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Journal articles on the topic 'Acinetobacter baumannii, RNA binding protein'

Author: Grafiati

Published: 11 March 2023

Last updated: 31 July 2025

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1

Ciani, Caterina, Anna Pérez-Ràfols, Isabelle Bonomo, et al. "Identification and Characterization of an RRM-Containing, RNA Binding Protein in Acinetobacter baumannii." Biomolecules 12, no. 7 (2022): 922. http://dx.doi.org/10.3390/biom12070922.

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Acinetobacter baumannii is a Gram-negative pathogen, known to acquire resistance to antibiotics used in the clinic. The RNA-binding proteome of this bacterium is poorly characterized, in particular for what concerns the proteins containing RNA Recognition Motif (RRM). Here, we browsed the A. baumannii proteome for homologous proteins to the human HuR(ELAVL1), an RNA binding protein containing three RRMs. We identified a unique locus that we called AB-Elavl, coding for a protein with a single RRM with an average of 34% identity to the first HuR RRM. We also widen the research to the genomes of

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De Silva, P. Malaka, Rakesh Patidar, Christopher I. Graham, Ann Karen C. Brassinga, and Ayush kumar. "A response regulator protein with antar domain, AvnR, in Acinetobacter baumannii ATCC 17978 impacts its virulence and amino acid metabolism." Microbiology 166, no. 6 (2020): 554–66. http://dx.doi.org/10.1099/mic.0.000913.

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Acinetobacter baumannii, a Gram-negative coccobacillus, is notorious for its involvement in opportunistic infections around the world. Its resistance to antibiotics makes treatment of infections challenging. In this study, we describe a novel response regulator protein, AvnR (A1S_2006) that regulates virulence-related traits in A. baumannii ATCC17978. Sequence analysis suggests that AvnR is a CheY-like response regulator and contains the RNA-binding ANTAR (AmiR and NasR transcription anti-termination regulators) domain. We show that AvnR plays a role in regulating biofilm formation (on glass a

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3

Gao, Lili, and Xiaochun Ma. "Transcriptome Analysis of Acinetobacter baumannii in Rapid Response to Subinhibitory Concentration of Minocycline." International Journal of Environmental Research and Public Health 19, no. 23 (2022): 16095. http://dx.doi.org/10.3390/ijerph192316095.

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The increasing emergence of multidrug-resistant Acinetobacter baumannii brings great threats to public health. Minocycline is a kind of semisynthetic derivative of the antibacterial drug tetracycline and is often used to treat infections caused by multidrug-resistant A. baumannii with other antibiotics. However, minocycline-resistant A. baumannii appears constantly. To rapidly explore the response of A. baumannii to minocycline stress, RNA-seq was carried out to compare the difference in the transcriptome of A. baumannii ATCC19606 in the presence or absence of minocycline. The results showed t

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Roja, Pathakota, and V. Santhosh Kumar. "In-silico Docking and Toxicity Analysis of N-acetyl D- glucosamine with Antimicrobial Proteins- A Novel Targeting against Antimicrobial Resistance." INTERNATIONAL JOURNAL OF PHARMACEUTICAL QUALITY ASSURANCE 14, no. 01 (2023): 66–75. http://dx.doi.org/10.25258/ijpqa.14.1.12.

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Nutraceuticals are popular health-promoting agents for various disease ailments such as food supplements, health promoters, etc. The rising antimicrobial resistance concerns are a serious challenge to researchers and need of the hour to be addressed by developing novel antimicrobial agents. One prospective nutraceutical that has been chosen as a candidate for development as an antibacterial agent is N-acetyl-D-glucosamine. GlcNAc is a monomer of chitin, a substance found in the cell walls of several fungi, mollusks, and cephalopod beaks. The present study aimed to evaluate NAG’s antimicrobial

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Oh, Kyu-Wan, Kyeongmin Kim, Md Maidul Islam, et al. "Transcriptional Regulation of the Outer Membrane Protein A in Acinetobacter baumannii." Microorganisms 8, no. 5 (2020): 706. http://dx.doi.org/10.3390/microorganisms8050706.

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Acinetobacter baumannii is known for its virulence in severely ill, hospitalized patients and for exhibiting multidrug resistance. A. baumannii infection treatment poses a serious problem in clinical environments. The outer membrane protein A (OmpA) of the Acinetobacter genus is involved in bacterial virulence. Regulatory factors of OmpA in the post-transcriptional stage have been previously identified. However, the regulatory factors that act before the transcriptional stage remain unclear. We investigated the A1S_0316 gene that encodes a putative transcription factor for OmpA expression in A

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Twana Salih and Hawzhin A. Salih. "In Silico Design and Molecular Docking Studies of Carbapenem Analogues Targeting Acinetobacter baumannii PBP1A Receptor." Al Mustansiriyah Journal of Pharmaceutical Sciences 20, no. 3 (2020): 35–50. http://dx.doi.org/10.32947/ajps.v20i3.759.

