Superbugs may have a soft spot, after all
Researchers found that superbugs like E. coli require a balance between two proteins, RbfA and KsgA, to produce proteins. Disrupting this balance could potentially kill the bacteria without harming humans.
Bacterial Proteins
Articles tagged with Bacterial Proteins
Antibacterial protein's molecular workings revealed
Vanderbilt investigators have identified the structural features of calprotectin's two metal binding sites and demonstrated that manganese binding is key to its antibacterial action. The study could guide efforts to develop novel antibacterials that limit a microbe's access to metals.
SourceVanderbilt University Medical Center·JournalProceedings of the National Academy of Sciences·DateFeb 21, 2013
What green algae are up to in the dark
Researchers at Ruhr-University Bochum have discovered a metabolic pathway for hydrogen production in green algae under stress conditions, even in the dark. This discovery provides new insights into the production of hydrogen gas and its potential application in sustainable energy solutions.
Cell: Protein folding via charge zippers
Researchers discovered a novel charge zipper principle used by membrane proteins to form functional units, allowing them to be immersed into hydrophobic cell membranes. The mechanism involves the assembly of amino acids with positive or negative charges, forming an uncharged ring that lines the TatA pore.
How the protein transport machinery in the chloroplasts of higher plants developed
Researchers discovered that the protein transport system in chloroplasts of higher plants evolved from a bacterial system, with Physcomitrella patens serving as an intermediate stage. The moss has both old and new components of the SRP system, guiding proteins to their place of work in the cell membrane.
Strange behavior: New study exposes living cells to synthetic protein
Researchers at Arizona State University have fabricated an artificial protein and examined its effects on living cells, revealing a peculiar set of adaptations including filamentation, ATP depletion, and the formation of endoliposomes. These findings may lead to the development of novel therapeutic agents.
Staphylococcus aureus: Why it just gets up your nose!
Researchers identified the mechanism by which Staphylococcus aureus colonizes nasal passages, finding that Clumping factor B (ClfB) binds to skin protein loricrin with high affinity. This interaction is crucial for successful colonization and opens new avenues for developing therapeutic strategies.
Surviving sepsis with LECT2
A recent study published in The Journal of Experimental Medicine found that patients with sepsis had abnormally low levels of the inflammatory protein LECT2. Injecting LECT2 into septic mice promoted bacterial clearance by immune cells and increased their production of survival-promoting factors.
Achilles' heel of pathogenic bacteria discovered
Scientists at Max Planck Institute discover that EF-P plays a crucial role in protein production of pathogenic bacteria, leading to the development of new specific antibiotics. Intestinal bacteria lacking EF-P are less fit and not as virulent.
Raising the blockade
Researchers have elucidated the function of Translation Elongation Factor P (EF-P) during protein synthesis, revealing its role in regulating protein copy numbers in response to changing conditions. EF-P helps stalled ribosomes overcome a specific proline-rich motif, allowing for adjusted protein production.
2 UT Southwestern scientists honored as rising stars in Texas research
Two UT Southwestern researchers, Dr. Lora Hooper and Dr. Youxing Jiang, are recognized for their innovative work on immune mechanisms and ion channels. Their discoveries have significant implications for understanding and treating conditions like inflammatory bowel disorders and channelopathies.
(Antibody) orientation matters
A study found that antibodies attached to bacteria via their Fc regions in saliva, while in blood they bound primarily via their Fab regions. This difference in orientation was linked to the local antibody concentration, with low levels favoring Fc-mediated binding and high levels favoring Fab-mediated binding.
Biochemists trap a chaperone machine in action
Researchers at the University of Massachusetts Amherst have deciphered key steps in the mechanism of Hsp70 molecular machines, which facilitate protein folding. The study provides insights into how chaperones work and their role in rapidly dividing cells, including cancer cells, highlighting potential therapeutic targets.
Bacteria hijack host cell process, create their own food supply to become infectious
Scientists found bacteria that cause tick-borne disease create their own food supply by hijacking autophagy process in host cells. This allows them to grow and remain hidden from the immune system.
Study suggests new way to prevent recurrent ear infections
Researchers found that eliminating bacteria's DNA and boosting human beta-defensin-3 can kill NTHI bacteria, a major cause of middle ear infections. The study suggests a new treatment approach to target biofilms formed by the bacteria.
Structure discovered for promising tuberculosis drug target
The Johns Hopkins team used X-ray crystallography to map the arrangement of atoms in the enzyme that forms unique molecular bonds within the cell wall of Mycobacterium tuberculosis. This structure reveals a distinct pattern of bonds, creating a new target for TB drug development.
