In silico analysis of antibody triggering biofilm associated protein in Acinetobacter baumannii

Rahbar, Mohammad Reza; Rasooli, Iraj; Gargari, Seyed Latif Mousavi; Amani, Jafar; Fattahian, Yaser

doi:10.1016/j.jtbi.2010.06.014

Cited by 48 publications

(30 citation statements)

References 66 publications

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“…In silico analysis of A. baumannii Bap indicated that the protein itself has a high degree of hydrophilicity (27). However, our data show that wild-type Ab307 cells expressing Bap readily incorporate into a hexadecane layer to a significantly greater degree than Bap-deficient cells with a BATH score 23-fold higher than the Bap mutant.…”

Section: Discussionmentioning

confidence: 61%

“…Interestingly, in silico analysis of the Bap sequence using InterProScan software (27) revealed that Ab307 Bap contains homologous domains to the PKD (polycystic kidney disease) domain and the concanavalin A-like lectin/ glucanase domain. The PKD domain has been implicated in protein-protein interactions, whereas the presence of the concanavalin A-like lectin/glucanase domain suggests possible proteincarbohydrate interactions (27). Thus, the structural composition of A. baumannii Bap suggests that future studies should focus on possible protein-protein and protein-carbohydrate interactions.…”

Section: Discussionmentioning

confidence: 99%

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The Acinetobacter baumannii Biofilm-Associated Protein Plays a Role in Adherence to Human Epithelial Cells

2012

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Acinetobacter baumannii is a significant source of nosocomial infections worldwide. This bacterium has the ability to survive and persist on multiple abiotic surfaces in health care facilities, and once a focus has been established, this opportunistic pathogen is difficult to eradicate. This paper demonstrates that the A. baumannii biofilm-associated protein (Bap) is necessary for mature biofilm formation on medically relevant surfaces, including polypropylene, polystyrene, and titanium. Scanning electron microscopy analyses of biofilms show that Bap is required for three-dimensional tower structure and water channel formation. In conjunction with persistence on abiotic surfaces, adherence to eukaryotic cells is an important step in bacterial colonization resulting in infection of the host. We have described Bap as the surface structure involved in adherence of A. baumannii to both normal human bronchial epithelial cells and normal human neonatal keratinocytes. However, Bap is not involved in internalization of the bacterium in these two cell lines. Furthermore, this study shows that the presence of Bap increases the bacterial cell surface hydrophobicity. The results of this study are pertinent, as the data lead to a better understanding of the role of Bap in biofilm formation on medical surfaces and in colonization of the host.

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Section: Discussionmentioning

confidence: 61%

Section: Discussionmentioning

confidence: 99%

The Acinetobacter baumannii Biofilm-Associated Protein Plays a Role in Adherence to Human Epithelial Cells

2012

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“…The difference in the size of the bap genes from A. baumannii strains MS1968 (ϳ16 kb) and AB307-0294 (25.863 kb), despite their similar genetic context, also demonstrates that there is significant variation in the bap genes from different A. baumannii strains. The A. baumannii Bap protein contains a modular structure (53), and the presence of large, identical repeat sequences within module D of bap MS1968 prevented us from generating a complete sequence of the gene. However, we did identify a nonrepetitive sequence that was used to examine the phylogeny of Bap from several species.…”

Section: Discussionmentioning

confidence: 99%

Molecular Analysis of the Acinetobacter baumannii Biofilm-Associated Protein

Goh

Beatson

Totsika

et al. 2013

Appl Environ Microbiol

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e Acinetobacter baumannii is a multidrug-resistant pathogen associated with hospital outbreaks of infection across the globe, particularly in the intensive care unit. The ability of A. baumannii to survive in the hospital environment for long periods is linked to antibiotic resistance and its capacity to form biofilms. Here we studied the prevalence, expression, and function of the A. baumannii biofilm-associated protein (Bap) in 24 carbapenem-resistant A. baumannii ST92 strains isolated from a single institution over a 10-year period. The bap gene was highly prevalent, with 22/24 strains being positive for bap by PCR. Partial sequencing of bap was performed on the index case strain MS1968 and revealed it to be a large and highly repetitive gene approximately 16 kb in size. Phylogenetic analysis employing a 1,948-amino-acid region corresponding to the C terminus of Bap showed that Bap MS1968 clusters with Bap sequences from clonal complex 2 (CC2) strains ACICU, TCDC-AB0715, and 1656-2 and is distinct from Bap in CC1 strains. By using overlapping PCR, the bap MS1968 gene was cloned, and its expression in a recombinant Escherichia coli strain resulted in increased biofilm formation. A Bap-specific antibody was generated, and Western blot analysis showed that the majority of A. baumannii strains expressed an ϳ200-kDa Bap protein. Further analysis of three Bap-positive A. baumannii strains demonstrated that Bap is expressed at the cell surface and is associated with biofilm formation. Finally, biofilm formation by these Bap-positive strains could be inhibited by affinity-purified Bap antibodies, demonstrating the direct contribution of Bap to biofilm growth by A. baumannii clinical isolates.

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“…Nowadays, numerous bioinformatics tools are used in the large variety of biological fields ranging from vaccinology to designing protein constructs, in order to decrease the costs and increase the accuracy of experimental researches (Ghasemi et al 2012;Nezafat et al 2014;Rahbar et al 2010;Sagemark et al 2010). Intracellular high-level expression of the recombinant hGH often leads to aggregation of misfolded protein (Soares et al 2003;Zamani et al 2014).…”

Section: Discussionmentioning

confidence: 99%

In Silico Evaluation of Different Signal Peptides for the Secretory Production of Human Growth Hormone in E. coli

Zamani

Nezafat

Negahdaripour

et al. 2015

Int J Pept Res Ther

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Various advantages of protein secretion have prompted scientists to search for secretory production of heterologous proteins. Signal peptides are one of the most important factors for prosperous secretion of the recombinant proteins. The aim of this study was to evaluate 23 different signal peptides and theoretically determine suitable ones for secretory production of the human growth hormone (hGH) in the E. coli host. The signal peptide sequences and the precise location of their cleavage sites were predicted using SignalP 4.0 server. Accordingly, six of the signal peptides, including hGH, major outer membrane lipoprotein, protease VII, protein TolB, periplasmic protein TorT and beta-lactamase TEM were excluded from the further study, due to their inappropriate cleavage scores. Different physico-chemical properties, which are essential for selecting a proper signal peptide, were evaluated using ProtParam and Solpro as the most accurate and reliable servers. Computational analysis of the abovementioned factors, indicates that outer membrane protein C, fimbrial chaperone SfmC, outer membrane protein F and disulfide interchange protein DsbA can theoretically be suitable signal peptides for hGH secretion.

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In silico analysis of antibody triggering biofilm associated protein in Acinetobacter baumannii

Cited by 48 publications

References 66 publications

The Acinetobacter baumannii Biofilm-Associated Protein Plays a Role in Adherence to Human Epithelial Cells

The Acinetobacter baumannii Biofilm-Associated Protein Plays a Role in Adherence to Human Epithelial Cells

Molecular Analysis of the Acinetobacter baumannii Biofilm-Associated Protein

In Silico Evaluation of Different Signal Peptides for the Secretory Production of Human Growth Hormone in E. coli

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