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Carbapenems are considered as the most effective antibiotic against Acinetobacter baumannii infections, as the pathogen has a resistance to the most of the other beta-lactam antibiotics; however, recent studies proved that this pathogen has developed resistance to carbapenems, as well. Therefore, development of novel therapeutics targeting A. baumannii resistant strains is an urgent global requirement. One of the causes responsible for this bacterial resistance against beta-lactam antibiotics is the decreased strength of interactions between A. baumannii Penicillin-Binding Proteins 1A (P

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7

Koenigs, Arno, Peter F. Zipfel, and Peter Kraiczy. "Translation Elongation Factor Tuf of Acinetobacter baumannii Is a Plasminogen-Binding Protein." PLOS ONE 10, no. 7 (2015): e0134418. http://dx.doi.org/10.1371/journal.pone.0134418.

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8

Suvaithenamudhan, Suvaiyarasan, Sivapunniyam Ananth, Vanitha Mariappan, et al. "In Silico Evaluation of Bioactive Compounds of Artemisia pallens Targeting the Efflux Protein of Multidrug-Resistant Acinetobacter baumannii (LAC-4 Strain)." Molecules 27, no. 16 (2022): 5188. http://dx.doi.org/10.3390/molecules27165188.

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Acinetobacter baumannii (A. baumannii) is one of the major representative aetiologies of recalcitrant nosocomial infections. Genotypic and phenotypic alterations in A. baumannii have resulted in a significant surge in multidrug resistance (MDR). Of all the factors responsible for the development of antimicrobial resistance (AMR), efflux protein pumps play a paramount role. In pursuit of a safe alternative for the prevention and control of A. baumannii infections, bioactive compounds from the aerial parts of the medicinal plant Artemisia pallens were studied. GC-MS analysis of the ethanol extra

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9

Patching, Simon G. "Spermidine Binding to the Acetinobacter baumannii Efflux Protein AceI Observed by Near-UV Synchrotron Radiation Circular Dichroism Spectroscopy." Radiation 2, no. 2 (2022): 228–33. http://dx.doi.org/10.3390/radiation2020016.

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The aim of this work was to test polyamines as potential natural substrates of the Acinetobacter baumannii chlorhexidine efflux protein AceI using near-UV synchrotron radiation circular dichroism (SRCD) spectroscopy. The Gram-negative bacterium A. Baumannii is a leading cause of hospital-acquired infections and an important foodborne pathogen. A. Baumannii strains are becoming increasingly resistant to antimicrobial agents, including the synthetic antiseptic chlorhexidine. AceI (144-residues) was the founding member of the recently recognised PACE family of bacterial multidrug efflux proteins.

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10

Gupta*, Debdoot, and Priya Mondal. "Drug Repurposing against Anhydro-N-acetylmuramic Acid Kinase of Multi-Drug Resistant Acinetobacter baumannii: An in Silico Approach." Biosciences Biotechnology Research Asia 20, no. 4 (2023): 1383–94. http://dx.doi.org/10.13005/bbra/3184.

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ABSTRACT: Acinetobacter baumannii, a gram-negative coccobacillus is accountable for different nosocomial diseases. It has been enlisted in the ‘critical’ category in WHO published list depending on the urgency for novel drug development as it becomes multidrug resistant (MDR). The aim of this study was to find a drug which can be repurposed against any drug target of these bacteria and thus the time and cost required for typical drug development procedure can be bypassed. In this study, Anhydro-N-acetylmuramic acid kinase (AnmK) of Acinetobacter baumannii was analyzed to be a good drug target

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11

Koenigs, Arno, Peter F. Zipfel, and Peter Kraiczy. "Correction: Translation Elongation Factor Tuf of Acinetobacter baumannii Is a Plasminogen-Binding Protein." PLOS ONE 10, no. 9 (2015): e0138398. http://dx.doi.org/10.1371/journal.pone.0138398.

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12

Shahryari, Shahab, Parvin Mohammadnejad, and Kambiz Akbari Noghabi. "Screening of anti- Acinetobacter baumannii phytochemicals, based on the potential inhibitory effect on OmpA and OmpW functions." Royal Society Open Science 8, no. 8 (2021): 201652. http://dx.doi.org/10.1098/rsos.201652.

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Therapeutic options including last-line or combined antibiotic therapies for multi-drug-resistant strains of Acinetobacter baumannii are ineffective. The outer membrane protein A (OmpA) and outer membrane protein W (OmpW) are two porins known for their different cellular functions. Identification of natural compounds with the potentials to block these putative porins can attenuate the growth of the bacteria and control the relating diseases. The current work aimed to screen a library of 384 phytochemicals according to their potentials to be used as a drug, and potentials to inhibit the functio

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13

Shil, Aparna, Most Afrin Akter, Arafin Sultana, Sajal Kumar Halder, and Mahbubul Kabir Himel. "Targeting Shikimate Kinase Pathway of Acinetobacter baumannii: A Structure-Based Computational Approach to Identify Antibacterial Compounds." Journal of Tropical Medicine 2023 (March 29, 2023): 1–14. http://dx.doi.org/10.1155/2023/6360187.

