Bio Photonics Research

Tiny insects trapped in amber could tell us a great deal about their roles in past ecosystems: pollinators, parasites, predators, and prey. But how many of the insects preserved alongside each other reflect interactions during life, and how many are just unlucky coincidences? Scientists in Spain scrutinized six key samples which preserve now-extinct insects unusually well, to try to learn more about the ants that lived at the same time as the dinosaurs. "Amber inclusions are representative of possible interactions between different organisms shaping the environment," explained Dr. Jose de la Fuente of the Institute for Game and Wildlife Research, Spain, lead author of the article in  Frontiers in Ecology and Evolution . "The identification and morphological characterization of fossil ants in amber with other inclusions of insects provides a snapshot of life on Earth millions of years ago." Snapshots of the past The scientists looked at six different pieces of amber ...

Researchers from the University of Sydney and the Centenary Institute have discovered how a promising class of experimental antibiotics disrupts the bacterium that causes tuberculosis (TB), paving the way for urgently needed new treatments. Globally, TB remains a major health crisis, claiming around 1.2 million lives each year and ranking among the world's deadliest infectious diseases. The rise of drug-resistant strains, including in the Asia-Pacific region, has made the search for new treatment strategies increasingly urgent. Investigating three experimental compounds In a study published in  Nature Communications , the team investigated how three naturally occurring antibiotic compounds—ecumicin, ilamycin and cyclomarin—act on a vital protein degradation machine inside Mycobacterium tuberculosis, the bacterium that causes TB. The molecular machine, known as the ClpC1–ClpP1P2 complex, allows the bacterium to break down damaged or unneeded proteins, helping it to survive stress an...

Researchers have discovered and characterized at the atomic level a mechanism that enables bacterial pathogens—including hospital bacteria Acinetobacter baumannii and Pseudomonas aeruginosa—to assemble antibiotic-resistant three-dimensional (3D) biofilms. These findings open a new avenue for developing therapies against multidrug-resistant bacterial infections by targeting the biofilm assembly. The work is  published  in the journal  Nature Communications . Many pathogenic bacteria form 3D biofilms to protect themselves from the immune system, antibiotic treatments, and drying on environmental surfaces. Some of the most problematic hospital bacteria, such as multidrug-resistant A. baumannii and P. aeruginosa, use specialized hair-like filaments called adhesive pili to attach to tissues or abiotic surfaces. After attaching, the bacteria then grow into thick 3D biofilms consisting of multiple layers of bacteria. This process is also mediated by adhesive pili, but until now ...

  Depending on others for something you need may feel like a risky proposition—and perhaps a human one. It is actually a survival strategy found in the microbial world, and far more frequently than one might expect. Discovering why is key to understanding how microbes form stable communities across medical, industrial, and ecological settings. A new study by bioengineering professor Sergei Maslov (CAIM co-leader), computational scientist Ashish George, and biology professor Tong Wang explores why interdependence can be such a winning move for microbial communities. Their work,  published   in   Cell Systems , demonstrated that a mathematical model of how bacteria produce and share resources accurately predicted the outcome of experiments with living E. coli strains. The researchers' collaboration began during their time as colleagues at the Carl R. Woese Institute for Genomic Biology at the University of Illinois Urbana-Champaign. George continued the collaboration i...

  Sometimes, transporting electrons from one cell to another is a team effort. In electroactive bacteria, that team is a group of proteins that shepherds electrons forward, passing them along like a relay baton, so they can penetrate the thick cell envelope comprising multiple layers of membranes that otherwise are not electroconductive. But how these proteins collaborate to achieve this has not been clear. Cornell researchers have discovered this electron transfer is mediated by CymA proteins' ability to synchronize and form a biomolecular condensate in the inner membrane—something that had not been previously observed in electroactive bacteria. The researchers then demonstrated for the first time that by applying an  electrochemical signal  to the bacteria, they could manipulate the spatial pattern of the proteins and spur the extracellular process. The technique could eventually find applications in biotechnologies such as microbial energy conversion, in which electr...

  Herpes simplex virus type 1 (HSV-1) infection dramatically remodels the host cell's nuclear structures. Infection leads to the formation of viral replication compartments and to chromatin marginalization to the nuclear periphery. Joint research by the Universities of Jyväskylä (Finland) and Bar-Ilan (Israel) reveals that viral infection also alters the structure of nuclear speckles, which are essential for messenger RNA processing. The study was  published   in the   Proceedings of the National Academy of Sciences . "Nuclear speckles are dynamic,  membraneless nuclear bodies  that primarily function as sites for the storage, assembly, and modification of factors involved in gene expression. Both cellular and viral messenger RNAs are processed in nuclear speckles. The disassembly of nuclear speckles severely limits the export of viral messenger RNAs from the nucleus, " explains Research Director Maija Vihinen-Ranta from the University of Jyväskylä. The re...

  Ribosomes, the cell's protein-making factories, consume large amounts of energy as they build the proteins that keep cells alive and functioning. When cells experience stress—such as lack of nutrients or sudden drops in temperature—they quickly switch into survival mode. New research from the Schuman Lab at the Max Planck Institute for Brain Research in Frankfurt now reveals an unexpected way cells manage this transition: by pairing up inactive ribosomes using a ribosomal RNA link. This RNA-based mechanism reveals a previously unknown role for ribosomal RNA in the cellular stress response.   The new study   is published in   Science . Ribosomes are large molecular machines made of protein and RNA that build all proteins in the cell. Because protein production is extremely energy-intensive, cells rapidly reduce protein synthesis when stressed. It has long been known that bacterial cells pair their inactive ribosomes into so-called " hibernating disomes "; however, s...