Antibiotics that only partly block protein machinery allow germs to poison themselves
Researchers discovered that powerful antibiotics can only partly block protein synthesis in bacteria, allowing the cells to continue producing proteins that may ultimately lead to their own demise. This finding has significant implications for antibiotic development and could lead to the creation of more effective treatments.
Scientists target bacterial transfer of resistance genes
Researchers at the University of Illinois have developed a new approach to inhibit the transfer of antibiotic-resistance genes in Streptococcus pneumoniae. By targeting a protein called CSP, they found that artificial versions of this protein can block gene transfer and reduce the infectious capacity of the bacteria.
Rejecting arsentate
Researchers discovered that bacteria in arsenic-rich environments developed a protein, PBP, with extreme selectivity for phosphate over arsenate. The unique bond between the protein and arsenate molecule led to repulsion and prevented its entry into the cell.
Duke Medicine news -- Protein structure unlocks 1 mystery of multi-drug tolerance
Researchers describe experiments exploring multi-drug tolerance, a phenomenon that allows bacteria to outwit antibiotics. By analyzing HipA protein's structure and biochemical components, they gained insight into how this mechanism enables bacterial dormancy.
Study finds germ-killing power in the eyes
Researchers at the University of California, Berkeley have identified a germ-killing power in the eyes' keratin protein, which can effectively combat bacteria such as Streptococcus pyogenes and Pseudomonas aeruginosa. The synthetic molecules derived from this protein show promise as low-cost therapeutics against various infections.
Horticultural hijacking
Researchers reveal that beneficial root bacteria, like Bacillus subtilis, suppress plant immunity to control the relationship, boosting growth through nitrogen conversion. This complex interaction raises questions about the benefits and drawbacks of these symbiotic relationships.
Evolution is as complicated as 1-2-3
A team of researchers analyzed 29 genomes from different generations of E. coli bacteria to understand how they evolved to supplement their traditional diet with citrate. They discovered a three-step process: potentiation, actualization, and refinement, which led to the development of new biological functions.
Notre Dame research could provide new insights into tuberculosis and other diseases
Researchers have developed a novel method to directly detect bacterial protein secretion, shedding light on the virulence mechanisms of pathogens like tuberculosis. The technique has significant implications for understanding disease progression and identifying potential therapeutic targets.
Reversible oxygen-sensing 'switching' mechanism discovered
Bacteria use a reversible switching mechanism to adapt to environments lacking oxygen, revealing a new 'antioxidant' pathway for repairing damaged proteins. This discovery has implications for the development of new antibiotics and our understanding of iron-sulfur cluster proteins in various cellular processes.
SourceUniversity of East Anglia·JournalProceedings of the National Academy of Sciences·DateSep 10, 2012
UGA chemistry discovery could have major medical implications
Researchers at UGA have made a major medical breakthrough by discovering how an oxygen-sensing bacterial protein senses oxygen through reversible structural changes in an iron-sulfur cluster. This mechanism could ultimately lead to a better understanding of the aging process and new treatments for human diseases.
Rice, MD Anderson scientists probe mystery of operon evolution
Researchers at Rice University and MD Anderson Cancer Center offer a possible explanation for the existence of operons, jointly controlled clusters of genes found in bacterial chromosomes. The study suggests that operons help bacteria deal with noisy biochemical signals by suppressing noise in gene regulatory networks.
Biophysicists unravel secrets of genetic switch
Researchers discovered how nonspecific binding plays a critical role in controlling the switch between dormant and virulent states in bacteria. The study used single-molecule techniques to characterize the role of non-specific binding in facilitating the closure of a DNA loop that switches off virulence.
The American Society for Microbiology honors Andrew Lovering
Andrew Lovering, a renowned structural biologist, has received the ICAAC Young Investigator Award for his seminal research on bacterial cell wall synthesis and modification. His work has significantly advanced our understanding of antibacterial targets and membrane-anchored proteins in bacteria.
Anthrax targets
Researchers have discovered a range of protein targets in Bacillus anthracis that could be used to create new drugs, potentially reducing the risk of resistance. The identification of novel targets is crucial in the fight against anthrax and biological weapon threats.
SourceInderscience Publishers·JournalInternational Journal of Computational Biology and Drug Design·DateAug 20, 2012
Teamwork against Benzene
Researchers from Helmholtz Centre for Environmental Research identified three teams of bacteria working together to degrade benzene, a highly toxic substance. By analyzing proteins, they shed light on the complex process, which could also apply to other bacterial cooperatives.