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Acinetobacter baumannii (A. baumannii) is an opportunistic bacterium that has developed multidrug resistance (MDR) to most of today’s antibiotics, posing a significant risk to human health. Considering the fact that developing novel drugs is a time-consuming and expensive procedure, this research focuses on utilizing computational resources for repurposing antibacterial agents for A. baumannii. We targeted shikimate kinase, an essential enzyme in A. baumannii, that plays a significant role in the metabolic process. The basis for generating new therapeutic compounds is to inhibit the shikimate

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14

Young, Mikaeel, Michaelle Chojnacki, Catlyn Blanchard, et al. "Genetic Determinants of Acinetobacter baumannii Serum-Associated Adaptive Efflux-Mediated Antibiotic Resistance." Antibiotics 12, no. 7 (2023): 1173. http://dx.doi.org/10.3390/antibiotics12071173.

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Acinetobacter baumannii is a nosocomial pathogen of serious healthcare concern that is becoming increasingly difficult to treat due to antibiotic treatment failure. Recent studies have revealed that clinically defined antibiotic-susceptible strains upregulate the expression of a repertoire of putative drug efflux pumps during their growth under biologically relevant conditions, e.g., in human serum, resulting in efflux-associated resistance to physiologically achievable antibiotic levels within a patient. This phenomenon, termed Adaptive Efflux Mediated Resistance (AEMR), has been hypothesized

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15

Beig, Masoumeh, Mohammad Sholeh, Safoura Moradkasani, Behzad Shahbazi, and Farzad Badmasti. "Development of a multi-epitope vaccine against Acinetobacter baumannii: A comprehensive approach to combating antimicrobial resistance." PLOS ONE 20, no. 3 (2025): e0319191. https://doi.org/10.1371/journal.pone.0319191.

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Background The World Health Organization has categorized Acinetobacter baumannii (A. baumannii) as a critical priority pathogen due to its high antibiotic resistance. This resistance complicates treatment and underscores the urgent need for new antibiotics and strategies. This study developed a multi-epitope vaccine (MEV) to address this significant public health threat. Methods This study employed a computational approach to design MEV targeting A. baumannii strain VB7036. Surface-exposed proteins were identified using PSORTb and TMHMM, followed by antigenicity and allergenicity predictions u

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Choi, Sungjae, Jungwoo Park, Jiwon Yeon, Ahjin Jang, Woo Cheol Lee та Yangmee Kim. "Deciphering the Binding Interactions between Acinetobacter baumannii ACP and β-ketoacyl ACP Synthase III to Improve Antibiotic Targeting Using NMR Spectroscopy". International Journal of Molecular Sciences 22, № 7 (2021): 3317. http://dx.doi.org/10.3390/ijms22073317.

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Fatty acid synthesis is essential for bacterial viability. Thus, fatty acid synthases (FASs) represent effective targets for antibiotics. Nevertheless, multidrug-resistant bacteria, including the human opportunistic bacteria, Acinetobacter baumannii, are emerging threats. Meanwhile, the FAS pathway of A. baumannii is relatively unexplored. Considering that acyl carrier protein (ACP) has an important role in the delivery of fatty acyl intermediates to other FAS enzymes, we elucidated the solution structure of A. baumannii ACP (AbACP) and, using NMR spectroscopy, investigated its interactions wi

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17

ud-din, Miraj, Aqel Albutti, Asad Ullah, et al. "Vaccinomics to Design a Multi-Epitopes Vaccine for Acinetobacter baumannii." International Journal of Environmental Research and Public Health 19, no. 9 (2022): 5568. http://dx.doi.org/10.3390/ijerph19095568.

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Antibiotic resistance (AR) is the result of microbes’ natural evolution to withstand the action of antibiotics used against them. AR is rising to a high level across the globe, and novel resistant strains are emerging and spreading very fast. Acinetobacter baumannii is a multidrug resistant Gram-negative bacteria, responsible for causing severe nosocomial infections that are treated with several broad spectrum antibiotics: carbapenems, β-lactam, aminoglycosides, tetracycline, gentamicin, impanel, piperacillin, and amikacin. The A. baumannii genome is superplastic to acquire new resistant mecha

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18

Liu, Cong, Xingyun Wang, Yueling Zheng, et al. "mRNA-LNP Vaccines Targeting SmpA-PLD and OmpK-Omp22 Induce Protective Immunity Against Acinetobacter baumannii." Vaccines 13, no. 7 (2025): 764. https://doi.org/10.3390/vaccines13070764.

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Background: Acinetobacter baumannii (A. baumannii) has emerged as a critical human pathogen, causing high mortality rates among hospitalized patients and frequently triggering nosocomial outbreaks. The increasing prevalence of multidrug-resistant (MDR) A. baumannii poses a pressing threat to public health. To date, no commercially available vaccine against A. baumannii has been developed for clinical use. messenger RNA (mRNA)–lipid nanoparticle (LNP) vaccines have emerged as a promising vaccination strategy. Methods: In this work, we developed two mRNA vaccines targeting SmpA-PLD and the fusio

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19

Hmadcha, Abdelkrim. "Antibiotic discovery with artificial intelligence for the treatment of Acinetobacter baumannii infections." mSystems 9, no. 6 (2024): e0032524. https://doi.org/10.1128/msystems.00325-24.

