instance – but can be life threatening in people with compromised immune systems. This particular fungal invader is highly resistant to drugs, but it doesn’t secrete the enzymes usually associated with resilience. To figure out why it’s such a formidable foe, researchers built a library of over 600 mutant C. glabrata strains, each lacking a specific gene. Pictured are the individual cells and the colonies they form. Top left is the wild-type strain and the others are deletion strains. By studying the various strains as they were exposed to stresses, including anti-fungal drugs, the scientists identified genes involved in C. glabrata’s fitness and resilience. Their deletion library could potentially help to reveal weak points that might be exploited with new anti-fungal drugs.
Written by Daniel Cossins
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Image by Karl Kuchler and colleaguesMedical University ViennaOriginally published under a Creative Commons Licence (BY 4.0)Research published in PLOS Pathogens, June 2014
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24 July 2014

Library of Fungus

The fungus Candida glabrata is an increasingly common cause of an infection called candidiasis, which is usually superficial and unpleasant – oral thrush, for instance – but can be life threatening in people with compromised immune systems. This particular fungal invader is highly resistant to drugs, but it doesn’t secrete the enzymes usually associated with resilience. To figure out why it’s such a formidable foe, researchers built a library of over 600 mutant C. glabrata strains, each lacking a specific gene. Pictured are the individual cells and the colonies they form. Top left is the wild-type strain and the others are deletion strains. By studying the various strains as they were exposed to stresses, including anti-fungal drugs, the scientists identified genes involved in C. glabrata’s fitness and resilience. Their deletion library could potentially help to reveal weak points that might be exploited with new anti-fungal drugs.

Written by Daniel Cossins

Image by Karl Kuchler and colleagues
Medical University Vienna
Originally published under a Creative Commons Licence (BY 4.0)
Research published in PLOS Pathogens, June 2014

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Jul 23

23 July 2014
Long-Life Livers
Organ transplantation can save the life of a patient with end-stage organ failure, but for the best chance of success the donor organ must be collected and transplanted all within 12 hours. After this point, the tissue begins to deteriorate and the organ is discarded. Researchers have now found a way to preserve rat livers by slowly cooling the organ to a sub-zero temperature. The livers are first submerged in an antifreeze solution (pictured) - preventing the formation of ice-crystals - and can be stored in this way for up to four days. This technique could potentially be scaled up for a variety of human organs simply by tweaking the rate of cooling. In the UK there is a pressing shortage of available donor organs, and over 7,000 people on the organ transplant list. Preserving organs in this way would enable thousands more transplants to take place every year.
Written by Helen Thomas
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Image by Wally Reeves, Korkut Uygun and Martin YarmushHarvard UniversityCopyright held by Nature Publishing GroupArticle published in Nature, June 2014
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23 July 2014

Long-Life Livers

Organ transplantation can save the life of a patient with end-stage organ failure, but for the best chance of success the donor organ must be collected and transplanted all within 12 hours. After this point, the tissue begins to deteriorate and the organ is discarded. Researchers have now found a way to preserve rat livers by slowly cooling the organ to a sub-zero temperature. The livers are first submerged in an antifreeze solution (pictured) - preventing the formation of ice-crystals - and can be stored in this way for up to four days. This technique could potentially be scaled up for a variety of human organs simply by tweaking the rate of cooling. In the UK there is a pressing shortage of available donor organs, and over 7,000 people on the organ transplant list. Preserving organs in this way would enable thousands more transplants to take place every year.

Written by Helen Thomas

Image by Wally Reeves, Korkut Uygun and Martin Yarmush
Harvard University
Copyright held by Nature Publishing Group
Article published in Nature, June 2014

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Jul 22

22 July 2014
Retinal Restoration
There’s currently no cure for retinitis pigmentosa (RP), a group of inherited eye diseases that impair the retina’s ability to respond to light, resulting in gradual loss of vision. But now, researchers have used stem cells to develop a promising experimental treatment. First they reprogrammed skin cells from RP patients into stem cells to make patient-specific retinal cells for closer inspection. They found that mutations in a gene called MFRP disrupt the production of actin (red), a protein that provides scaffolding for retinal cells. When this structure doesn’t form properly (left), retinal cells don’t work very well. But when the team used a virus to smuggle in a working copy of MFRP, the structure was restored (right). And in mice with an RP-like condition, the treatment slowly improved vision. It’s early days yet but these results show how patient-specific stem cells can kick start the development of tailor-made therapies.
Written by Daniel Cossins
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Image by Stephen Tsang and colleaguesColumbia University Medical Center, USAOriginally published under a Creative Commons Licence (BY 4.0)Research published in Molecular Therapy, July 2014
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22 July 2014