Powerful lasers, deep-sea bacteria's pressure tolerance, and more at meeting of crystallographers
At the annual meeting of crystallographers, researchers presented groundbreaking studies on X-ray laser technology, deep-sea bacteria's pressure tolerance, and molecular mechanisms underlying bacterial resistance to antibiotics. The discoveries have significant implications for fields such as medicine, genomics, and material science.
Delving into the molecular mechanism behind deep-sea bacteria's pressure tolerance
A Japanese research team identified a structural change in a protein that confers pressure-resistant properties on deep-sea bacteria. This finding may help guide the design of enzymes for use in high-pressure chemical industrial processes, exploiting the unique adaptation mechanisms of these organisms.
Newfound gene may help bacteria survive in extreme environments
Researchers at MIT have discovered a bacterial gene that enables microbes to thrive in oxygen-depleted conditions, producing lipid biomarkers that may signify dramatic changes in Earth's history. This discovery could provide insights into mass extinctions and climate disturbances.
SourceMassachusetts Institute of Technology·JournalProceedings of the National Academy of Sciences·DateJul 25, 2012
New recruits in the fight against disease
Scientists at Monash University have deciphered the atomic structure of PlyC, a powerful anti-bacterial lysin that kills bacteria causing infections from sore throats to pneumonia. PlyC's unique 'saucer' shape and eight docking sites make it 100 times more efficient than other lysins at killing certain bacteria.
Giving ancient life another chance to evolve
Researchers inserted ancient gene into modern-day E. coli and observed its evolution over 1,000 generations. The results showed that the ancient gene did not mutate to become more similar to its modern form, but rather the bacteria adapted through novel mutations.
NUS-led research team discovers how bacteria sense salt stress
A NUS-led team has discovered how bacteria respond to salt changes using specialized protein molecules that change shape in response to environmental salt concentrations. This finding provides a unified model of how bacteria sense their environment and has immediate applications in understanding life processes across species.
BESC researchers tap into genetic reservoir of heat-loving bacteria
A team of researchers has identified a group of proteins in heat-loving bacteria that enable them to break down cellulose, a key challenge in producing cost-effective biofuels. By analyzing the genomes and proteomics of these bacteria, the scientists pinpointed unique genes responsible for their ability to degrade cellulose.
Innate immune system protein provides a new target in war against bacterial infections
A new study led by St. Jude Children's Research Hospital identified an innate immune system component that suppresses inflammation, which in turn dampens the immune response to infections. The findings suggest that targeting this protein could block bacterial infection and offer a completely new approach to fighting infections.
A step toward minute factories that produce medicine inside the body
Researchers have created micro- and nano-sized capsules containing DNA, biological machinery, and protein synthesis equipment for making medicines. These tiny production units can be turned on with an external signal, producing active proteins on demand.
Discovery increases understanding how bacteria spread: U of A study
Researchers discovered how bacteria release proteins to spread infections, providing a new target for antibiotic development. The discovery sheds light on the mechanism by which normal, non-pathogenic bacteria can release proteins through their membrane pores.
Researchers reveal crucial immune fighter role of the STING protein
The study reveals STING protein's double wing-like crystal structure that captures secreted molecules from invading pathogens, activating the body's powerful immune response. This discovery provides insights into how STING activates an immune response by engaging with specific molecular patterns linked to microbial pathogens.
Bacterial armor for the first time visualized in minute detail
Researchers have imaged the structure of the S-layer protein coat in bacteria down to individual atoms, revealing its role as a protective layer. The discovery provides insights into how bacteria interact with their environment and could lead to new nanomaterials and drug delivery methods.
Scientists reveal structure of bacterial chainmail
Researchers have imaged S-layer of Geobacillus stearothermophilus bacterium down to atomic scale, revealing chainmail-like structure that provides tough yet flexible protection and allows nutrients to diffuse in and out. This discovery holds promise for developing new vaccines by exploiting the ability of S-layers to self-assemble.
A new strategy for developing meningitis vaccines
Researchers identified glycerophosphate oxidase as a critical protein for bacterial progression to the brain. A vaccine against this protein protected mice from invasive pneumococcal disease, offering a new approach to immunizing against S. pneumoniae.
Scientists study serious immune malfunction
Scientists have mapped how the XIAP protein activates a vital component of the immune defense system, specifically fighting bacterial infections. The study provides important insights into X-linked lymphoproliferative syndrome type 2 (XLP2), a rare genetic disorder affecting male children.