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Global challenges presented by multidrug-resistant <em>Acinetobacter baumannii</em> infections have stimulated the development of new treatment strategies. We reported that outer membrane protein W (OmpW) is a potential therapeutic target in <em>A. baumannii</em>. Here, a library of 11,648 natural compounds was subjected to a primary screening using quantitative structure-activity relationship (QSAR) models generated from a ChEMBL data set with >7,000 compounds with their reported minimal inhibitory concentration (MIC) values against <em>A. baumannii</em> followed b

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20

Crua Asensio, Nuria, Javier Macho Rendón, and Marc Torrent Burgas. "Time-Resolved Transcriptional Profiling of Epithelial Cells Infected by Intracellular Acinetobacter baumannii." Microorganisms 9, no. 2 (2021): 354. http://dx.doi.org/10.3390/microorganisms9020354.

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The rise in the number of antibiotic-resistant bacteria has become a serious threat to health, making it important to identify, characterize and optimize new molecules to help us to overcome the infections they cause. It is well known that Acinetobacter baumannii has a significant capacity to evade the actions of antibacterial drugs, leading to its emergence as one of the bacteria responsible for hospital and community-acquired infections. Nonetheless, how this pathogen infects and survives inside the host cell is unclear. In this study, we analyze the time-resolved transcriptional profile cha

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21

Xu, Jingzhi, Xiaobo Li, Guangbo Kang, Liang Bai, Ping Wang, and He Huang. "Isolation and Characterization of AbTJ, an Acinetobacter baumannii Phage, and Functional Identification of Its Receptor-Binding Modules." Viruses 12, no. 2 (2020): 205. http://dx.doi.org/10.3390/v12020205.

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A. baumannii is an opportunistic pathogen and a major cause of various community-acquired infections. Strains of this species can be resistant to multiple antimicrobial agents, leaving limited therapeutic options, also lacking in methods for accurate and prompt diagnosis. In this context, AbTJ, a novel phage that infects A. baumannii MDR-TJ, was isolated and characterized, together with its two tail fiber proteins. Morphological analysis revealed that it belongs to Podoviridae family. Its host range, growth characteristics, stability under various conditions, and genomic sequence, were systema

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Ambrosi, Cecilia, Daniela Scribano, Meysam Sarshar, Carlo Zagaglia, Bernhard B. Singer, and Anna Teresa Palamara. "Acinetobacter baumannii Targets Human Carcinoembryonic Antigen-Related Cell Adhesion Molecules (CEACAMs) for Invasion of Pneumocytes." mSystems 5, no. 6 (2020): e00604-20. http://dx.doi.org/10.1128/msystems.00604-20.

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ABSTRACTMultidrug-resistant Acinetobacter baumannii is regarded as a life-threatening pathogen mainly associated with nosocomial and community-acquired pneumonia. Here, we show that A. baumannii can bind the human carcinoembryonic antigen-related cell adhesion molecule (CEACAM) receptors CEACAM1, CEACAM5, and CEACAM6. This specific interaction enhances A. baumannii internalization in membrane-bound vacuoles, promptly decorated with Rab5, Rab7, and lipidated microtubule-associated protein light chain 3 (LC3). Dissecting intracellular signaling pathways revealed that infected pneumocytes trigger

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Wilson, Timothy James, Aminul A. Islam, and Luis A. Actis. "Natural antibodies mediate resistance to Acinetobacter baumanniirespiratory infections." Journal of Immunology 210, no. 1_Supplement (2023): 241.19. http://dx.doi.org/10.4049/jimmunol.210.supp.241.19.

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Abstract Acinetobacter baumanniiis a growing public health threat due to increasing incidence of carbapenem-resistant strains in U.S. hospitals. With widespread antibiotic resistance, there is an urgent need for alternative therapies to treat these infections, which are often acquired in hospital intensive care units. Antibody-based immunotherapies offer one potential treatment avenue, however, adaptive immune responses to A. baumanniihave not been well characterized. Pilot experiments, using a mouse pneumonia model to explore the role of adaptive immunity in clearing A. baumannii, uncovered a

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Jang, Hyunseok, Chang Min Kim, Eunmi Hong, and Hyun Ho Park. "Fully closed conformation of penicillin-binding protein revealed by structure of PBP2 from Acinetobacter baumannii." Biochemical and Biophysical Research Communications 729 (October 2024): 150368. http://dx.doi.org/10.1016/j.bbrc.2024.150368.

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Bohac, Tabbetha J., Luting Fang, Daryl E. Giblin, and Timothy A. Wencewicz. "Fimsbactin and Acinetobactin Compete for the Periplasmic Siderophore Binding Protein BauB in Pathogenic Acinetobacter baumannii." ACS Chemical Biology 14, no. 4 (2019): 674–87. http://dx.doi.org/10.1021/acschembio.8b01051.

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Thorpe, James H., Ian D. Wall, Robert H. Sinnamon, Amy N. Taylor, and Robert A. Stavenger. "Cocktailed fragment screening by X-ray crystallography of the antibacterial target undecaprenyl pyrophosphate synthase from Acinetobacter baumannii." Acta Crystallographica Section F Structural Biology Communications 76, no. 1 (2020): 40–46. http://dx.doi.org/10.1107/s2053230x19017199.

