Acinetobacter baumannii strain:MRSN110819
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA950448 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| Other | ||||
| SRR24034150_1.fastq.gz | Fastqsanger.gz | |||
| SRR24034150_2.fastq.gz | Fastqsanger.gz |
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Project description:The bacterial pathogen, Acinetobacter baumannii, is a leading cause of drug-resistant infections. Here, we investigated the potential of developing nanobodies that specifically recognize A. baumannii over other Gram-negative bacteria. Through generation and panning of a synthetic nanobody library, we identified several potential lead candidates. We demonstrate how incorporation of next generation sequencing analysis can aid in selection of lead candidates for further characterization. Using monoclonal phage display, we validated the binding of several lead nanobodies to A. baumannii. Subsequent purification and biochemical characterization revealed one particularly robust nanobody that broadly and specifically bound A. baumannii compared to other common drug resistant pathogens. These findings support the potentially for nanobodies to selectively target A. baumannii and the identification of lead candidates for possible future diagnostic and therapeutic development.
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Project description:Background: Acinetobacter baumannii is one of the most dangerous multidrug-resistant pathogens worldwide. Currently, 50-70% of clinical isolates of A. baumannii are extensively drug-resistant (XDR) and available antibiotic options against A. baumannii infections are limited. There are still needs to discover specific de facto bacterial antigenic proteins that could be effective vaccine candidates in human infection. With the growth of research in recent years, several candidate molecules have been identified for vaccine development. So far, there is no public health authorities approved vaccine against A. baumannii. Methods: The purpose of this study was to identify immunodominant vaccine candidate proteins that can be immunoprecipitated specifically with patients’ IgGs. Relaying on hypothesis that IgGs of infected person have capacity to capture immunodominant bacterial proteins. Herein, outer membrane and secreted proteins of sensitive and drug resistant A. baumannii were captured by using IgGs obtained from patient and healthy control sera and were identified by LC-MS/MS analysis. Results: By using subtractive proteomic approach, we determined 34 unique proteins which were captured only in drug-resistant A. baumannii strain via patient sera. After extensive evaluation of predicted epitope regions, solubility, membrane transverse characteristics, and structural properties, we selected several notable vaccine candidates. Conclusion: We identified vaccine candidate proteins that triggered de facto response of human immune system against the antibiotic-resistant A. baumannii. Precipitation of bacterial proteins via patient immunoglobulins was a novel approach to identify the proteins which have potential to trigger to response in patient immune system.
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Project description:Acinetobacter baumannii is currently a major threat to human health. With the spread of multidrug-resistant (MDR) and extensively drug-resistant (XDR) strains, the development of complementary strategies is needed. A promising complimentary and realistic strategy could be phage therapy, which uses bacteriophages (phages), i.e viruses that specifically infect and kill bacterial cells during their life cycle. We designed a two-phage cocktail highly efficient against an extensive drug-resistant (XDR) A. baumannii isolate collected from a patient with burn wound infection at CHUV (termed Ab125). A first in vitro screen of our collection of 34 different phages identified only phage vB_AbaM_3098 as capable of lysing Ab125. However, quick selection of phage-resistant clones (termed Ab139) occurred. Comparative genomics and proteomics between Ab125 and Ab139 revealed several key variations. Very interestingly, we observed that Ab139 became susceptible to six different phages in the collection, otherwise inactive on Ab125. Phage-resistance was also selected when Ab139 was challenged with either of the six phages, with bacterial regrowth observed between 14 h and 16 h. However, combination of vB_AbaM_3098 and vB_AbaM_3014 led to a two-phage cocktail capable of totally inhibiting the growth of Ab125. Treatment with the phage cocktail led to 90% survival after 5 days in the in vivo Galleria Mellonella model of infectious diseases, compared to 0% in the non-treated group. We show that the combination of a phage that only slightly shifted the in vitro bacterial growth curve with an “inactive phage” led to the formulation of a highly bactericidal phage cocktail against Ab125. We then tested the therapeutic potential of the assembled cocktail in synergy with antibiotics and found a synergy with colistin. This work highlights the complexity sometimes involved in the assembly of potent phage cocktail.
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