Bio-hybrid device acts as 'thermostat' to control systemic inflammation in sepsis
Researchers at University of Pittsburgh School of Medicine developed a bio-hybrid device that acts as an 'inflammation thermostat' to control systemic inflammation in sepsis. The device loads human liver cells engineered to produce anti-inflammatory proteins, which balance inflammation and immune responses.
SourceUniversity of Pittsburgh Schools of the Health Sciences·JournalDisruptive Science and Technology·DateMay 14, 2012
Researchers at the RUB and from Taiwan discover energy supply for protein secretion
Scientists have identified the energy supplier ATP and its binding protein TssM, which drives the export of Hcp through two membranes into the environment. The discovery sheds light on the mechanism of the type VI secretion system, a previously unknown bacterial transport system.
A needle in a haystack: How does a broken DNA molecule get repaired?
Researchers from Delft University of Technology have discovered a crucial step in the DNA repair process, revealing how a broken DNA molecule efficiently searches for a matching sequence. The discovery uses a dual-molecule technique to clarify why certain sequences lead to quick dissociation while others form strong bonds.
Bacteria discovery could lead to antibiotics alternatives
Researchers at the University of Manchester have identified a protein called calpain that allows Listeria bacteria to spread infection within human cells. By blocking this protein, new anti-infective drugs may be developed to combat antibiotic resistance.
Discovery of earliest life forms' operation promises new therapies for key diseases
Researchers at Case Western Reserve University have discovered a parallel between bacterial and human cell behavior, shedding light on potential treatments for diseases. The study found that nitric oxide plays a fundamental regulatory role in controlling bacterial function via S-nitrosylation.
Scientist wins $3 million renewal of one of longest-running NIH grants to Scripps Research
James Hoch's research aims to understand bacterial signaling interactions and their role in disease. His work has identified strategies for disrupting virulence factors and essential bacterial functions, suggesting potential approaches to treating antibiotic-resistant infections.
Research offers new clues to prevent infection in cardiac devices
Scientists at the University of York discovered that bacteria release long protein chains to form biofilms on implanted devices, making infections difficult to treat. This understanding could lead to new treatments and prevention methods for cardiac device infections.
Disarming disease-causing bacteria
Research discovered a protein complex called the Translocation and Assembly Module (TAM), which forms a molecular pump allowing bacteria to shuttle disease-causing molecules from inside to outside the bacterial cell. This finding paves the way for designing new drugs that inhibit this process, potentially preventing antibiotic resistance.
Bacteria use chat to play the 'Prisoner's Dilemma' game in deciding their fate
Scientists discovered that bacteria engage in quorum sensing to discuss options for life-or-death situations, deciding between sporing or competency. This communication process has implications for understanding human cell behavior and developing new treatments for diseases.
From scourge to saint: E. coli bacteria becomes a factory – to make cheaper, faster pharmaceuticals
Researchers at Cornell University have engineered E. coli bacteria to produce glycoproteins for pharmaceuticals, reducing production time and cost. The method, called 'glycans by design,' uses enzymes to tailor sugar structures, leading to the development of cheaper and faster pharmaceuticals.
Team discovers how bacteria resist a 'Trojan horse' antibiotic
Researchers discovered how bacteria modify an enzyme to recognize and disarm a potent antibiotic. The adaptation allows bacteria to protect themselves from toxins while still being susceptible to certain antibiotics, offering new insights into treatment strategies.
SourceUniversity of Illinois at Urbana-Champaign, News Bureau·JournalProceedings of the National Academy of Sciences·DateMar 19, 2012
Nanopills release drugs directly from the inside of cells
Researchers developed nanoparticles called nanopills to release proteins with therapeutic effects, successfully recovering activity in 'sick' mammalian cells. The technology has been licensed and is being developed by biotech firm Janus Developments.
Targeted antibacterial agent rapidly created in response to serious food safety pathogen
A highly targeted bactericidal protein against the life-threatening foodborne E. coli O104 strain was rapidly created, demonstrating its ability to specifically bind and kill tested E. coli strains that produce the O104 lipopolysaccharide antigen.
The dance of the chaperones
Researchers have identified DnaK as a central player in the chaperone network of E. coli, which helps proteins fold into their complex three-dimensional structures. This discovery sheds light on the mechanisms behind protein folding and has implications for understanding diseases such as Alzheimer's and Parkinson's.