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Direct soaking of protein crystals with small-molecule fragments grouped into complementary clusters is a useful technique when assessing the potential of a new crystal system to support structure-guided drug discovery. It provides a robustness check prior to any extensive crystal screening, a double check for assay binding cutoffs and structural data for binding pockets that may or may not be picked out in assay measurements. The structural output from this technique for three novel fragment molecules identified to bind to the antibacterial target Acinetobacter baumannii undecaprenyl pyrophos

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Siroy, Axel, Virginie Molle, Christelle Lemaître-Guillier, et al. "Channel Formation by CarO, the Carbapenem Resistance-Associated Outer Membrane Protein of Acinetobacter baumannii." Antimicrobial Agents and Chemotherapy 49, no. 12 (2005): 4876–83. http://dx.doi.org/10.1128/aac.49.12.4876-4883.2005.

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ABSTRACT It has been recently shown that resistance to both imipenem and meropenem in multidrug-resistant clinical strains of Acinetobacter baumannii is associated with the loss of a heat-modifiable 25/29-kDa outer membrane protein, called CarO. This study aimed to investigate the channel-forming properties of CarO. Mass spectrometry analyses of this protein band detected another 25-kDa protein (called Omp25), together with CarO. Both proteins presented similar physicochemical parameters (M w and pI). We overproduced and purified the two polypeptides as His-tagged recombinant proteins. Circula

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Boral, Jale, Cansel Vatansever, Gulin Ozcan, et al. "Resensitization to colistin results in rapid and stable recovery of adherence, serum resistance and ompW in Acinetobacter baumannii." PLOS ONE 19, no. 8 (2024): e0309307. http://dx.doi.org/10.1371/journal.pone.0309307.

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Background Colistin resistance in Acinetobacter baumannii is an emerging problem that limits antimicrobial therapy options. Materials & methods We isolated two pairs of colistin susceptible and colistin-resistant A. baumannii (K1007/K1006 and K408/K409) from two patients diagnosed with carbapenem-resistant A. baumannii infection. Colistin susceptible isolates were exposed to in vitro colistin induction for 50 generations. The selected cell populations were subjected to DNA and RNA sequencing and phenotypic assays. Results In the in vitro induction assay, K408 gained colistin resistance on

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Ghavanloughajar, Hannaneh, Moamen M. Elmassry, Amanda M. V. Brown, and Abdul N. Hamood. "Human whole blood influences the expression of Acinetobacter baumannii genes related to translation and siderophore production." PLOS One 20, no. 7 (2025): e0326330. https://doi.org/10.1371/journal.pone.0326330.

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Acinetobacter baumannii is a major cause of bloodstream infections, yet its adaptation and survival mechanisms in human blood remain poorly understood. While previous studies focused on individual blood components, the impact of human whole blood on A. baumannii gene expression has not been explored. To address this, we used an ex vivo model where A. baumannii was grown in human whole blood from healthy volunteers (WBHV) and compared its gene expression to that in Luria-Bertani (LB) broth using RNA-seq. Our lab has previously employed a similar WBHV vs. LB comparison in Pseudomonas aeruginosa,

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Badie, Omar H., Ahmed F. Basyony, and Reham Samir. "Computer-Based Identification of Potential Druggable Targets in Multidrug-Resistant Acinetobacter baumannii: A Combined In Silico, In Vitro and In Vivo Study." Microorganisms 10, no. 10 (2022): 1973. http://dx.doi.org/10.3390/microorganisms10101973.

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The remarkable rise in antimicrobial resistance is alarming for Acinetobacter baumannii, which necessitates effective strategies for the discovery of promising anti-acinetobacter agents. We used a subtractive proteomics approach to identify unique protein drug targets. Shortlisted targets passed through subtractive channels, including essentiality, non-homology to the human proteome, druggability, sub-cellular localization prediction and conservation. Sixty-eight drug targets were shortlisted; among these, glutamine synthetase, dihydrodipicolinate reductase, UDP-N-acetylglucosamine acyltransfe

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Lee, Kyung Hyeon, Soo Hyeon Lee, Iswarduth Soojhawona, et al. "The Structure of Apo Acinetobacter baumannii Dithiol Oxidase DsbA and Isothermal Titration Calorimetry Validation of DsbA for Antimicrobial Drug Development." Structural Dynamics 12, no. 2_Supplement (2025): A375. https://doi.org/10.1063/4.0000681.

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Novel antibacterials with new mechanisms of action are urgently required to overcome multidrug-resistant (MDR) Acinetobacter baumannii. Enzymes in the bacterial disulfide bond (Dsb) forming machinery provide excellent targets for new inhibitor development. One of the enzymes, DsbA, found in the periplasmic space, catalyzes disulfide bond formation for proper folding of proteins in bacteria and represents a promising drug target. Elucidation of the X-ray crystal structure of A. baumannii DsbA (AbDsbA) in-complex with E. coli elongation factor thermal unstable (EcEF-Tu), led to the identificatio

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Salunke, Dinakar M. "Multiple target sites for designing candidate drugs." Biochemical Journal 475, no. 5 (2018): 977–79. http://dx.doi.org/10.1042/bcj20180007.