Retinal Restoration

There’s currently no cure for retinitis pigmentosa (RP), a group of inherited eye diseases that impair the retina’s ability to respond to light, resulting in gradual loss of vision. But now, researchers have used stem cells to develop a promising experimental treatment. First they reprogrammed skin cells from RP patients into stem cells to make patient-specific retinal cells for closer inspection. They found that mutations in a gene called MFRP disrupt the production of actin (red), a protein that provides scaffolding for retinal cells. When this structure doesn’t form properly (left), retinal cells don’t work very well. But when the team used a virus to smuggle in a working copy of MFRP, the structure was restored (right). And in mice with an RP-like condition, the treatment slowly improved vision. It’s early days yet but these results show how patient-specific stem cells can kick start the development of tailor-made therapies.

Written by Daniel Cossins

Image by Stephen Tsang and colleagues
Columbia University Medical Center, USA
Originally published under a Creative Commons Licence (BY 4.0)
Research published in Molecular Therapy, July 2014

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Jul 21

21 July 2014
Ripped Genes
X marks the spot of the location of our body’s genetic material, as that’s the normal shape of chromosomes. Formed from two identical strands (arms) of DNA joined at a single point, the set of chromosomes holds our genetic blueprint in each of our cells. But when a cell divides, their cross-like form changes radically (stained dark purple). Long tentacular protein spindles (green lines) creep out from opposite sides of the cell and latch onto one arm of the chromosome – the two spindle groups seen at the centre of the image are one cell’s worth. After reaching their targets, the spindles then retract, tearing the chromosomes apart thus dividing the genetic material in two. Understanding this complex process could help fight maladies linked to cell division such as cancer and birth defects. And help is much needed because developing medical treatments is never as easy as following a treasure map.
Written by Jan Piotrowski
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Image by Nasser RusanLife: Magnified Exhibition from National Institutes of Health, USACopyright held by National Institutes of HealthResearch published in Nature, June 2014
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21 July 2014

Ripped Genes

X marks the spot of the location of our body’s genetic material, as that’s the normal shape of chromosomes. Formed from two identical strands (arms) of DNA joined at a single point, the set of chromosomes holds our genetic blueprint in each of our cells. But when a cell divides, their cross-like form changes radically (stained dark purple). Long tentacular protein spindles (green lines) creep out from opposite sides of the cell and latch onto one arm of the chromosome – the two spindle groups seen at the centre of the image are one cell’s worth. After reaching their targets, the spindles then retract, tearing the chromosomes apart thus dividing the genetic material in two. Understanding this complex process could help fight maladies linked to cell division such as cancer and birth defects. And help is much needed because developing medical treatments is never as easy as following a treasure map.

Written by Jan Piotrowski

Image by Nasser Rusan
Life: Magnified Exhibition from National Institutes of Health, USA
Copyright held by National Institutes of Health
Research published in Nature, June 2014

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Jul 20

20 July 2014
Hard Hearted
As calcium builds up in tissues it gradually causes them to harden or calcify. It’s how our bodies build teeth and bones. When calcification happens in cardiovascular tissue, however, it reduces blood flow and eventually leads to heart failure. To better understand the problem, researchers have taken snapshots of calcified heart valves using a special microscope that can measure the density of a material as well as its surface features. Images like this one, where denser material appears orange, have revealed that spherical particles forming during soft-tissue calcification are composed of a form of calcium known as hydroxyapatite, which is structurally different to that found in bone. Such insights might help figure out how to break down the mineral deposits or even prevent them forming in the first place.
Written by Daniel Cossins
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Image by Sergio Bertazzo from the Wellcome Image Awards 2014Imperial College LondonOriginally published under a Creative Commons Licence (BY 4.0)Research published in Nature, April 2013
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20 July 2014

Hard Hearted

As calcium builds up in tissues it gradually causes them to harden or calcify. It’s how our bodies build teeth and bones. When calcification happens in cardiovascular tissue, however, it reduces blood flow and eventually leads to heart failure. To better understand the problem, researchers have taken snapshots of calcified heart valves using a special microscope that can measure the density of a material as well as its surface features. Images like this one, where denser material appears orange, have revealed that spherical particles forming during soft-tissue calcification are composed of a form of calcium known as hydroxyapatite, which is structurally different to that found in bone. Such insights might help figure out how to break down the mineral deposits or even prevent them forming in the first place.

Written by Daniel Cossins

Image by Sergio Bertazzo from the Wellcome Image Awards 2014
Imperial College London
Originally published under a Creative Commons Licence (BY 4.0)
Research published in Nature, April 2013

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