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Rational drug discovery strategy requires a design of small molecules as candidate drugs which can specifically inhibit a target protein or any other macromolecule and effectively interfere in a defined physiological process. One of the important bacterial protein targets aimed toward developing new antibiotics is peptidyl-tRNA hydrolase (Pth). The discovery that cytarabine, a known anticancer drug, binds to Pth from Acinetobacter baumannii in a cleft located away from the catalytic site of this enzyme, published in Biochemical Journal, opens up interesting new avenues for drug design. An appr

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Li, Jiarui, Guillem Prats-Ejarque, Marc Torrent, et al. "In Vivo Evaluation of ECP Peptide Analogues for the Treatment of Acinetobacter baumannii Infection." Biomedicines 10, no. 2 (2022): 386. http://dx.doi.org/10.3390/biomedicines10020386.

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Antimicrobial peptides (AMPs) are alternative therapeutics to traditional antibiotics against bacterial resistance. Our previous work identified an antimicrobial region at the N-terminus of the eosinophil cationic protein (ECP). Following structure-based analysis, a 30mer peptide (ECPep-L) was designed that combines antimicrobial action against Gram-negative species with lipopolysaccharides (LPS) binding and endotoxin-neutralization activities. Next, analogues that contain non-natural amino acids were designed to increase serum stability. Here, two analogues were selected for in vivo assays: t

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Eijkelkamp, Bart A., Uwe H. Stroeher, Karl A. Hassan, Liam D. H. Elbourne, Ian T. Paulsen, and Melissa H. Brown. "H-NS Plays a Role in Expression of Acinetobacter baumannii Virulence Features." Infection and Immunity 81, no. 7 (2013): 2574–83. http://dx.doi.org/10.1128/iai.00065-13.

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ABSTRACTAcinetobacter baumanniihas become a major problem in the clinical setting with the prevalence of infections caused by multidrug-resistant strains on the increase. Nevertheless, only a limited number of molecular mechanisms involved in the success ofA. baumanniias a human pathogen have been described. In this study, we examined the virulence features of a hypermotile derivative ofA. baumanniistrain ATCC 17978, which was found to display enhanced adherence to human pneumocytes and elevated levels of lethality towardCaenorhabditis elegansnematodes. Analysis of cellular lipids revealed mod

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Gaona, Marc, Jordi Corral, Miquel Sánchez−Osuna, et al. "Reciprocal regulation between Acinetobacter baumannii and Enterobacter cloacae AdeR homologs: implications for antimicrobial resistance and pathogenesis." PLOS ONE 20, no. 3 (2025): e0315428. https://doi.org/10.1371/journal.pone.0315428.

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Acinetobacter baumannii and Enterobacter cloacae are phylogenetically distant Gram−negative bacterial pathogens that represent significant challenges in healthcare settings due to their remarkable ability to acquire antimicrobial resistance. This study investigates one of the most important efflux pump systems in A. baumannii, AdeABC−AdeRS, and identifies homologous components in E. cloacae. By constructing isogenic knockout mutants, we show that the AdeB pump component and the AdeR regulator are significant for antimicrobial resistance and pathogenicity in A. baumannii. Through in silico pred

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Bolla, Jani Reddy, Anna C. Howes, Francesco Fiorentino, and Carol V. Robinson. "Assembly and regulation of the chlorhexidine-specific efflux pump AceI." Proceedings of the National Academy of Sciences 117, no. 29 (2020): 17011–18. http://dx.doi.org/10.1073/pnas.2003271117.

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Few antibiotics are effective againstAcinetobacter baumannii, one of the most successful pathogens responsible for hospital-acquired infections. Resistance to chlorhexidine, an antiseptic widely used to combatA. baumannii, is effected through the proteobacterial antimicrobial compound efflux (PACE) family. The prototype membrane protein of this family, AceI (Acinetobacterchlorhexidine efflux protein I), is encoded for by theaceIgene and is under the transcriptional control of AceR (Acinetobacterchlorhexidine efflux protein regulator), a LysR-type transcriptional regulator (LTTR) protein. Here

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Ciani, Caterina, Anna Pérez-Ràfols, Isabelle Bonomo, et al. "Identification and Characterization of an RRM-Containing, RNA Binding Protein in Acinetobacter baumannii." June 30, 2022. https://doi.org/10.3390/biom12070922.

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Acinetobacter baumannii is a Gram-negative pathogen, known to acquire resistance to antibiotics used in the clinic. The RNA-binding proteome of this bacterium is poorly characterized, in particular for what concerns the proteins containing RNA Recognition Motif (RRM). Here, we browsed the A. baumannii proteome for homologous proteins to the human HuR(ELAVL1), an RNA binding protein containing three RRMs. We identified a unique locus that we called AB-Elavl, coding for a protein with a single RRM with an average of 34% identity to the first HuR RRM. We also widen the researc

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Hamrock, Fergal J., Daniel Ryan, Ali Shaibah, et al. "Global analysis of the RNA–RNA interactome in Acinetobacter baumannii AB5075 uncovers a small regulatory RNA repressing the virulence-related outer membrane protein CarO." Nucleic Acids Research, August 16, 2024. http://dx.doi.org/10.1093/nar/gkae668.

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Abstract Acinetobacter baumannii is an opportunistic Gram-negative pathogen that infects critically ill patients. The emergence of antimicrobial resistant A. baumannii has exacerbated the need to characterize environmental adaptation, antibiotic resistance and pathogenicity and their genetic regulators to inform intervention strategies. Critical to adaptation to changing environments in bacteria are small regulatory RNAs (sRNAs), however, the role that sRNAs play in the biology of A. baumannii is poorly understood. To assess the regulatory function of sRNAs and to uncover their RNA interaction

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Singh, Raja, María Pérez-Varela, Jennifer M. Colquhoun, et al. "CsrA-mediated regulation of a virulence switch in Acinetobacter baumannii." mBio, February 25, 2025. https://doi.org/10.1128/mbio.04058-24.

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ABSTRACT CsrA is an RNA binding protein that functions as a global regulator in bacteria. We demonstrate that, in Acinetobacter baumannii , CsrA acts as a positive regulator of the switch from virulent (VIR-O) to avirulent (AV-T) subpopulations. This regulation is mediated, in part, by CsrA interfering with Rho-dependent termination in the mRNA leader region of the ABUW_1645 gene, encoding the primary TetR-type transcriptional regulator that drives cells from the VIR-O to the AV-T state. We demonstrate that CsrA directly binds to the ABUW_1645 mRNA leader region and interferes with Rho binding

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Kofoed, Eric M., Ignacio Aliagas, Terry Crawford, et al. "Discovery of GuaB inhibitors with efficacy against Acinetobacter baumannii infection." mBio, August 29, 2024. http://dx.doi.org/10.1128/mbio.00897-24.

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ABSTRACT Guanine nucleotides are required for growth and viability of cells due to their structural role in DNA and RNA, and their regulatory roles in translation, signal transduction, and cell division. The natural antibiotic mycophenolic acid (MPA) targets the rate-limiting step in de novo guanine nucleotide biosynthesis executed by inosine-5´-monophosphate dehydrogenase (IMPDH). MPA is used clinically as an immunosuppressant, but whether in vivo inhibition of bacterial IMPDH (GuaB) is a valid antibacterial strategy is controversial. Here, we describe the discovery of extremely potent small

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Han, Sunyong, Jihyeon Min, Yerim Park, and Woojun Park. "Fine‐tuning regulation of (p)ppGpp‐driven outer membrane vesicle formation in Acinetobacter baumannii." FEBS Journal, April 2, 2025. https://doi.org/10.1111/febs.70087.

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The roles of (p)ppGpp in regulating cytosolic proteins are well established; however, their effects on membrane remodeling remain elusive. The translocation of signal recognition particle (SRP)‐dependent proteins can be modulated through (p)ppGpp binding to two key GTPase components: FtsY, which interacts with SecYEG, and Ffh, a homolog of SRP54. A (p)ppGpp‐specific Broccoli RNA aptamer and the chemometer PyDPA were used to quantify the (p)ppGpp levels in the ΔrelA and ΔrelA/ΔspoT strains of Acinetobacter baumannii, confirming a stepwise reduction in (p)ppGpp levels in the following order: wil

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Kumaran, V. Thiru, A. S. Smiline Girija, P. P. Sankar Ganesh, and J. Vijayashree Priyadharshini. "Effect of Azadirachta indica Bio-Compounds against KpsM Protein of Acinetobacter baumannii." Journal of Pharmaceutical Research International, November 5, 2021, 773–80. http://dx.doi.org/10.9734/jpri/2021/v33i47b33182.

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Background: Acinetobacter baumannii was considered as a low priority pathogen earlier, and is been now reported as a priority pathogen causing nosocomial infections. Selection of natural compounds to target the organism is the need of the hour. Aim: This study is aimed to target the KpsM protein of A. baumannii with the bio-compounds from Azadirachta indica using in-silico docking analysis. Materials and Methods: KpsM protein was retrieved and optimisation of protein was done. After that optimization and ligand preparation was carried out. It was continued by molinspiration assessm

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Khan, Shama, Shabir A. Madhi, and Courtney Olwagen. "Structure-based identification of novel inhibitors targeting the enoyl-ACP reductase enzyme of Acinetobacter baumannii." Scientific Reports 13, no. 1 (2023). http://dx.doi.org/10.1038/s41598-023-48696-z.

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AbstractAcinetobacter baumannii is a Gram-negative multidrug-resistant bacterial pathogen primarily associated with nosocomial infections resulting in increased morbidity and mortality in adults and infants, especially in sub-Saharan Africa where the clinical burden is high. New therapeutics are needed to treat multidrug-resistant Acinetobacter baumannii infections and reduce transmission. The study used computer-integrated drug discovery approaches including pharmacophore modelling, molecular docking, and molecular dynamics simulation to screen potential inhibitors against the enoyl-acyl carr

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Russo, Thomas A., Ulrike Carlino-MacDonald, Cassandra L. Alvarado, et al. "Penicillin Binding Protein 7/8 Is a Potential Drug Target in Carbapenem-Resistant Acinetobacter baumannii." Antimicrobial Agents and Chemotherapy, December 7, 2022. http://dx.doi.org/10.1128/aac.01033-22.

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Limited therapeutic options dictate the need for new classes of antimicrobials active against carbapenem-resistant Acinetobacter baumannii . Presented data confirm and extend penicillin binding protein 7/8 (PBP 7/8) as a high-value target in the CR A. baumannii strain HUMC1.

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Viale, Alejandro M., and Benjamin A. Evans. "Microevolution in the major outer membrane protein OmpA of Acinetobacter baumannii." Microbial Genomics 6, no. 6 (2020). http://dx.doi.org/10.1099/mgen.0.000381.

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Acinetobacter baumannii is nowadays a relevant nosocomial pathogen characterized by multidrug resistance (MDR) and concomitant difficulties to treat infections. OmpA is the most abundant A. baumannii outer membrane (OM) protein, and is involved in virulence, host-cell recognition, biofilm formation, regulation of OM stability, permeability and antibiotic resistance. OmpA members are two‐domain proteins with an N‐terminal eight‐stranded β‐barrel domain with four external loops (ELs) interacting with the environment, and a C‐terminal periplasmic domain binding non‐covalently to the peptidoglycan

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Ching, Carly, Kevin Gozzi, Björn Heinemann, Yunrong Chai, and Veronica G. Godoy. "RNA-Mediated cis Regulation in Acinetobacter baumannii Modulates Stress-Induced Phenotypic Variation." Journal of Bacteriology 199, no. 11 (2017). http://dx.doi.org/10.1128/jb.00799-16.

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ABSTRACT In the nosocomial opportunistic pathogen Acinetobacter baumannii, RecA-dependent mutagenesis, which causes antibiotic resistance acquisition, is linked to the DNA damage response (DDR). Notably, unlike the Escherichia coli paradigm, recA and DDR gene expression in A. baumannii is bimodal. Namely, there is phenotypic variation upon DNA damage, which may provide a bet-hedging strategy for survival. Thus, understanding recA gene regulation is key to elucidate the yet unknown DDR regulation in A. baumannii. Here, we identify a structured 5′ untranslated region (UTR) in the recA transcript

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Kamuyu, Gathoni, Yat Suen Cheng, Sam Willcocks, et al. "Sequential Vaccination With Heterologous Acinetobacter baumannii Strains Induces Broadly Reactive Antibody Responses." Frontiers in Immunology 12 (July 30, 2021). http://dx.doi.org/10.3389/fimmu.2021.705533.

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Antibody therapy may be an alternative treatment option for infections caused by the multi-drug resistant (MDR) bacterium Acinetobacter baumannii. As A. baumannii has multiple capsular serotypes, a universal antibody therapy would need to target conserved protein antigens rather than the capsular polysaccharides. We have immunized mice with single or multiple A. baumannii strains to induce antibody responses to protein antigens, and then assessed whether these responses provide cross-protection against a collection of genetically diverse clinical A. baumannii isolates. Immunized mice developed

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Lei, Eric K., Shannon Ryan, Henk van Faassen, et al. "Isolation and characterization of a VHH targeting the Acinetobacter baumannii cell surface protein CsuA/B." Applied Microbiology and Biotechnology, June 7, 2023. http://dx.doi.org/10.1007/s00253-023-12594-1.

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Abstract Acinetobacter baumannii is a Gram-negative bacterial pathogen that exhibits high intrinsic resistance to antimicrobials, with treatment often requiring the use of last-resort antibiotics. Antibiotic-resistant strains have become increasingly prevalent, underscoring a need for new therapeutic interventions. The aim of this study was to use A. baumannii outer membrane vesicles as immunogens to generate single-domain antibodies (VHHs) against bacterial cell surface targets. Llama immunization with the outer membrane vesicle preparations from four A. baumannii strains (ATCC 19606, ATCC 17

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Ries, Julia I., Marie Heß, Noura Nouri, et al. "CipA mediates complement resistance of Acinetobacter baumannii by formation of a factor I-dependent quadripartite assemblage." Frontiers in Immunology 13 (July 26, 2022). http://dx.doi.org/10.3389/fimmu.2022.942482.

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Multidrug-resistant Acinetobacter baumannii is known to be one of the leading pathogens that cause severe nosocomial infections. To overcome eradication by the innate immune system during infection, A. baumannii developed a number of immune evasion strategies. Previously, we identified CipA as a plasminogen-binding and complement-inhibitory protein. Here we show that CipA inhibits all three complement activation pathways and interacts with key complement components C3, C3b, C4b, C5, Factor B, Factor D, and in particular Factor I. CipA also targets function of the C5 convertase as cleavage of C

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Kang, Katie N., Misha I. Kazi, Jacob Biboy, et al. "Septal Class A Penicillin-Binding Protein Activity and LD-Transpeptidases Mediate Selection of Colistin-Resistant Lipooligosaccharide-Deficient Acinetobacter baumannii." mBio 12, no. 1 (2021). http://dx.doi.org/10.1128/mbio.02185-20.

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ABSTRACT Despite dogma suggesting that lipopolysaccharide/lipooligosaccharide (LOS) was essential for viability of Gram-negative bacteria, several Acinetobacter baumannii clinical isolates produced LOS− colonies after colistin selection. Inactivation of the conserved class A penicillin-binding protein, PBP1A, was a compensatory mutation that supported isolation of LOS− A. baumannii, but the impact of PBP1A mutation was not characterized. Here, we show that the absence of PBP1A causes septation defects and that these, together with ld-transpeptidase activity, support isolation of LOS− A. bauman

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